NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|386647928|gb|AFJ14794|]
View 

PlpE [Paenibacillus elgii]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
813-4611 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 3281.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  813 ISLPLRDvfRYPTVEKLAEAisGMGeqvYSSIPAAEAREYY---PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDR 889
Cdd:PRK12467   14 ITLPLEK--RRLYLEKMQEE--GVS---FANLPIPQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  890 NRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVeHIRANEEEADAAVKQFIRA---------FDLAKPPLLRV 960
Cdd:PRK12467   87 SALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTI-PLDDLANEQGRARESQIEAyineevarpFDLANGPLLRV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  961 GLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGE------DLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLE 1034
Cdd:PRK12467  166 RLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1035 VFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAG 1114
Cdd:PRK12467  246 QLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNAN 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1115 RTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNT- 1193
Cdd:PRK12467  326 RNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTa 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1194 ---ENKEF-RLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIA 1269
Cdd:PRK12467  406 tggRDREGaQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLG 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1270 SLGILTVEEKAQLVHVFNPAAPDAPENEVfHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQL 1349
Cdd:PRK12467  486 ELPLLDAEERARELVRWNAPATEYAPDCV-HQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVL 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1350 VGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLqeRAQQWGQTLQAVLCLDDEAA--- 1426
Cdd:PRK12467  565 VGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHL--LAQLPVPAGLRSLCLDEPADllc 642
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1427 -YAEDASNVANvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTL 1505
Cdd:PRK12467  643 gYSGHNPEVAL--DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD-SMLMVSTFAFDLGVTELFGAL 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1506 YNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLdmSSMELLITSSDSCSVtDYRVLQERFGS 1585
Cdd:PRK12467  720 ASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQV-DLLARVRALGP 796
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1586 QFRIINAYGVTEAAIDSSLYDEPLAKLPeAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELT 1665
Cdd:PRK12467  797 GARLINHYGPTETTVGVSTYELSDEERD-FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALT 875
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1666 EEKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvL 1744
Cdd:PRK12467  876 AERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQ-L 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1745 CAYFT-------AESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEA 1817
Cdd:PRK12467  955 VAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-AVQATFVAPQTELEK 1033
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1818 KLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEE 1897
Cdd:PRK12467 1034 RLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDR 1113
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1898 REYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAV 1977
Cdd:PRK12467 1114 DQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTL 1193
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1978 EHYRTSEAEAGEV-VRGFV-----RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGES-- 2049
Cdd:PRK12467 1194 EEPLLLAADKDEAqLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSqg 1273
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2050 ----LATLRIQYKDYAVWQ-QSEEQLERvKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKR 2124
Cdd:PRK12467 1274 qslqLPALPIQYADYAVWQrQWMDAGER-ARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRA 1352
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2125 VAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLG 2204
Cdd:PRK12467 1353 LARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALE 1432
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2205 AYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEEL-QLDGLKLAPYPSGNTIARFDLTLDVTETGSGLECNLE 2283
Cdd:PRK12467 1433 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLT 1512
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2284 YATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQTQLHHVFNATAADYEADKTIHQLFEEQAERIPDHPA 2363
Cdd:PRK12467 1513 YATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVA 1592
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2364 VVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSA 2443
Cdd:PRK12467 1593 LVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGI 1672
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2444 QVLLAQRRLQERVSFAGTV--VTVDDEQAY-AGDG-SNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFAN 2519
Cdd:PRK12467 1673 ELLLTQSHLQARLPLPDGLrsLVLDQEDDWlEGYSdSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQE 1752
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2520 TLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTY-AVYLNPD----H 2594
Cdd:PRK12467 1753 AYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMlQQLLQMDeqveH 1832
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2595 MPDFKRLIAAGSASSLELLQQWKDKVKY---FNAYGPTEDSICTTIWTPSTEDISQLKSVPIGGPIVNHRIYIVDAHYQP 2671
Cdd:PRK12467 1833 PLSLRRVVCGGEALEVEALRPWLERLPDtglFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNP 1912
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2672 VPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEI 2750
Cdd:PRK12467 1913 VPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2751 EEQLLKVASVQEAIVIAHDDASGqKQLCAYFV----------ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPN 2820
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQDGANG-KQLVAYVVptdpglvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPN 2071
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2821 GKIDRKALPAPQGNASAgADYVAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDL 2900
Cdd:PRK12467 2072 GKLDRKALPAPDASELQ-QAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDL 2150
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2901 FKYPTVAQLSKhirpVARM------ADQGEVSGDVSLTPIQHWFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLV 2974
Cdd:PRK12467 2151 FQHQTVQSLAA----VAQEgdgtvsIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALL 2226
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2975 EHHDALRVVFHKSENGYTAWNRAIGEGE---LYGLEVVDLkgieesaQAVEAKANEIQSSIDLEAGPFVKAGLFQCADGD 3051
Cdd:PRK12467 2227 VHHDALRLGFVQEDGGWSAMHRAPEQERrplLWQVVVADK-------EELEALCEQAQRSLDLEEGPLLRAVLATLPDGS 2299
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3052 H-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYRTWSEQLAAYAQSPVIERELAYWKRVAQTEVQPL 3130
Cdd:PRK12467 2300 QrLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTEL 2379
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3131 PKDEQvDVSLQQDSE-SISIEWTREETEQLLKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGRESIMTDID 3209
Cdd:PRK12467 2380 PCDHP-QGGLQRRHAaSVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEID 2458
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3210 ITRTVGWFTSKYPVvlELEQGKDISYLLKKTKEDLRGIPNKGIGYGICRYL--SAAKNDIAWGAEPEVSFNYLGQFDQDL 3287
Cdd:PRK12467 2459 LTRTVGWFTSLYPV--KLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLgsEAARQTLQALPVPRITFNYLGQFDGSF 2536
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3288 QNSDIGVSAHTGGKQSSDRQKRIFV---LDINGMIADGTLSLELSYNGKEYRRETMERLAASLQESLRVIIAHCVSKERA 3364
Cdd:PRK12467 2537 DAEKQALFVPSGEFSGAEQSEEAPLgnwLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQR 2616
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3365 ELTPSDVQFKGLSVEELEQISgqtQHLGDIENIYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGaLNIELFSRSWNEL 3444
Cdd:PRK12467 2617 GVTPSDFPLAGLSQEQLDRLP---VAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAV 2692
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3445 AARHAVLRTNFHS-GWRGEPLQIVYRYKPVEFAYEDLRHLAEAEWSayLDQLVNDDKTRGFDLEQDALMRVKVVRTQEES 3523
Cdd:PRK12467 2693 IDRHEILRSGFLWdGELEEPLQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADRQQGFDLLSAPLLRLTLVRTGEDR 2770
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3524 FHVLWSFHHILMDGWCLPLIAKELFDTYEAylrndlsERPAAPS--YSHYIEWLEKQDMEAAARYWTGFLAGYDSQTTLP 3601
Cdd:PRK12467 2771 HHLIYTNHHILMDGWSGSQLLGEVLQRYFG-------QPPPAREgrYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLA 2843
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3602 QG-KLHNKDGEYTEANILRSLGKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEM 3680
Cdd:PRK12467 2844 RAlYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQ 2923
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3681 IGLFINTIPVRVSCEAEQSFADVMKRVQEAALESGGYDYYPLYEIQAQSAQ-KQDLITHIMAFENFPMDEQIEQAGsyeD 3759
Cdd:PRK12467 2924 LGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGA---P 3000
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3760 GKLAITDVDIAEQTNYDFTLVVMPGEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAEI 3839
Cdd:PRK12467 3001 SGLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQV 3080
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3840 IHVFNNTAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVV 3919
Cdd:PRK12467 3081 LHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIV 3160
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3920 GIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFA--GTFVAVDDEQAYHADGSNLEPVVGPNHLA 3997
Cdd:PRK12467 3161 ALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPagDTALTLDRLDLNGYSENNPSTRVMGENLA 3240
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3998 YVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIpTSTTILDYPLF 4077
Cdd:PRK12467 3241 YVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDPEEL 3319
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4078 ESYMNENGITATILPPTY----AAYLNPDRMPSLKKLITGGSAASVEFVQQWKDK---VLYFNAYGPTEASIVTSIWDEA 4150
Cdd:PRK12467 3320 WQAIHAHRISIACFPPAYlqqfAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKlkpRGLTNGYGPTEAVVTVTLWKCG 3399
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4151 SDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFE-PGERMYRTGDLV 4229
Cdd:PRK12467 3400 GDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLA 3479
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4230 RWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGqQQLVAYFVAQRELTA--AELRATMSQ 4307
Cdd:PRK12467 3480 RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQGDwrETLRDHLAA 3558
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4308 ELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPEGSMHagGEYVAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELGGHS 4387
Cdd:PRK12467 3559 SLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS--REYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDS 3636
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4388 LRATALASKVRKELNMELPLRHIFQFPTVEQLAeaigqleqqefdaipvveereyypvssaqkrlyilqqlegaaqSYNM 4467
Cdd:PRK12467 3637 LLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA-------------------------------------------GYSP 3673
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4468 PGVMGLEGALDRERFEETFRKLIARHETLRTGFeliDGEPVQRIYPEvdfavetvqaseqeakaivrdfirpfdlakppl 4547
Cdd:PRK12467 3674 LGDVPVNLLLDLNRLETGFPALFCRHEGLGTVF---DYEPLAVILEG--------------------------------- 3717
                        3850      3860      3870      3880      3890      3900
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4548 lrvglielapERCILMLDMHHIVSDGvsadvlveefarlYSGEELPGLRIQYKDYAVWQQSEAQ 4611
Cdd:PRK12467 3718 ----------DRHVLGLTCRHLLDDG-------------WQDTSLQAMAVQYADYILWQQAKGP 3758
PRK12467 super family cl36129
peptide synthase; Provisional
4403-8198 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 3278.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4403 MELPLRHIFQFptVEQLAEaigqlEQQEFDAIPVVEEREYY---PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDR 4479
Cdd:PRK12467   14 ITLPLEKRRLY--LEKMQE-----EGVSFANLPIPQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4480 ERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAVETV---QASEQEAKAIVRDFI-----RPFDLAKPPLLRVG 4551
Cdd:PRK12467   87 SALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDdlaNEQGRARESQIEAYIneevaRPFDLANGPLLRVR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4552 LIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGE------ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEA 4625
Cdd:PRK12467  167 LLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4626 FRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGR 4705
Cdd:PRK12467  247 LGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4706 THADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNT-- 4783
Cdd:PRK12467  327 NRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTat 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4784 --ENKEM-HLPGLHLTPYPTEYGMSKFDLSLDMMEDSEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIAS 4860
Cdd:PRK12467  407 ggRDREGaQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGE 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4861 LGILTADEKAQIVHVFNPAAPDAPeNEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLV 4940
Cdd:PRK12467  487 LPLLDAEERARELVRWNAPATEYA-PDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLV 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4941 GILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLqeRAQQWGQTLQAALCLDDEAA---- 5016
Cdd:PRK12467  566 GIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHL--LAQLPVPAGLRSLCLDEPADllcg 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5017 YAEDASNVANvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTLY 5096
Cdd:PRK12467  644 YSGHNPEVAL--DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD-SMLMVSTFAFDLGVTELFGALA 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5097 NGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLdmSSMVLLITSSDSCSVtDYRVLQERFGSQ 5176
Cdd:PRK12467  721 SGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQV-DLLARVRALGPG 797
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5177 FRIINAYGVTEAAIDSSLYDEPLAKLPeAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTE 5256
Cdd:PRK12467  798 ARLINHYGPTETTVGVSTYELSDEERD-FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTA 876
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5257 EKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvLC 5335
Cdd:PRK12467  877 ERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQ-LV 955
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5336 AHFT-------AESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEAK 5408
Cdd:PRK12467  956 AYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-AVQATFVAPQTELEKR 1034
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5409 LVSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEER 5488
Cdd:PRK12467 1035 LAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRD 1114
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5489 EYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVE 5568
Cdd:PRK12467 1115 QPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLE 1194
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5569 HYRTSEAEAGEV-VRGFV-----RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGES--- 5639
Cdd:PRK12467 1195 EPLLLAADKDEAqLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSqgq 1274
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5640 ---LAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIA 5716
Cdd:PRK12467 1275 slqLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALA 1354
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5717 AESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAY 5796
Cdd:PRK12467 1355 RREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQ 1434
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5797 EHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNK-ETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSEGLELSMEYS 5875
Cdd:PRK12467 1435 AHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDdHQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYA 1514
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5876 TALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEKEHIQRVFNATEAKYPSDKTIHQLFEEQAERIPDHLAVT 5955
Cdd:PRK12467 1515 TDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALV 1594
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5956 FEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKL 6035
Cdd:PRK12467 1595 FGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIEL 1674
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6036 LLVQGHLLDRASFADKL--VNLNDDGAYHE--DGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNT-NYV 6110
Cdd:PRK12467 1675 LLTQSHLQARLPLPDGLrsLVLDQEDDWLEgySDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATqEAY 1754
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6111 ELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDsGMFAG- 6189
Cdd:PRK12467 1755 QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHp 1833
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6190 --LKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENT---TFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLL 6264
Cdd:PRK12467 1834 lsLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdvTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPV 1913
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6265 PVGVWGELIVGGDGVARGYLNRPELTAEKFVESSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIE 6343
Cdd:PRK12467 1914 PIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6344 EQLLKVASVKEATVIVREDESGqKQLCAYFV---------AERELTI-GELRAALSQELPNYMIPSHFVPLERMPLTPNG 6413
Cdd:PRK12467 1994 ARLREQGGVREAVVIAQDGANG-KQLVAYVVptdpglvddDEAQVALrAILKNHLKASLPEYMVPAHLVFLARMPLTPNG 2072
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6414 KIDRRALPAPQGNAPVGAeYVAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLF 6493
Cdd:PRK12467 2073 KLDRKALPAPDASELQQA-YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLF 2151
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6494 KYPTLAQLSQhiqpVARM------IDQGEVTGEIGLTPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAE 6567
Cdd:PRK12467 2152 QHQTVQSLAA----VAQEgdgtvsIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLV 2227
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6568 HHDALRTVFRKSENGYAAWNRAIGEGE---LYSLEVADfrdvksaEQAVEAKANEIQSSIDLEVGPLFKAGLFQCADGDH 6644
Cdd:PRK12467 2228 HHDALRLGFVQEDGGWSAMHRAPEQERrplLWQVVVAD-------KEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQ 2300
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6645 -LLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEEVRLPAKTDSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAPLP 6723
Cdd:PRK12467 2301 rLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELP 2380
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6724 KDKQSDRSLQQDSESITIQWSRKETEQLLKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDIT 6803
Cdd:PRK12467 2381 CDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLT 2460
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6804 RTVGWFTSKYPVLLQmePGRSLSTRIKKVKEDLRRIPNKGIGYGLCRYLSAQPDGTVWGA--EPEISFNYLGQFDQDLSN 6881
Cdd:PRK12467 2461 RTVGWFTSLYPVKLS--PTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQAlpVPRITFNYLGQFDGSFDA 2538
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6882 NDIGL---SPYSSGLEMSDRQARSFILDINGMITDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAHCAAKEWTEL 6958
Cdd:PRK12467 2539 EKQALfvpSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGV 2618
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6959 TPSDVQLKGLTVEELEQISAQtrnVGEIENIYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGsLDAEQFARSWNDLVA 7038
Cdd:PRK12467 2619 TPSDFPLAGLSQEQLDRLPVA---VGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVID 2694
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7039 RHAILRTNFFS-GPRGEPLQIVYRDKRIGFVYEDLSHLPadERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYR 7117
Cdd:PRK12467 2695 RHEILRSGFLWdGELEEPLQVVYKQARLPFSRLDWRDRA--DLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHH 2772
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7118 VLWSFHHILMDGWCLPLVVKELFETYeayvqGDRPEQKAAPAYSQYIEWLENQDSAAASAYWSNYLAGYEGQTALPQEKA 7197
Cdd:PRK12467 2773 LIYTNHHILMDGWSGSQLLGEVLQRY-----FGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALY 2847
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7198 QKRSEGyVAEH--VVCELDKELSERMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGL 7275
Cdd:PRK12467 2848 PAPAEA-VAGHgaHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGL 2926
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7276 FINTIPVRVACQPEESFADVMGRMQEAALESGRYDFYPLYEIQTQSAQ-KQELINHLLVFENYPMDEQVEQAGgddSGTL 7354
Cdd:PRK12467 2927 FINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGA---PSGL 3003
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7355 SITDVDVAEHTNYNFTVTVFPGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHV 7434
Cdd:PRK12467 3004 RFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHA 3083
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7435 FNNTAAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAF 7514
Cdd:PRK12467 3084 WNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALL 3163
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7515 AIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQE--CVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVI 7592
Cdd:PRK12467 3164 AVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEqlPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVI 3243
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7593 YTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDtILDYPLFESY 7672
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDND-LWDPEELWQA 3322
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 MNENGITAAILPPTYAIYLSPD----RLPSLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDG 7745
Cdd:PRK12467 3323 IHAHRISIACFPPAYLQQFAEDaggaDCASLDIYVFGGEAVPPAAFEQVKRKlkpRGLTNGYGPTEAVVTVTLWKCGGDA 3402
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7746 LDLRS-VPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFL-AGERMYRTGDLARWL 7823
Cdd:PRK12467 3403 VCEAPyAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYR 3482
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7824 PDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARgDANGQQQLCAYFVADRELT--VSELRGTLSQELP 7901
Cdd:PRK12467 3483 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGdwRETLRDHLAASLP 3561
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7902 GYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSMQtgADFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRA 7981
Cdd:PRK12467 3562 DYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS--REYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLA 3639
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7982 TVLSSKVNKELNVNLPLRDIFRFPTVEALAQVIdGLEQEEHSaipvigereyyPVSSAQKRlfilhqlegaqqsynipgf 8061
Cdd:PRK12467 3640 LQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS-PLGDVPVN-----------LLLDLNRL------------------- 3688
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8062 atiegpldRDRFEAVFRqlieRHETLRTGFEmanGEPVQRVysdvefaveyskadreeaveiaqrfvrpfdlrkppllrv 8141
Cdd:PRK12467 3689 --------ETGFPALFC----RHEGLGTVFD---YEPLAVI--------------------------------------- 3714
                        3850      3860      3870      3880      3890
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 8142 glieVEPERHILMLDMHHIISDGASVgilqeefsrlyagEELPPLRIQYKDYAAWQR 8198
Cdd:PRK12467 3715 ----LEGDRHVLGLTCRHLLDDGWQD-------------TSLQAMAVQYADYILWQQ 3754
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
5-1098 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 874.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    5 AFERETAFWNKIFEGEENPPTALPYSKAQKQAPALVRRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSS 84
Cdd:COG1020   203 ELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQ 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   85 SSILVGMPVVtkpneNRRP----------VNQLViLREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYA 154
Cdd:COG1020   283 DDVVVGTPVA-----GRPRpeleglvgffVNTLP-LRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERD 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  155 DG-VPVVNTLVA----------LKQLHITDY---RQSAVSDVLFEFELDKDEVRLHLTYNGNLYTESFIAQAVDHLNRLF 220
Cdd:COG1020   357 LSrNPLFQVMFVlqnapadeleLPGLTLEPLeldSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLL 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  221 SVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLAR 300
Cdd:COG1020   437 EALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAH 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  301 TLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERV-SFSGTWIR 379
Cdd:COG1020   517 HLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLpELGVPVLA 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  380 LDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN-YIDVTGQDKLLQLSSYSFDGSTFDI 458
Cdd:COG1020   597 LDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQrRYGLGPGDRVLQFASLSFDASVWEI 676
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  459 FGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRHARAILFGGERVSVSHVRKALGHLG 538
Cdd:COG1020   677 FGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLP 756
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  539 PGKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTA 618
Cdd:COG1020   757 GARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTA 836
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  619 EKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLC 697
Cdd:COG1020   837 ERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLV 916
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  698 AYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGVEFVEPRTELEAGIVNIWKE 777
Cdd:COG1020   917 AYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALL 996
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  778 ILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISGMGEQVYSSIPAAEAREYYPLSS 857
Cdd:COG1020   997 LLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLL 1076
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  858 AQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFA------VEH 931
Cdd:COG1020  1077 LSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAAlalaalLAL 1156
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IRANEEEADAAVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY------GGEDLPAL 1005
Cdd:COG1020  1157 LLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLllaaaaAALLALAL 1236
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1006 RIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATL 1085
Cdd:COG1020  1237 LLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLL 1316
                        1130
                  ....*....|...
gi 386647928 1086 YMVLLAAYTILLQ 1098
Cdd:COG1020  1317 LLLLLALLLLALL 1329
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
8033-8446 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


:

Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 580.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8033 YYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY 8112
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 ------SKADREEAVE--IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGE--- 8181
Cdd:cd19531    81 vdlsglPEAEREAEAQrlAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8182 ---ELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNEL 8258
Cdd:cd19531   161 rpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8259 AARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGA 8338
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8339 FEHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDqTVAAQFDLTLSVAEDDGAIRGSFQY 8418
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVD-SGTAKFDLTLSLTETDGGLRGSLEY 399
                         410       420
                  ....*....|....*....|....*...
gi 386647928 8419 AAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19531   400 NTDLFDAATIERMAGHFQTLLEAIVADP 427
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
813-4611 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 3281.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  813 ISLPLRDvfRYPTVEKLAEAisGMGeqvYSSIPAAEAREYY---PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDR 889
Cdd:PRK12467   14 ITLPLEK--RRLYLEKMQEE--GVS---FANLPIPQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  890 NRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVeHIRANEEEADAAVKQFIRA---------FDLAKPPLLRV 960
Cdd:PRK12467   87 SALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTI-PLDDLANEQGRARESQIEAyineevarpFDLANGPLLRV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  961 GLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGE------DLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLE 1034
Cdd:PRK12467  166 RLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1035 VFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAG 1114
Cdd:PRK12467  246 QLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNAN 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1115 RTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNT- 1193
Cdd:PRK12467  326 RNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTa 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1194 ---ENKEF-RLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIA 1269
Cdd:PRK12467  406 tggRDREGaQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLG 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1270 SLGILTVEEKAQLVHVFNPAAPDAPENEVfHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQL 1349
Cdd:PRK12467  486 ELPLLDAEERARELVRWNAPATEYAPDCV-HQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVL 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1350 VGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLqeRAQQWGQTLQAVLCLDDEAA--- 1426
Cdd:PRK12467  565 VGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHL--LAQLPVPAGLRSLCLDEPADllc 642
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1427 -YAEDASNVANvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTL 1505
Cdd:PRK12467  643 gYSGHNPEVAL--DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD-SMLMVSTFAFDLGVTELFGAL 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1506 YNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLdmSSMELLITSSDSCSVtDYRVLQERFGS 1585
Cdd:PRK12467  720 ASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQV-DLLARVRALGP 796
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1586 QFRIINAYGVTEAAIDSSLYDEPLAKLPeAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELT 1665
Cdd:PRK12467  797 GARLINHYGPTETTVGVSTYELSDEERD-FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALT 875
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1666 EEKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvL 1744
Cdd:PRK12467  876 AERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQ-L 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1745 CAYFT-------AESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEA 1817
Cdd:PRK12467  955 VAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-AVQATFVAPQTELEK 1033
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1818 KLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEE 1897
Cdd:PRK12467 1034 RLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDR 1113
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1898 REYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAV 1977
Cdd:PRK12467 1114 DQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTL 1193
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1978 EHYRTSEAEAGEV-VRGFV-----RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGES-- 2049
Cdd:PRK12467 1194 EEPLLLAADKDEAqLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSqg 1273
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2050 ----LATLRIQYKDYAVWQ-QSEEQLERvKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKR 2124
Cdd:PRK12467 1274 qslqLPALPIQYADYAVWQrQWMDAGER-ARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRA 1352
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2125 VAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLG 2204
Cdd:PRK12467 1353 LARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALE 1432
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2205 AYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEEL-QLDGLKLAPYPSGNTIARFDLTLDVTETGSGLECNLE 2283
Cdd:PRK12467 1433 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLT 1512
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2284 YATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQTQLHHVFNATAADYEADKTIHQLFEEQAERIPDHPA 2363
Cdd:PRK12467 1513 YATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVA 1592
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2364 VVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSA 2443
Cdd:PRK12467 1593 LVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGI 1672
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2444 QVLLAQRRLQERVSFAGTV--VTVDDEQAY-AGDG-SNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFAN 2519
Cdd:PRK12467 1673 ELLLTQSHLQARLPLPDGLrsLVLDQEDDWlEGYSdSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQE 1752
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2520 TLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTY-AVYLNPD----H 2594
Cdd:PRK12467 1753 AYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMlQQLLQMDeqveH 1832
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2595 MPDFKRLIAAGSASSLELLQQWKDKVKY---FNAYGPTEDSICTTIWTPSTEDISQLKSVPIGGPIVNHRIYIVDAHYQP 2671
Cdd:PRK12467 1833 PLSLRRVVCGGEALEVEALRPWLERLPDtglFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNP 1912
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2672 VPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEI 2750
Cdd:PRK12467 1913 VPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2751 EEQLLKVASVQEAIVIAHDDASGqKQLCAYFV----------ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPN 2820
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQDGANG-KQLVAYVVptdpglvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPN 2071
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2821 GKIDRKALPAPQGNASAgADYVAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDL 2900
Cdd:PRK12467 2072 GKLDRKALPAPDASELQ-QAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDL 2150
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2901 FKYPTVAQLSKhirpVARM------ADQGEVSGDVSLTPIQHWFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLV 2974
Cdd:PRK12467 2151 FQHQTVQSLAA----VAQEgdgtvsIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALL 2226
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2975 EHHDALRVVFHKSENGYTAWNRAIGEGE---LYGLEVVDLkgieesaQAVEAKANEIQSSIDLEAGPFVKAGLFQCADGD 3051
Cdd:PRK12467 2227 VHHDALRLGFVQEDGGWSAMHRAPEQERrplLWQVVVADK-------EELEALCEQAQRSLDLEEGPLLRAVLATLPDGS 2299
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3052 H-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYRTWSEQLAAYAQSPVIERELAYWKRVAQTEVQPL 3130
Cdd:PRK12467 2300 QrLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTEL 2379
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3131 PKDEQvDVSLQQDSE-SISIEWTREETEQLLKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGRESIMTDID 3209
Cdd:PRK12467 2380 PCDHP-QGGLQRRHAaSVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEID 2458
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3210 ITRTVGWFTSKYPVvlELEQGKDISYLLKKTKEDLRGIPNKGIGYGICRYL--SAAKNDIAWGAEPEVSFNYLGQFDQDL 3287
Cdd:PRK12467 2459 LTRTVGWFTSLYPV--KLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLgsEAARQTLQALPVPRITFNYLGQFDGSF 2536
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3288 QNSDIGVSAHTGGKQSSDRQKRIFV---LDINGMIADGTLSLELSYNGKEYRRETMERLAASLQESLRVIIAHCVSKERA 3364
Cdd:PRK12467 2537 DAEKQALFVPSGEFSGAEQSEEAPLgnwLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQR 2616
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3365 ELTPSDVQFKGLSVEELEQISgqtQHLGDIENIYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGaLNIELFSRSWNEL 3444
Cdd:PRK12467 2617 GVTPSDFPLAGLSQEQLDRLP---VAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAV 2692
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3445 AARHAVLRTNFHS-GWRGEPLQIVYRYKPVEFAYEDLRHLAEAEWSayLDQLVNDDKTRGFDLEQDALMRVKVVRTQEES 3523
Cdd:PRK12467 2693 IDRHEILRSGFLWdGELEEPLQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADRQQGFDLLSAPLLRLTLVRTGEDR 2770
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3524 FHVLWSFHHILMDGWCLPLIAKELFDTYEAylrndlsERPAAPS--YSHYIEWLEKQDMEAAARYWTGFLAGYDSQTTLP 3601
Cdd:PRK12467 2771 HHLIYTNHHILMDGWSGSQLLGEVLQRYFG-------QPPPAREgrYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLA 2843
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3602 QG-KLHNKDGEYTEANILRSLGKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEM 3680
Cdd:PRK12467 2844 RAlYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQ 2923
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3681 IGLFINTIPVRVSCEAEQSFADVMKRVQEAALESGGYDYYPLYEIQAQSAQ-KQDLITHIMAFENFPMDEQIEQAGsyeD 3759
Cdd:PRK12467 2924 LGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGA---P 3000
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3760 GKLAITDVDIAEQTNYDFTLVVMPGEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAEI 3839
Cdd:PRK12467 3001 SGLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQV 3080
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3840 IHVFNNTAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVV 3919
Cdd:PRK12467 3081 LHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIV 3160
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3920 GIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFA--GTFVAVDDEQAYHADGSNLEPVVGPNHLA 3997
Cdd:PRK12467 3161 ALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPagDTALTLDRLDLNGYSENNPSTRVMGENLA 3240
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3998 YVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIpTSTTILDYPLF 4077
Cdd:PRK12467 3241 YVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDPEEL 3319
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4078 ESYMNENGITATILPPTY----AAYLNPDRMPSLKKLITGGSAASVEFVQQWKDK---VLYFNAYGPTEASIVTSIWDEA 4150
Cdd:PRK12467 3320 WQAIHAHRISIACFPPAYlqqfAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKlkpRGLTNGYGPTEAVVTVTLWKCG 3399
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4151 SDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFE-PGERMYRTGDLV 4229
Cdd:PRK12467 3400 GDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLA 3479
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4230 RWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGqQQLVAYFVAQRELTA--AELRATMSQ 4307
Cdd:PRK12467 3480 RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQGDwrETLRDHLAA 3558
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4308 ELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPEGSMHagGEYVAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELGGHS 4387
Cdd:PRK12467 3559 SLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS--REYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDS 3636
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4388 LRATALASKVRKELNMELPLRHIFQFPTVEQLAeaigqleqqefdaipvveereyypvssaqkrlyilqqlegaaqSYNM 4467
Cdd:PRK12467 3637 LLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA-------------------------------------------GYSP 3673
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4468 PGVMGLEGALDRERFEETFRKLIARHETLRTGFeliDGEPVQRIYPEvdfavetvqaseqeakaivrdfirpfdlakppl 4547
Cdd:PRK12467 3674 LGDVPVNLLLDLNRLETGFPALFCRHEGLGTVF---DYEPLAVILEG--------------------------------- 3717
                        3850      3860      3870      3880      3890      3900
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4548 lrvglielapERCILMLDMHHIVSDGvsadvlveefarlYSGEELPGLRIQYKDYAVWQQSEAQ 4611
Cdd:PRK12467 3718 ----------DRHVLGLTCRHLLDDG-------------WQDTSLQAMAVQYADYILWQQAKGP 3758
PRK12467 PRK12467
peptide synthase; Provisional
4403-8198 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 3278.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4403 MELPLRHIFQFptVEQLAEaigqlEQQEFDAIPVVEEREYY---PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDR 4479
Cdd:PRK12467   14 ITLPLEKRRLY--LEKMQE-----EGVSFANLPIPQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4480 ERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAVETV---QASEQEAKAIVRDFI-----RPFDLAKPPLLRVG 4551
Cdd:PRK12467   87 SALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDdlaNEQGRARESQIEAYIneevaRPFDLANGPLLRVR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4552 LIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGE------ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEA 4625
Cdd:PRK12467  167 LLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4626 FRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGR 4705
Cdd:PRK12467  247 LGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4706 THADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNT-- 4783
Cdd:PRK12467  327 NRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTat 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4784 --ENKEM-HLPGLHLTPYPTEYGMSKFDLSLDMMEDSEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIAS 4860
Cdd:PRK12467  407 ggRDREGaQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGE 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4861 LGILTADEKAQIVHVFNPAAPDAPeNEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLV 4940
Cdd:PRK12467  487 LPLLDAEERARELVRWNAPATEYA-PDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLV 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4941 GILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLqeRAQQWGQTLQAALCLDDEAA---- 5016
Cdd:PRK12467  566 GIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHL--LAQLPVPAGLRSLCLDEPADllcg 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5017 YAEDASNVANvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTLY 5096
Cdd:PRK12467  644 YSGHNPEVAL--DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD-SMLMVSTFAFDLGVTELFGALA 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5097 NGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLdmSSMVLLITSSDSCSVtDYRVLQERFGSQ 5176
Cdd:PRK12467  721 SGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQV-DLLARVRALGPG 797
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5177 FRIINAYGVTEAAIDSSLYDEPLAKLPeAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTE 5256
Cdd:PRK12467  798 ARLINHYGPTETTVGVSTYELSDEERD-FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTA 876
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5257 EKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvLC 5335
Cdd:PRK12467  877 ERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQ-LV 955
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5336 AHFT-------AESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEAK 5408
Cdd:PRK12467  956 AYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-AVQATFVAPQTELEKR 1034
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5409 LVSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEER 5488
Cdd:PRK12467 1035 LAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRD 1114
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5489 EYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVE 5568
Cdd:PRK12467 1115 QPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLE 1194
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5569 HYRTSEAEAGEV-VRGFV-----RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGES--- 5639
Cdd:PRK12467 1195 EPLLLAADKDEAqLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSqgq 1274
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5640 ---LAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIA 5716
Cdd:PRK12467 1275 slqLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALA 1354
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5717 AESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAY 5796
Cdd:PRK12467 1355 RREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQ 1434
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5797 EHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNK-ETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSEGLELSMEYS 5875
Cdd:PRK12467 1435 AHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDdHQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYA 1514
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5876 TALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEKEHIQRVFNATEAKYPSDKTIHQLFEEQAERIPDHLAVT 5955
Cdd:PRK12467 1515 TDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALV 1594
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5956 FEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKL 6035
Cdd:PRK12467 1595 FGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIEL 1674
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6036 LLVQGHLLDRASFADKL--VNLNDDGAYHE--DGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNT-NYV 6110
Cdd:PRK12467 1675 LLTQSHLQARLPLPDGLrsLVLDQEDDWLEgySDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATqEAY 1754
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6111 ELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDsGMFAG- 6189
Cdd:PRK12467 1755 QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHp 1833
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6190 --LKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENT---TFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLL 6264
Cdd:PRK12467 1834 lsLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdvTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPV 1913
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6265 PVGVWGELIVGGDGVARGYLNRPELTAEKFVESSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIE 6343
Cdd:PRK12467 1914 PIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6344 EQLLKVASVKEATVIVREDESGqKQLCAYFV---------AERELTI-GELRAALSQELPNYMIPSHFVPLERMPLTPNG 6413
Cdd:PRK12467 1994 ARLREQGGVREAVVIAQDGANG-KQLVAYVVptdpglvddDEAQVALrAILKNHLKASLPEYMVPAHLVFLARMPLTPNG 2072
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6414 KIDRRALPAPQGNAPVGAeYVAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLF 6493
Cdd:PRK12467 2073 KLDRKALPAPDASELQQA-YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLF 2151
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6494 KYPTLAQLSQhiqpVARM------IDQGEVTGEIGLTPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAE 6567
Cdd:PRK12467 2152 QHQTVQSLAA----VAQEgdgtvsIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLV 2227
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6568 HHDALRTVFRKSENGYAAWNRAIGEGE---LYSLEVADfrdvksaEQAVEAKANEIQSSIDLEVGPLFKAGLFQCADGDH 6644
Cdd:PRK12467 2228 HHDALRLGFVQEDGGWSAMHRAPEQERrplLWQVVVAD-------KEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQ 2300
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6645 -LLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEEVRLPAKTDSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAPLP 6723
Cdd:PRK12467 2301 rLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELP 2380
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6724 KDKQSDRSLQQDSESITIQWSRKETEQLLKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDIT 6803
Cdd:PRK12467 2381 CDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLT 2460
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6804 RTVGWFTSKYPVLLQmePGRSLSTRIKKVKEDLRRIPNKGIGYGLCRYLSAQPDGTVWGA--EPEISFNYLGQFDQDLSN 6881
Cdd:PRK12467 2461 RTVGWFTSLYPVKLS--PTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQAlpVPRITFNYLGQFDGSFDA 2538
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6882 NDIGL---SPYSSGLEMSDRQARSFILDINGMITDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAHCAAKEWTEL 6958
Cdd:PRK12467 2539 EKQALfvpSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGV 2618
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6959 TPSDVQLKGLTVEELEQISAQtrnVGEIENIYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGsLDAEQFARSWNDLVA 7038
Cdd:PRK12467 2619 TPSDFPLAGLSQEQLDRLPVA---VGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVID 2694
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7039 RHAILRTNFFS-GPRGEPLQIVYRDKRIGFVYEDLSHLPadERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYR 7117
Cdd:PRK12467 2695 RHEILRSGFLWdGELEEPLQVVYKQARLPFSRLDWRDRA--DLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHH 2772
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7118 VLWSFHHILMDGWCLPLVVKELFETYeayvqGDRPEQKAAPAYSQYIEWLENQDSAAASAYWSNYLAGYEGQTALPQEKA 7197
Cdd:PRK12467 2773 LIYTNHHILMDGWSGSQLLGEVLQRY-----FGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALY 2847
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7198 QKRSEGyVAEH--VVCELDKELSERMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGL 7275
Cdd:PRK12467 2848 PAPAEA-VAGHgaHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGL 2926
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7276 FINTIPVRVACQPEESFADVMGRMQEAALESGRYDFYPLYEIQTQSAQ-KQELINHLLVFENYPMDEQVEQAGgddSGTL 7354
Cdd:PRK12467 2927 FINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGA---PSGL 3003
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7355 SITDVDVAEHTNYNFTVTVFPGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHV 7434
Cdd:PRK12467 3004 RFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHA 3083
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7435 FNNTAAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAF 7514
Cdd:PRK12467 3084 WNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALL 3163
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7515 AIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQE--CVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVI 7592
Cdd:PRK12467 3164 AVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEqlPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVI 3243
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7593 YTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDtILDYPLFESY 7672
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDND-LWDPEELWQA 3322
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 MNENGITAAILPPTYAIYLSPD----RLPSLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDG 7745
Cdd:PRK12467 3323 IHAHRISIACFPPAYLQQFAEDaggaDCASLDIYVFGGEAVPPAAFEQVKRKlkpRGLTNGYGPTEAVVTVTLWKCGGDA 3402
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7746 LDLRS-VPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFL-AGERMYRTGDLARWL 7823
Cdd:PRK12467 3403 VCEAPyAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYR 3482
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7824 PDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARgDANGQQQLCAYFVADRELT--VSELRGTLSQELP 7901
Cdd:PRK12467 3483 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGdwRETLRDHLAASLP 3561
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7902 GYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSMQtgADFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRA 7981
Cdd:PRK12467 3562 DYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS--REYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLA 3639
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7982 TVLSSKVNKELNVNLPLRDIFRFPTVEALAQVIdGLEQEEHSaipvigereyyPVSSAQKRlfilhqlegaqqsynipgf 8061
Cdd:PRK12467 3640 LQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS-PLGDVPVN-----------LLLDLNRL------------------- 3688
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8062 atiegpldRDRFEAVFRqlieRHETLRTGFEmanGEPVQRVysdvefaveyskadreeaveiaqrfvrpfdlrkppllrv 8141
Cdd:PRK12467 3689 --------ETGFPALFC----RHEGLGTVFD---YEPLAVI--------------------------------------- 3714
                        3850      3860      3870      3880      3890
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 8142 glieVEPERHILMLDMHHIISDGASVgilqeefsrlyagEELPPLRIQYKDYAAWQR 8198
Cdd:PRK12467 3715 ----LEGDRHVLGLTCRHLLDDGWQD-------------TSLQAMAVQYADYILWQQ 3754
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1891-3183 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1169.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1891 SIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVY 1970
Cdd:COG1020     8 ALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1971 KEVNFAVEHYRTS--------EAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFG 2042
Cdd:COG1020    88 PVVAAPLPVVVLLvdlealaeAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2043 RLYN------GESLATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDA 2116
Cdd:COG1020   168 RLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2117 GLNEALKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLE 2196
Cdd:COG1020   248 ELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2197 EVKETTLGAYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEELQLDGLKLAPYPSGNTIARFDLTLDVTETGS 2276
Cdd:COG1020   328 RVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2277 GLECNLEYATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQTQLHHVFNATAADYEADKTIHQLFEEQAE 2356
Cdd:COG1020   408 GLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAA 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2357 RIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISY 2436
Cdd:COG1020   488 RTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY 567
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2437 MLEDSSAQVLLAQRRLQERV-SFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQ 2515
Cdd:COG1020   568 MLEDAGARLVLTQSALAARLpELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2516 MFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYA---VYLNP 2592
Cdd:COG1020   648 WMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLralLDAAP 727
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2593 DHMPDFKRLIAAGSASSLELLQQWKDK---VKYFNAYGPTEDSICTTIWTPSTEDISQlKSVPIGGPIVNHRIYIVDAHY 2669
Cdd:COG1020   728 EALPSLRLVLVGGEALPPELVRRWRARlpgARLVNLYGPTETTVDSTYYEVTPPDADG-GSVPIGRPIANTRVYVLDAHL 806
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2670 QPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELG 2748
Cdd:COG1020   807 QPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELG 886
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2749 EIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGE--LSGELPGYMIPAHFVQLERMPLTPNGKIDRK 2826
Cdd:COG1020   887 EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRlaLALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2827 ALPAPQgnASAGADYVAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTV 2906
Cdd:COG1020   967 ALPAPA--AAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAA 1044
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2907 AQLSKHIRPVARMADQGEVSGDVSLTPIQHWFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHK 2986
Cdd:COG1020  1045 AAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAA 1124
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2987 SENGYTAWNRAIGEGEL--YGLEVVDLKGIEESAQAVEAKANEIQSSIDLEAGPFVKAGLFQCADG----DHLLIVIHHG 3060
Cdd:COG1020  1125 LRARRAVRQEGPRLRLLvaLAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLllllLLLLLLLLLL 1204
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3061 VVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYRTWSEQLAAYAQSPVIERELAYWKRVAQTEVQPLPKDEQVDVSL 3140
Cdd:COG1020  1205 LLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALA 1284
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|...
gi 386647928 3141 QQDSESISIEWTREETEQLLKGVHRAYNTEMNDILLAALGMAV 3183
Cdd:COG1020  1285 RARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
5481-6775 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1157.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5481 SIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVY 5560
Cdd:COG1020     8 ALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5561 KEVNFAVEHYRTS--------EAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFG 5632
Cdd:COG1020    88 PVVAAPLPVVVLLvdlealaeAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5633 RMYN------GESLAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEP 5706
Cdd:COG1020   168 RLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5707 KLGEGLQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLD 5786
Cdd:COG1020   248 ELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5787 EVKETMLGAYEHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSE 5866
Cdd:COG1020   328 RVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5867 GLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEKEHIQRVFNATEAKYPSDKTIHQLFEEQAE 5946
Cdd:COG1020   408 GLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAA 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5947 RIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRY 6026
Cdd:COG1020   488 RTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY 567
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6027 MLEDSGAKLLLVQGHLLDR-ASFADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVK 6105
Cdd:COG1020   568 MLEDAGARLVLTQSALAARlPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6106 NTN-YVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDS 6184
Cdd:COG1020   648 WMQrRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP 727
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6185 GMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEA--VPIGKPINNSTAYIVDSKLS 6262
Cdd:COG1020   728 EALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsVPIGRPIANTRVYVLDAHLQ 807
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6263 LLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGE 6341
Cdd:COG1020   808 PVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGE 887
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTI--GELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRA 6419
Cdd:COG1020   888 IEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAaaALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6420 LPAPQgnAPVGAEYVAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTLA 6499
Cdd:COG1020   968 LPAPA--AAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAA 1045
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6500 QLSQHIQPVARMIDQGEVTGEIGLTPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKS 6579
Cdd:COG1020  1046 AAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAAL 1125
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6580 ENGYAAWNRAIGEGELYSLEVADFRDVKSAEQAVEAKANE--IQSSIDLEVGPLFKAGLFQCADGDHLLLVIHHGVVDGV 6657
Cdd:COG1020  1126 RARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAelLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLL 1205
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6658 SWRILLEDVALG----YEQAAKGEEVRLPAKTDSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAPLPKDKQSDRSLQ 6733
Cdd:COG1020  1206 LLLLLLLLLLLLllllLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALAR 1285
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|..
gi 386647928 6734 QDSESITIQWSRKETEQLLKKVHRAYNTEMNDILLTALGMAV 6775
Cdd:COG1020  1286 ARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
5-1098 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 874.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    5 AFERETAFWNKIFEGEENPPTALPYSKAQKQAPALVRRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSS 84
Cdd:COG1020   203 ELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQ 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   85 SSILVGMPVVtkpneNRRP----------VNQLViLREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYA 154
Cdd:COG1020   283 DDVVVGTPVA-----GRPRpeleglvgffVNTLP-LRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERD 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  155 DG-VPVVNTLVA----------LKQLHITDY---RQSAVSDVLFEFELDKDEVRLHLTYNGNLYTESFIAQAVDHLNRLF 220
Cdd:COG1020   357 LSrNPLFQVMFVlqnapadeleLPGLTLEPLeldSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLL 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  221 SVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLAR 300
Cdd:COG1020   437 EALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAH 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  301 TLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERV-SFSGTWIR 379
Cdd:COG1020   517 HLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLpELGVPVLA 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  380 LDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN-YIDVTGQDKLLQLSSYSFDGSTFDI 458
Cdd:COG1020   597 LDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQrRYGLGPGDRVLQFASLSFDASVWEI 676
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  459 FGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRHARAILFGGERVSVSHVRKALGHLG 538
Cdd:COG1020   677 FGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLP 756
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  539 PGKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTA 618
Cdd:COG1020   757 GARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTA 836
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  619 EKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLC 697
Cdd:COG1020   837 ERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLV 916
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  698 AYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGVEFVEPRTELEAGIVNIWKE 777
Cdd:COG1020   917 AYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALL 996
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  778 ILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISGMGEQVYSSIPAAEAREYYPLSS 857
Cdd:COG1020   997 LLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLL 1076
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  858 AQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFA------VEH 931
Cdd:COG1020  1077 LSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAAlalaalLAL 1156
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IRANEEEADAAVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY------GGEDLPAL 1005
Cdd:COG1020  1157 LLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLllaaaaAALLALAL 1236
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1006 RIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATL 1085
Cdd:COG1020  1237 LLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLL 1316
                        1130
                  ....*....|...
gi 386647928 1086 YMVLLAAYTILLQ 1098
Cdd:COG1020  1317 LLLLLALLLLALL 1329
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
7451-7932 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 755.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 7610
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7611 LCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAIY 7690
Cdd:cd17655   162 VVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7691 LSPDRL---PSLKKLITGGSAASVEFVQQWKDK----VRYFNAYGPTEASIVTSVWAASPDGLDLRSVPIGRPIANHQIF 7763
Cdd:cd17655   242 LDAADDsegLSLKHLIVGGEALSTELAKKIIELfgtnPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRIY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7764 IVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGY 7843
Cdd:cd17655   322 ILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7844 RIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:cd17655   402 RIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKV 481

                  ....*....
gi 386647928 7924 DRNALPAPE 7932
Cdd:cd17655   482 DRKALPEPD 490
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
264-747 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 743.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  264 RLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPE 343
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  344 YPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTwIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHR 423
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEV-AVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  424 NIIRVVKNTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNV 503
Cdd:cd12117   160 GVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  504 LVDMNPDCLRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAIYI 583
Cdd:cd12117   240 LADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANTRVYV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  584 VNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFR 663
Cdd:cd12117   320 LDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  664 IELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVD 743
Cdd:cd12117   400 IELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVD 479

                  ....
gi 386647928  744 RRAL 747
Cdd:cd12117   480 RRAL 483
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
3859-4341 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 740.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY 3938
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 PEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 4018
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4019 LCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAY 4098
Cdd:cd17655   162 VVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4099 LNPDRM---PSLKKLITGGSAASVEFVQQWKDK----VLYFNAYGPTEASIVTSIW--DEASDSLGdrkSVPIGRPLANH 4169
Cdd:cd17655   242 LDAADDsegLSLKHLIVGGEALSTELAKKIIELfgtnPTITNAYGPTETTVDASIYqyEPETDQQV---SVPIGKPLGNT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4170 RIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKI 4249
Cdd:cd17655   319 RIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKI 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4250 RGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPN 4329
Cdd:cd17655   399 RGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPN 478
                         490
                  ....*....|..
gi 386647928 4330 GKIDRKALPAPE 4341
Cdd:cd17655   479 GKVDRKALPEPD 490
PRK12316 PRK12316
peptide synthase; Provisional
7-1140 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 707.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    7 ERETAFWNKIFeGEENPPTALPYSKAQKQAPALV-RRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSSS 85
Cdd:PRK12316  237 ERQLEYWRAQL-GEEHPVLELPTDHPRPAVPSYRgSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQT 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   86 SILVGMPVVtkpNENRRPVNQLV-------ILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYA---- 154
Cdd:PRK12316  316 DIRVGVPIA---NRNRAEVEGLIgffvntqVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSlshs 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  155 -------DGVPVVNTLVALKQ---LHITDY-RQSAVSDvlFEFELDKDEV--RLH--LTYNGNLYTESFIAQAVDHLNRL 219
Cdd:PRK12316  393 plfqvmyNHQPLVADIEALDTvagLEFGQLeWKSRTTQ--FDLTLDTYEKggRLHaaLTYATDLFEARTVERMARHWQNL 470
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  220 FSVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLA 299
Cdd:PRK12316  471 LRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLA 550
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  300 RTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSG--TW 377
Cdd:PRK12316  551 HALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAgvQV 630
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  378 IRLDDEEAYHEDGS--NLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIrvvkntNYIDVTGQ-------DKLLQLSS 448
Cdd:PRK12316  631 LDLDRPAAWLEGYSeeNPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALS------NRLCWMQQayglgvgDTVLQKTP 704
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  449 YSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVM-FITTAFFNVLVDMNPDCLRHARAILFGGERVSV 527
Cdd:PRK12316  705 FSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLhFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPA 784
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  528 SHVRKALGHLGPGKIKHVYGPTESTVFATSYDVheVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLA 607
Cdd:PRK12316  785 DAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLA 862
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  608 RGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVvr 687
Cdd:PRK12316  863 RGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL-- 940
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  688 esANGEKQLCAYYVADRslPANEVRSTLSQ----ELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGvEFVEP 763
Cdd:PRK12316  941 --AVDGKQLVGYVVLES--EGGDWREALKAhlaaSLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ-GYVAP 1015
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  764 RTELEAGIVNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLhKELNISLPLRDVFRYPTVEKLAEAISGMGEQVYSS 843
Cdd:PRK12316 1016 RNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRA-RQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQ 1094
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  844 IPAAEAreyYPLSSAQKRLYilHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYP 923
Cdd:PRK12316 1095 GPASGE---VALAPVQRWFF--EQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAA 1169
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  924 EVEFAVEHIR--ANEEEADAAVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY--GG 999
Cdd:PRK12316 1170 PQAGEVLWQRqaASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYadLD 1249
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1000 EDLPALRIQYKDYAVWQQSEAQKEqlKRQEAYWLEVFRGELPvlEMPTDYARPAVQSYAGNALRFELDA-QKREGLQRIA 1078
Cdd:PRK12316 1250 ADLPARTSSYQAWARRLHEHAGAR--AEELDYWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAeRTRQLLQEAP 1325
                        1130      1140      1150      1160      1170      1180
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1079 SENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTH----GDLHPLIGMFVNTLAIRNYPAAD 1140
Cdd:PRK12316 1326 AAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDlfedIDLSRTVGWFTSLFPVRLTPAAD 1391
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
8033-8446 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 580.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8033 YYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY 8112
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 ------SKADREEAVE--IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGE--- 8181
Cdd:cd19531    81 vdlsglPEAEREAEAQrlAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8182 ---ELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNEL 8258
Cdd:cd19531   161 rpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8259 AARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGA 8338
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8339 FEHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDqTVAAQFDLTLSVAEDDGAIRGSFQY 8418
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVD-SGTAKFDLTLSLTETDGGLRGSLEY 399
                         410       420
                  ....*....|....*....|....*...
gi 386647928 8419 AAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19531   400 NTDLFDAATIERMAGHFQTLLEAIVADP 427
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3881-4274 5.46e-170

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 531.46  E-value: 5.46e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3881 TYGELNERANRLARTLRDA-GVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQR 3959
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3960 HLRERVSFAGTFVA--VDDEQAYHADGSNLEPV---VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTE 4034
Cdd:TIGR01733   81 ALASRLAGLVLPVIllDPLELAALDDAPAPPPPdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4035 QDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYM-NENGITATILPPTYAAYL---NPDRMPSLKKL 4110
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLaaaLPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4111 ITGGSAASVEFVQQWKDK---VLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAG 4187
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4188 ELCISGVGLARGYLNRPELTAEKFVDNPF--EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAK 4265
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 386647928  4266 IDAVQEAIV 4274
Cdd:TIGR01733  401 HPGVREAVV 409
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
287-684 4.70e-165

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 517.20  E-value: 4.70e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   287 TYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQG 365
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   366 HLQERVSFSGTWIRLDD--EEAYHEDGSNLESVN---GPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVV-KNTNYIDVTG 439
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDplELAALDDAPAPPPPDapsGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLaWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   440 QDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKL-AGLIEKQQISVMFITTAFFNVLVDMNPDCLRHARAI 518
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   519 LFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEE-GAVSIPIGGPISNTAIYIVNAQNKLQPIGVAG 597
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDApRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   598 ELCVAGDGLARGYLNRPDLTAEKFADNPFAP--GERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLK 675
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 386647928   676 LEAIEKATV 684
Cdd:TIGR01733  401 HPGVREAVV 409
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
7473-7865 5.00e-162

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 508.73  E-value: 5.00e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7473 TYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQR 7551
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7552 HLQECVSFDGKVIA--ADDEQAYGEDGSNLEPV---VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITE 7626
Cdd:TIGR01733   81 ALASRLAGLVLPVIllDPLELAALDDAPAPPPPdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7627 EDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYM-NENGITAAILPPTYA---IYLSPDRLPSLKKL 7702
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLallAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7703 ITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDGLDL-RSVPIGRPIANHQIFIVDSQNHMLPVGVAG 7778
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVDPDDAPReSPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7779 ELCISGAGLARGYLNRPELTAEKFVDNPFL--AGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLK 7856
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 386647928  7857 IASVQETIV 7865
Cdd:TIGR01733  401 HPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
853-1283 1.04e-148

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 472.59  E-value: 1.04e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   853 YPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEM-VGGEPMQRIYPEVEFAVEH 931
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   932 I---RANEEEADAAVKQFIRA-----FDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYG----G 999
Cdd:pfam00668   85 IdisDLSESEEEEAIEAFIQRdlqspFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQqllkG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1000 EDLPALRIQ-YKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIA 1078
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1079 SENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAF 1158
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1159 ERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNT-----ENKEFRLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFLCG 1233
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYlgqdsQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTIK 404
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 386647928  1234 IEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEEKAQLV 1283
Cdd:pfam00668  405 IDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
4443-4873 1.51e-143

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 457.57  E-value: 1.51e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4443 YPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFEL-IDGEPVQRIYPEVDFAVET 4521
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4522 VQASEQEAKA--------IVRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLY----SG 4589
Cdd:pfam00668   85 IDISDLSESEeeeaieafIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqqllKG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4590 EELPGLRIQ-YKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIA 4668
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4669 AESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAF 4748
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4749 EHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQN-------TENKEMHLPGLHLTPYPTEygMSKFDLSLDMMEDSEGLE 4821
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNylgqdsqEEEFQLSELDLSVSSVIEE--EAKYDLSLTASERGGGLT 402
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386647928  4822 CSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIASLGILTADEKAQIV 4873
Cdd:pfam00668  403 IKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
8034-8455 1.49e-134

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 431.76  E-value: 1.49e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8034 YPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEM-ANGEPVQRVYSDVEFAVEY 8112
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8113 ---SKADREEAVEIAQRFVR-----PFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYA----G 8180
Cdd:pfam00668   85 idiSDLSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQqllkG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8181 EELPPLRIQ-YKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELA 8259
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8260 ARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAF 8339
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8340 EHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTVA----AQFDLTLSVAEDDGAIRGS 8415
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSVieeeAKYDLSLTASERGGGLTIK 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 386647928  8416 FQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQL 8455
Cdd:pfam00668  405 IDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDL 444
AMP-binding pfam00501
AMP-binding enzyme;
266-660 6.06e-118

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 382.43  E-value: 6.06e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   266 FEEQAERRPDAVAV-TFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEY 344
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   345 PEERIRYMLEDSGTQVLLSQGHLQ--------ERVSFSGTWIRLDDEEAYHEDGSNLESV-----------NGPEHLTYV 405
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleellealGKLEVVKLVLVLDRDPVLKEEPLPEEAKpadvpppppppPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   406 IYTSGTTGKPKGNLTTHRNIIRVVKNTNYID-----VTGQDKLLQLSSYSFDGS-TFDIFGALLNGAKLVLVPKETVLDV 479
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfgLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   480 AKLAGLIEKQQISVMFITTAFFNVLVDM---NPDCLRHARAILFGGERVSVSHVRKALGHLGPGkIKHVYGPTESTVFAT 556
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAgapKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   557 sYDVHEVEEGAVSIPIGGPISNTAIYIVNAQ-NKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADnpfapgERMYRT 635
Cdd:pfam00501  320 -TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 386647928   636 GDLARWLPDGTIEYVGRIDDQVKIR 660
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
8017-8455 2.20e-109

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 385.36  E-value: 2.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8017 LEQEEHSAIPVIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANG 8096
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8097 EPVQRVYSDVEFAVEY--------SKADREEAVEIAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVG 8168
Cdd:COG1020    81 RPVQVIQPVVAAPLPVvvllvdleALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8169 ILQEEFSRLY------AGEELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAE 8242
Cdd:COG1020   161 LLLAELLRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8243 LEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDK 8322
Cdd:COG1020   241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8323 TFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTvAAQFDLT 8402
Cdd:COG1020   321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSG-TAKFDLT 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 8403 LSVAEDDGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQL 8455
Cdd:COG1020   400 LTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPL 452
PRK12467 PRK12467
peptide synthase; Provisional
7992-8455 1.14e-93

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 344.45  E-value: 1.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7992 LNVNLPLRDIFRFPT--VEALAQVIDGLEQEEHS----AIP-VIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATI 8064
Cdd:PRK12467    1 MDNNVALRIARRFITlpLEKRRLYLEKMQEEGVSfanlPIPqVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8065 EGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY------SKADREEAVE--IAQRFVRPFDLRKP 8136
Cdd:PRK12467   81 RGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLddlaneQGRARESQIEayINEEVARPFDLANG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8137 PLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGE------ELPPLRIQYKDYAAWQRSEAYAKRVKQQE 8210
Cdd:PRK12467  161 PLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8211 GYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVG 8290
Cdd:PRK12467  241 AYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8291 TPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNPVFDTMFV 8370
Cdd:PRK12467  321 VPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8371 LQNTEDRGIEADAFSLTPFVFD----QTVAAQFDLTLSVAEDDGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:PRK12467  401 HQNTATGGRDREGAQLPGLTVEelswARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEP 480

                  ....*....
gi 386647928 8447 DIRLSQIQL 8455
Cdd:PRK12467  481 RRRLGELPL 489
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
8213-8466 6.48e-12

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 73.56  E-value: 6.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8213 WLQTLAGeLPVIELPTDYERTSTRSFEGAELEFEADEAltqrlnELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTp 8292
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8293 vagRTHADVEPIIgmfvntlaIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNPV-FDTMFVl 8371
Cdd:TIGR03443   74 ---SSNKSGRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPlFRLAFQ- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8372 qntedrgiEADAFSLTPFVFDQTVaaqfDLTLSVAEDDGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLS 8451
Cdd:TIGR03443  142 --------DAPDNQQTTYSTGSTT----DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIG 209
                          250
                   ....*....|....*
gi 386647928  8452 QIQLNEPenDSNDSL 8466
Cdd:TIGR03443  210 KVSLITP--SQKSLL 222
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2837-2914 7.96e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 53.41  E-value: 7.96e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   2837 AGADYVAPRSEEEKVLADVWQAVLG---AERVGATDHFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTVAQLSKH 2912
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGhaaAEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEH 81

                    ..
gi 386647928   2913 IR 2914
Cdd:smart00823   82 LA 83
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
6435-6505 9.30e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 53.02  E-value: 9.30e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928   6435 APRTEQEKALAAVWQ----AVLG---AERVGVTDHFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTLAQLSQHI 6505
Cdd:smart00823    4 LPPAERRRLLLDLVReqvaAVLGhaaAEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHL 82
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
762-835 2.78e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 51.87  E-value: 2.78e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928    762 EPRTELEAGIVNIWKEILKI---EKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISG 835
Cdd:smart00823    8 ERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
813-4611 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 3281.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  813 ISLPLRDvfRYPTVEKLAEAisGMGeqvYSSIPAAEAREYY---PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDR 889
Cdd:PRK12467   14 ITLPLEK--RRLYLEKMQEE--GVS---FANLPIPQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  890 NRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVeHIRANEEEADAAVKQFIRA---------FDLAKPPLLRV 960
Cdd:PRK12467   87 SALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTI-PLDDLANEQGRARESQIEAyineevarpFDLANGPLLRV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  961 GLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGE------DLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLE 1034
Cdd:PRK12467  166 RLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1035 VFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAG 1114
Cdd:PRK12467  246 QLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNAN 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1115 RTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNT- 1193
Cdd:PRK12467  326 RNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTa 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1194 ---ENKEF-RLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIA 1269
Cdd:PRK12467  406 tggRDREGaQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLG 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1270 SLGILTVEEKAQLVHVFNPAAPDAPENEVfHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQL 1349
Cdd:PRK12467  486 ELPLLDAEERARELVRWNAPATEYAPDCV-HQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVL 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1350 VGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLqeRAQQWGQTLQAVLCLDDEAA--- 1426
Cdd:PRK12467  565 VGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHL--LAQLPVPAGLRSLCLDEPADllc 642
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1427 -YAEDASNVANvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTL 1505
Cdd:PRK12467  643 gYSGHNPEVAL--DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD-SMLMVSTFAFDLGVTELFGAL 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1506 YNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLdmSSMELLITSSDSCSVtDYRVLQERFGS 1585
Cdd:PRK12467  720 ASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQV-DLLARVRALGP 796
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1586 QFRIINAYGVTEAAIDSSLYDEPLAKLPeAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELT 1665
Cdd:PRK12467  797 GARLINHYGPTETTVGVSTYELSDEERD-FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALT 875
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1666 EEKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvL 1744
Cdd:PRK12467  876 AERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQ-L 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1745 CAYFT-------AESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEA 1817
Cdd:PRK12467  955 VAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-AVQATFVAPQTELEK 1033
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1818 KLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEE 1897
Cdd:PRK12467 1034 RLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDR 1113
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1898 REYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAV 1977
Cdd:PRK12467 1114 DQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTL 1193
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1978 EHYRTSEAEAGEV-VRGFV-----RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGES-- 2049
Cdd:PRK12467 1194 EEPLLLAADKDEAqLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSqg 1273
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2050 ----LATLRIQYKDYAVWQ-QSEEQLERvKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKR 2124
Cdd:PRK12467 1274 qslqLPALPIQYADYAVWQrQWMDAGER-ARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRA 1352
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2125 VAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLG 2204
Cdd:PRK12467 1353 LARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALE 1432
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2205 AYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEEL-QLDGLKLAPYPSGNTIARFDLTLDVTETGSGLECNLE 2283
Cdd:PRK12467 1433 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLT 1512
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2284 YATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQTQLHHVFNATAADYEADKTIHQLFEEQAERIPDHPA 2363
Cdd:PRK12467 1513 YATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVA 1592
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2364 VVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSA 2443
Cdd:PRK12467 1593 LVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGI 1672
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2444 QVLLAQRRLQERVSFAGTV--VTVDDEQAY-AGDG-SNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFAN 2519
Cdd:PRK12467 1673 ELLLTQSHLQARLPLPDGLrsLVLDQEDDWlEGYSdSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQE 1752
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2520 TLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTY-AVYLNPD----H 2594
Cdd:PRK12467 1753 AYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMlQQLLQMDeqveH 1832
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2595 MPDFKRLIAAGSASSLELLQQWKDKVKY---FNAYGPTEDSICTTIWTPSTEDISQLKSVPIGGPIVNHRIYIVDAHYQP 2671
Cdd:PRK12467 1833 PLSLRRVVCGGEALEVEALRPWLERLPDtglFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNP 1912
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2672 VPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEI 2750
Cdd:PRK12467 1913 VPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2751 EEQLLKVASVQEAIVIAHDDASGqKQLCAYFV----------ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPN 2820
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQDGANG-KQLVAYVVptdpglvdddEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPN 2071
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2821 GKIDRKALPAPQGNASAgADYVAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDL 2900
Cdd:PRK12467 2072 GKLDRKALPAPDASELQ-QAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDL 2150
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2901 FKYPTVAQLSKhirpVARM------ADQGEVSGDVSLTPIQHWFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLV 2974
Cdd:PRK12467 2151 FQHQTVQSLAA----VAQEgdgtvsIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALL 2226
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2975 EHHDALRVVFHKSENGYTAWNRAIGEGE---LYGLEVVDLkgieesaQAVEAKANEIQSSIDLEAGPFVKAGLFQCADGD 3051
Cdd:PRK12467 2227 VHHDALRLGFVQEDGGWSAMHRAPEQERrplLWQVVVADK-------EELEALCEQAQRSLDLEEGPLLRAVLATLPDGS 2299
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3052 H-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYRTWSEQLAAYAQSPVIERELAYWKRVAQTEVQPL 3130
Cdd:PRK12467 2300 QrLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTEL 2379
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3131 PKDEQvDVSLQQDSE-SISIEWTREETEQLLKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGRESIMTDID 3209
Cdd:PRK12467 2380 PCDHP-QGGLQRRHAaSVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEID 2458
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3210 ITRTVGWFTSKYPVvlELEQGKDISYLLKKTKEDLRGIPNKGIGYGICRYL--SAAKNDIAWGAEPEVSFNYLGQFDQDL 3287
Cdd:PRK12467 2459 LTRTVGWFTSLYPV--KLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLgsEAARQTLQALPVPRITFNYLGQFDGSF 2536
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3288 QNSDIGVSAHTGGKQSSDRQKRIFV---LDINGMIADGTLSLELSYNGKEYRRETMERLAASLQESLRVIIAHCVSKERA 3364
Cdd:PRK12467 2537 DAEKQALFVPSGEFSGAEQSEEAPLgnwLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQR 2616
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3365 ELTPSDVQFKGLSVEELEQISgqtQHLGDIENIYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGaLNIELFSRSWNEL 3444
Cdd:PRK12467 2617 GVTPSDFPLAGLSQEQLDRLP---VAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAV 2692
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3445 AARHAVLRTNFHS-GWRGEPLQIVYRYKPVEFAYEDLRHLAEAEWSayLDQLVNDDKTRGFDLEQDALMRVKVVRTQEES 3523
Cdd:PRK12467 2693 IDRHEILRSGFLWdGELEEPLQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADRQQGFDLLSAPLLRLTLVRTGEDR 2770
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3524 FHVLWSFHHILMDGWCLPLIAKELFDTYEAylrndlsERPAAPS--YSHYIEWLEKQDMEAAARYWTGFLAGYDSQTTLP 3601
Cdd:PRK12467 2771 HHLIYTNHHILMDGWSGSQLLGEVLQRYFG-------QPPPAREgrYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLA 2843
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3602 QG-KLHNKDGEYTEANILRSLGKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEM 3680
Cdd:PRK12467 2844 RAlYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQ 2923
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3681 IGLFINTIPVRVSCEAEQSFADVMKRVQEAALESGGYDYYPLYEIQAQSAQ-KQDLITHIMAFENFPMDEQIEQAGsyeD 3759
Cdd:PRK12467 2924 LGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGA---P 3000
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3760 GKLAITDVDIAEQTNYDFTLVVMPGEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAEI 3839
Cdd:PRK12467 3001 SGLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQV 3080
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3840 IHVFNNTAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVV 3919
Cdd:PRK12467 3081 LHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIV 3160
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3920 GIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFA--GTFVAVDDEQAYHADGSNLEPVVGPNHLA 3997
Cdd:PRK12467 3161 ALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPagDTALTLDRLDLNGYSENNPSTRVMGENLA 3240
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3998 YVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIpTSTTILDYPLF 4077
Cdd:PRK12467 3241 YVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDPEEL 3319
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4078 ESYMNENGITATILPPTY----AAYLNPDRMPSLKKLITGGSAASVEFVQQWKDK---VLYFNAYGPTEASIVTSIWDEA 4150
Cdd:PRK12467 3320 WQAIHAHRISIACFPPAYlqqfAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKlkpRGLTNGYGPTEAVVTVTLWKCG 3399
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4151 SDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFE-PGERMYRTGDLV 4229
Cdd:PRK12467 3400 GDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLA 3479
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4230 RWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGqQQLVAYFVAQRELTA--AELRATMSQ 4307
Cdd:PRK12467 3480 RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQGDwrETLRDHLAA 3558
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4308 ELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPEGSMHagGEYVAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELGGHS 4387
Cdd:PRK12467 3559 SLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS--REYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDS 3636
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4388 LRATALASKVRKELNMELPLRHIFQFPTVEQLAeaigqleqqefdaipvveereyypvssaqkrlyilqqlegaaqSYNM 4467
Cdd:PRK12467 3637 LLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA-------------------------------------------GYSP 3673
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4468 PGVMGLEGALDRERFEETFRKLIARHETLRTGFeliDGEPVQRIYPEvdfavetvqaseqeakaivrdfirpfdlakppl 4547
Cdd:PRK12467 3674 LGDVPVNLLLDLNRLETGFPALFCRHEGLGTVF---DYEPLAVILEG--------------------------------- 3717
                        3850      3860      3870      3880      3890      3900
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4548 lrvglielapERCILMLDMHHIVSDGvsadvlveefarlYSGEELPGLRIQYKDYAVWQQSEAQ 4611
Cdd:PRK12467 3718 ----------DRHVLGLTCRHLLDDG-------------WQDTSLQAMAVQYADYILWQQAKGP 3758
PRK12467 PRK12467
peptide synthase; Provisional
4403-8198 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 3278.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4403 MELPLRHIFQFptVEQLAEaigqlEQQEFDAIPVVEEREYY---PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDR 4479
Cdd:PRK12467   14 ITLPLEKRRLY--LEKMQE-----EGVSFANLPIPQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4480 ERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAVETV---QASEQEAKAIVRDFI-----RPFDLAKPPLLRVG 4551
Cdd:PRK12467   87 SALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDdlaNEQGRARESQIEAYIneevaRPFDLANGPLLRVR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4552 LIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGE------ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEA 4625
Cdd:PRK12467  167 LLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4626 FRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGR 4705
Cdd:PRK12467  247 LGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4706 THADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNT-- 4783
Cdd:PRK12467  327 NRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTat 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4784 --ENKEM-HLPGLHLTPYPTEYGMSKFDLSLDMMEDSEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIAS 4860
Cdd:PRK12467  407 ggRDREGaQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGE 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4861 LGILTADEKAQIVHVFNPAAPDAPeNEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLV 4940
Cdd:PRK12467  487 LPLLDAEERARELVRWNAPATEYA-PDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLV 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4941 GILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLqeRAQQWGQTLQAALCLDDEAA---- 5016
Cdd:PRK12467  566 GIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHL--LAQLPVPAGLRSLCLDEPADllcg 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5017 YAEDASNVANvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTLY 5096
Cdd:PRK12467  644 YSGHNPEVAL--DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD-SMLMVSTFAFDLGVTELFGALA 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5097 NGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLdmSSMVLLITSSDSCSVtDYRVLQERFGSQ 5176
Cdd:PRK12467  721 SGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQV-DLLARVRALGPG 797
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5177 FRIINAYGVTEAAIDSSLYDEPLAKLPeAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTE 5256
Cdd:PRK12467  798 ARLINHYGPTETTVGVSTYELSDEERD-FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTA 876
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5257 EKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvLC 5335
Cdd:PRK12467  877 ERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQ-LV 955
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5336 AHFT-------AESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEAK 5408
Cdd:PRK12467  956 AYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-AVQATFVAPQTELEKR 1034
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5409 LVSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEER 5488
Cdd:PRK12467 1035 LAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRD 1114
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5489 EYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVE 5568
Cdd:PRK12467 1115 QPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLE 1194
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5569 HYRTSEAEAGEV-VRGFV-----RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGES--- 5639
Cdd:PRK12467 1195 EPLLLAADKDEAqLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSqgq 1274
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5640 ---LAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIA 5716
Cdd:PRK12467 1275 slqLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALA 1354
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5717 AESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAY 5796
Cdd:PRK12467 1355 RREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQ 1434
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5797 EHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNK-ETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSEGLELSMEYS 5875
Cdd:PRK12467 1435 AHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDdHQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYA 1514
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5876 TALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEKEHIQRVFNATEAKYPSDKTIHQLFEEQAERIPDHLAVT 5955
Cdd:PRK12467 1515 TDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALV 1594
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5956 FEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKL 6035
Cdd:PRK12467 1595 FGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIEL 1674
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6036 LLVQGHLLDRASFADKL--VNLNDDGAYHE--DGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNT-NYV 6110
Cdd:PRK12467 1675 LLTQSHLQARLPLPDGLrsLVLDQEDDWLEgySDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATqEAY 1754
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6111 ELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDsGMFAG- 6189
Cdd:PRK12467 1755 QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHp 1833
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6190 --LKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENT---TFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLL 6264
Cdd:PRK12467 1834 lsLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdvTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPV 1913
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6265 PVGVWGELIVGGDGVARGYLNRPELTAEKFVESSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIE 6343
Cdd:PRK12467 1914 PIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6344 EQLLKVASVKEATVIVREDESGqKQLCAYFV---------AERELTI-GELRAALSQELPNYMIPSHFVPLERMPLTPNG 6413
Cdd:PRK12467 1994 ARLREQGGVREAVVIAQDGANG-KQLVAYVVptdpglvddDEAQVALrAILKNHLKASLPEYMVPAHLVFLARMPLTPNG 2072
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6414 KIDRRALPAPQGNAPVGAeYVAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLF 6493
Cdd:PRK12467 2073 KLDRKALPAPDASELQQA-YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLF 2151
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6494 KYPTLAQLSQhiqpVARM------IDQGEVTGEIGLTPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAE 6567
Cdd:PRK12467 2152 QHQTVQSLAA----VAQEgdgtvsIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLV 2227
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6568 HHDALRTVFRKSENGYAAWNRAIGEGE---LYSLEVADfrdvksaEQAVEAKANEIQSSIDLEVGPLFKAGLFQCADGDH 6644
Cdd:PRK12467 2228 HHDALRLGFVQEDGGWSAMHRAPEQERrplLWQVVVAD-------KEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQ 2300
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6645 -LLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEEVRLPAKTDSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAPLP 6723
Cdd:PRK12467 2301 rLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELP 2380
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6724 KDKQSDRSLQQDSESITIQWSRKETEQLLKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDIT 6803
Cdd:PRK12467 2381 CDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLT 2460
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6804 RTVGWFTSKYPVLLQmePGRSLSTRIKKVKEDLRRIPNKGIGYGLCRYLSAQPDGTVWGA--EPEISFNYLGQFDQDLSN 6881
Cdd:PRK12467 2461 RTVGWFTSLYPVKLS--PTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQAlpVPRITFNYLGQFDGSFDA 2538
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6882 NDIGL---SPYSSGLEMSDRQARSFILDINGMITDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAHCAAKEWTEL 6958
Cdd:PRK12467 2539 EKQALfvpSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGV 2618
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6959 TPSDVQLKGLTVEELEQISAQtrnVGEIENIYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGsLDAEQFARSWNDLVA 7038
Cdd:PRK12467 2619 TPSDFPLAGLSQEQLDRLPVA---VGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVID 2694
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7039 RHAILRTNFFS-GPRGEPLQIVYRDKRIGFVYEDLSHLPadERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYR 7117
Cdd:PRK12467 2695 RHEILRSGFLWdGELEEPLQVVYKQARLPFSRLDWRDRA--DLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHH 2772
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7118 VLWSFHHILMDGWCLPLVVKELFETYeayvqGDRPEQKAAPAYSQYIEWLENQDSAAASAYWSNYLAGYEGQTALPQEKA 7197
Cdd:PRK12467 2773 LIYTNHHILMDGWSGSQLLGEVLQRY-----FGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALY 2847
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7198 QKRSEGyVAEH--VVCELDKELSERMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGL 7275
Cdd:PRK12467 2848 PAPAEA-VAGHgaHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGL 2926
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7276 FINTIPVRVACQPEESFADVMGRMQEAALESGRYDFYPLYEIQTQSAQ-KQELINHLLVFENYPMDEQVEQAGgddSGTL 7354
Cdd:PRK12467 2927 FINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQgGEALFDSILVFENYPISEALKQGA---PSGL 3003
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7355 SITDVDVAEHTNYNFTVTVFPGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHV 7434
Cdd:PRK12467 3004 RFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHA 3083
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7435 FNNTAAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAF 7514
Cdd:PRK12467 3084 WNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALL 3163
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7515 AIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQE--CVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVI 7592
Cdd:PRK12467 3164 AVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEqlPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVI 3243
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7593 YTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDtILDYPLFESY 7672
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDND-LWDPEELWQA 3322
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 MNENGITAAILPPTYAIYLSPD----RLPSLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDG 7745
Cdd:PRK12467 3323 IHAHRISIACFPPAYLQQFAEDaggaDCASLDIYVFGGEAVPPAAFEQVKRKlkpRGLTNGYGPTEAVVTVTLWKCGGDA 3402
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7746 LDLRS-VPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFL-AGERMYRTGDLARWL 7823
Cdd:PRK12467 3403 VCEAPyAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYR 3482
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7824 PDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARgDANGQQQLCAYFVADRELT--VSELRGTLSQELP 7901
Cdd:PRK12467 3483 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGdwRETLRDHLAASLP 3561
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7902 GYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSMQtgADFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRA 7981
Cdd:PRK12467 3562 DYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS--REYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLA 3639
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7982 TVLSSKVNKELNVNLPLRDIFRFPTVEALAQVIdGLEQEEHSaipvigereyyPVSSAQKRlfilhqlegaqqsynipgf 8061
Cdd:PRK12467 3640 LQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS-PLGDVPVN-----------LLLDLNRL------------------- 3688
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8062 atiegpldRDRFEAVFRqlieRHETLRTGFEmanGEPVQRVysdvefaveyskadreeaveiaqrfvrpfdlrkppllrv 8141
Cdd:PRK12467 3689 --------ETGFPALFC----RHEGLGTVFD---YEPLAVI--------------------------------------- 3714
                        3850      3860      3870      3880      3890
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 8142 glieVEPERHILMLDMHHIISDGASVgilqeefsrlyagEELPPLRIQYKDYAAWQR 8198
Cdd:PRK12467 3715 ----LEGDRHVLGLTCRHLLDDGWQD-------------TSLQAMAVQYADYILWQQ 3754
PRK12316 PRK12316
peptide synthase; Provisional
1859-5900 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 3160.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1859 MNVE--LPLRDVFRCSTVEEMAQAIARMEEQ----AYVSIPT-VEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVL 1931
Cdd:PRK12316    1 MNAEdsLKLARRFIELPLEKRRVFLATLRGEgvdfSLFPIPAgVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1932 EGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYRTS---EAE-----AGEVVRGFVRTFDLAKP 2003
Cdd:PRK12316   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSglpEAEqearlRDEAQRESLQPFDLCEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2004 PLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGES------LATLRIQYKDYAVWQQSEEQLERVKRQE 2077
Cdd:PRK12316  161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYAtgaepgLPALPIQYADYALWQRSWLEAGEQERQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2078 AYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIG 2157
Cdd:PRK12316  241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2158 TPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFV 2237
Cdd:PRK12316  321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2238 LQNTENEE---LQLDGLKLAPYPSGNTIARFDLTLDVTETGSGLECNLEYATSLYARETIARMAKHLEQLLTAIAKAPEA 2314
Cdd:PRK12316  401 HQPLVADIealDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2315 PIAGLEMLTAAEQTQLHHVFNATAADYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKT 2394
Cdd:PRK12316  481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2395 DQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFAG--TVVTVDDEQAYA 2472
Cdd:PRK12316  561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAgvQVLDLDRPAAWL 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2473 GDGS--NLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFF 2550
Cdd:PRK12316  641 EGYSeeNPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2551 GATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAVYLNPDHMPD----FKRLIAAGSASSLELLQQWKDKV---KYF 2623
Cdd:PRK12316  721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAsctsLRRIVCSGEALPADAQEQVFAKLpqaGLY 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2624 NAYGPTEDSICTTIWTPSTEDisqLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFV 2703
Cdd:PRK12316  801 NLYGPTEAAIDVTHWTCVEEG---GDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFV 877
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2704 DNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDdasgQKQLCAYFVA 2783
Cdd:PRK12316  878 PSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVL 953
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2784 DRT--MTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALPAPQGNASAgADYVAPRSEEEKVLADVWQAVLG 2861
Cdd:PRK12316  954 ESEggDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQ-QGYVAPRNALERTLAAIWQDVLG 1032
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2862 AERVGATDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTVAQLSKHIR-PVARMADQGEVSGDVSLTPIQHWFFE 2940
Cdd:PRK12316 1033 VERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKaGQATAADQGPASGEVALAPVQRWFFE 1112
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2941 PQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFhKSENGytAWNRAIGEGElyGLEVVDLKGIeESAQA 3020
Cdd:PRK12316 1113 QAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRF-REEDG--GWQQAYAAPQ--AGEVLWQRQA-ASEEE 1186
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3021 VEAKANEIQSSIDLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVkgeeLRFPAKTDAYRTW 3099
Cdd:PRK12316 1187 LLALCEEAQRSLDLEQGPLLRALLVDMADGSQrLLLVIHHLVVDGVSWRILLEDLQRAYADLD----ADLPARTSSYQAW 1262
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3100 SEQLAAYAQSPVieRELAYWKRVAQTEVQPLPKDEQVDVSLQQDSESISIEWTREETEQLLKGVHRAYNTEMNDILLAAL 3179
Cdd:PRK12316 1263 ARRLHEHAGARA--EELDYWQAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTAL 1340
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3180 GMAVQKWSGLDRVLVNLEGHGRESIMTDIDITRTVGWFTSKYPVVLELEQgkDISYLLKKTKEDLRGIPNKGIGYGICRY 3259
Cdd:PRK12316 1341 ARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGWFTSLFPVRLTPAA--DLGESIKAIKEQLRAVPDKGIGYGLLRY 1418
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3260 LSA--AKNDIAWGAEPEVSFNYLGQFDQDLQNSDIGVSAHTGGKQSSDRQKRIF-VLDINGMIADGTLSLELSYNGKEYR 3336
Cdd:PRK12316 1419 LAGeeAAARLAALPQPRITFNYLGQFDRQFDEAALFVPATESAGAAQDPCAPLAnWLSIEGQVYGGELSLHWSFSREMFA 1498
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3337 RETMERLAASLQESLRVIIAHCVSKERAELTPSDVQFKGLSVEELEQISGQTqhlGDIENIYALTPMQKGMWFHNTLNRH 3416
Cdd:PRK12316 1499 EATVQRLADDYARELQALIEHCCDERNRGVTPSDFPLAGLSQAQLDALPLPA---GEIADIYPLSPMQQGMLFHSLYEQE 1575
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3417 GGAYIEQTLFNVRGaLNIELFSRSWNELAARHAVLRTNFHsgWRG---EPLQIVYRYKPVEFAYEDLRhlAEAEWSAYLD 3493
Cdd:PRK12316 1576 AGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFL--WQDgleQPLQVIHKQVELPFAELDWR--GREDLGQALD 1650
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3494 QLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAylrndlsERPAAPS--YSHY 3571
Cdd:PRK12316 1651 ALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-------QPVAAPGgrYRDY 1723
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3572 IEWLEKQDMEAAARYWTGFLAGYDSQTTLPQgKLHNKDGEYTEANILRSLGKSLTERMSRIAKQHQVTVNTLMQAAWGII 3651
Cdd:PRK12316 1724 IAWLQRQDAAASEAFWKEQLAALEEPTRLAQ-AARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLL 1802
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3652 LQKYNGTDDAVFGSVVSGRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAALESGGYDYYPLYEIQAQSAQ 3731
Cdd:PRK12316 1803 LQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQ 1882
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3732 K-QDLITHIMAFENFPMDEQIEQAGsyeDGKLAITDVDIAEQTNYDFTLVVMPGEELAVRFYYNASVYEHSAMERLMGHL 3810
Cdd:PRK12316 1883 GgEALFDSLLVFENYPVAEALKQGA---PAGLVFGRVSNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHL 1959
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3811 IHVLEQVTASPNAPVSMLELVTEAEKAEIIHVFNNTAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERAN 3890
Cdd:PRK12316 1960 LHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRAN 2039
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3891 RLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGT 3970
Cdd:PRK12316 2040 RLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAG 2119
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3971 FVAVD-DEQAYHADGSNLEPVV--GPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFD 4047
Cdd:PRK12316 2120 VARLPlDRDAEWADYPDTAPAVqlAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFD 2199
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4048 ASCWEIFKALFFGATLYIPTSTTILDYPLFESyMNENGITATILPPTY----AAYLNPD-RMPSLKKLITGGSAASVEFV 4122
Cdd:PRK12316 2200 GAHEQWFHPLLNGARVLIRDDELWDPEQLYDE-MERHGVTILDFPPVYlqqlAEHAERDgRPPAVRVYCFGGEAVPAASL 2278
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4123 QQWK---DKVLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARG 4199
Cdd:PRK12316 2279 RLAWealRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARG 2358
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4200 YLNRPELTAEKFVDNPFE-PGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLARE 4278
Cdd:PRK12316 2359 YLNRPGLTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQD 2438
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4279 DANGqQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPEGSMhAGGEYVAPRTP 4356
Cdd:PRK12316 2439 GASG-KQLVAYVVPDdaAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQ-LRQAYVAPQEG 2516
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4357 TEAKLAHIWQDVLGLEKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQFPTVEQLAEAIGQLEQQEFDAIPV 4436
Cdd:PRK12316 2517 LEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQK 2596
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4437 VEEREYYPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEV- 4515
Cdd:PRK12316 2597 VTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMs 2676
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4516 --DFAVETVQASEQEAKAIVRDFI-RPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGE-- 4590
Cdd:PRK12316 2677 lrIVLEDCAGVADAAIRQRVAEEIqRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGArr 2756
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4591 ----ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKR 4666
Cdd:PRK12316 2757 geqpTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLA 2836
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4667 IAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLG 4746
Cdd:PRK12316 2837 LARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALG 2916
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4747 AFEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEMHLPGLHLTPYPTEYGMSKFDLSLDMMEDSEGLECSLEF 4826
Cdd:PRK12316 2917 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTY 2996
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4827 ATALYKRETIERMAKHFEQLLTAIVNDPAAKIASLGILTADEKAQIVHVFNPAAPDAPENEAFHALFEKQAECTPEAAAV 4906
Cdd:PRK12316 2997 ATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVAL 3076
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4907 VYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAAS 4986
Cdd:PRK12316 3077 AFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQ 3156
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4987 VLLTQTHLQERAQQWGQTlqaaLCLDDEAAYAEDAsNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRRE 5066
Cdd:PRK12316 3157 LLLSQSHLRLPLAQGVQV----LDLDRGDENYAEA-NPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA 3231
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5067 YRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGL 5146
Cdd:PRK12316 3232 YGLGV-GDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRC 3310
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5147 DMSSMVLLITSSDSCSvtdyrvLQERFGSQFRIINAYGVTEAAIDSSLYDeplAKLPEAGNVPIGKAALNAKFYIVDAHL 5226
Cdd:PRK12316 3311 TSLKRIVCGGEALPAD------LQQQVFAGLPLYNLYGPTEATITVTHWQ---CVEEGKDAVPIGRPIANRACYILDGSL 3381
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5227 NPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGE 5306
Cdd:PRK12316 3382 EPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGE 3461
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5307 IETQLLKAEGvreAVVVVREDAKGQKVLCAHFTAESELKLSE-LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK12316 3462 IEARLLEHPW---VREAVVLAVDGRQLVAYVVPEDEAGDLREaLKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5386 PAPDASM-QTGmeYVAPRTPQEAKLVSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVhKEMNVELPLRDVFRCSTV 5464
Cdd:PRK12316 3539 PRPDAALlQQD--YVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTI 3615
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5465 EEMAQAI----ARMEEQAYVSIPTV---EEREYYPVSSAQKRLYILHQLegaeqsynmtgeLVLEGILDRGKLEEAFRQL 5537
Cdd:PRK12316 3616 QGLARVArvggGVAVDQGPVSGETLllpIQQQFFEEPVPERHHWNQSLL------------LKPREALDAAALEAALQAL 3683
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5538 IARHETLRTGFELVNGE-PVQRVYKEVNFAVE-HYRTSEAEA----GEVVRgfvRTFDLAKPPLLRVGLVELAEDLHILL 5611
Cdd:PRK12316 3684 VEHHDALRLRFVEDAGGwTAEHLPVELGGALLwRAELDDAEElerlGEEAQ---RSLDLADGPLLRALLATLADGSQRLL 3760
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5612 LDMHHIVSDGVSTDVLTEEFGRMY----NGE--SLAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPvlELPT 5685
Cdd:PRK12316 3761 LVIHHLVVDGVSWRILLEDLQQAYqqllQGEapRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSS--ELPC 3838
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5686 DYPRPAVRKFEGSLLQRQLEPKLGEG-LQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGR----THSDLQP 5760
Cdd:PRK12316 3839 DHPQGALQNRHAASVQTRLDRELTRRlLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGRedlfADIDLSR 3918
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5761 IIGMFVNTLAIRSYPddKKTFRSFLDEVKEtMLGAYEHQSYPFEEL--VEKAQPARDLSRNPLFDTLFALQNKETGELQL 5838
Cdd:PRK12316 3919 TVGWFTSLFPVRLSP--VEDLGASIKAIKE-QLRAIPNKGIGFGLLryLGDEESRRTLAGLPVPRITFNYLGQFDGSFDE 3995
                        4090      4100      4110      4120      4130      4140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5839 DGLRLTPYP----AEHTV-AKFDLSVDVTEGSEGLELSME--YSTALYTRETIERMAKHFEQLLTAIVQ 5900
Cdd:PRK12316 3996 EMALFVPAGesagAEQSPdAPLDNWLSLNGRVYGGELSLDwtFSREMFEEATIQRLADDYAAELTALVE 4064
PRK12316 PRK12316
peptide synthase; Provisional
843-4434 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 2857.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  843 SIPAAEAREYYPLSSAQKRLyILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGG--EPMQR 920
Cdd:PRK12316 1547 PLPAGEIADIYPLSPMQQGM-LFHSLYEQEAGDYINQLRVDVQGLDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQV 1625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  921 IYPEVE--FAVEHIRANEEEADA----AVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFA 994
Cdd:PRK12316 1626 IHKQVElpFAELDWRGREDLGQAldalAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVL 1705
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  995 RLYGGEDLPALRIQYKDYAVWQQSEAQKEQlkrqEAYWlevfRGELPVLEMPTDYAR----PAVQSYAGNALRfELDAQK 1070
Cdd:PRK12316 1706 QRYAGQPVAAPGGRYRDYIAWLQRQDAAAS----EAFW----KEQLAALEEPTRLAQaartEDGQVGYGDHQQ-LLDPAQ 1776
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1071 REGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRThGDLHPL---IGMFVNTLAIRNYPAADKTFLSYL 1147
Cdd:PRK12316 1777 TRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRP-AELPGIeqqIGLFINTLPVIAAPRPDQSVADWL 1855
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1148 EDVKETTLGAFERQDYPfeeLVDKLKLArDLSRNPLFDTMFTLQN---TENKEFRLP-GLQLTPYPVEEHTSkFDLSLDI 1223
Cdd:PRK12316 1856 QEVQALNLALREHEHTP---LYDIQRWA-GQGGEALFDSLLVFENypvAEALKQGAPaGLVFGRVSNHEQTN-YPLTLAV 1930
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1224 mESGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEEKAQLVHVFNPAAPDAPENEVFHALF 1303
Cdd:PRK12316 1931 -TLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRI 2009
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1304 EKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 1383
Cdd:PRK12316 2010 AEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPA 2089
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1384 DRIQFMLEDSAASVLLTQTHLQERAQQWGQTlqAVLCLDDEAAYAEDAS-NVANVNEPHDLAYVIYTSGTTGRPKGVMIE 1462
Cdd:PRK12316 2090 ERLAYMLEDSGAALLLTQRHLLERLPLPAGV--ARLPLDRDAEWADYPDtAPAVQLAGENLAYVIYTSGSTGLPKGVAVS 2167
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1463 HRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTLYNGGTMVIcpKDDRI-DPARLHYWISEEKITIFESTP 1541
Cdd:PRK12316 2168 HGALVAHCQAAGERYELSPAD-CELQFMSFSFDGAHEQWFHPLLNGARVLI--RDDELwDPEQLYDEMERHGVTILDFPP 2244
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 ALIIPFMDyVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIG 1621
Cdd:PRK12316 2245 VYLQQLAE-HAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV-YLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIG 2322
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1622 KAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGR 1700
Cdd:PRK12316 2323 RALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGR 2402
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1701 IDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvLCAYFTAES--ELKLSELRSSLSQELPGYMIPSYFVQ 1778
Cdd:PRK12316 2403 IDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQ-LVAYVVPDDaaEDLLAELRAWLAARLPAYMVPAHWVV 2481
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1779 LEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEAKLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKE 1858
Cdd:PRK12316 2482 LERLPLNPNGKLDRKALPKPDVS-QLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQD 2560
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1859 MNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRG 1938
Cdd:PRK12316 2561 LGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQA 2640
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1939 KLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFA---VEHYRTSEAEAGEVVRGFV-RTFDLAKPPLLRVGLVELA 2014
Cdd:PRK12316 2641 ALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRivlEDCAGVADAAIRQRVAEEIqRPFDLARGPLLRVRLLALD 2720
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2015 EDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGES------LATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGEL 2088
Cdd:PRK12316 2721 GQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQ 2800
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2089 PVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDL 2168
Cdd:PRK12316 2801 PVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAET 2880
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2169 QPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEELQL 2248
Cdd:PRK12316 2881 ERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQL 2960
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2249 DGLKLAPYPSGNTIARFDLTLDVTETGSGLECNLEYATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQT 2328
Cdd:PRK12316 2961 PGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERG 3040
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2329 QLHHVFNATAADYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEM 2408
Cdd:PRK12316 3041 QLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEM 3120
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2409 VVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSfAGTVVTVDDEQAYAGDGSNLESAVGPNDLA 2488
Cdd:PRK12316 3121 VVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLA-QGVQVLDLDRGDENYAEANPAIRTMPENLA 3199
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2489 YIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWF 2568
Cdd:PRK12316 3200 YVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALL 3279
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2569 ERYMSDNGITTATLPPTYAVYLNPDHMP----DFKRLIAAGSASSLELLQQWKDKVKYFNAYGPTEDSICTTIWTPSTED 2644
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFLEEEDAhrctSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEG 3359
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2645 ISQlksVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLP 2724
Cdd:PRK12316 3360 KDA---VPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRA 3436
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2725 DGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDasgqKQLCAYFVADRTMTV--GELRGELSGELPG 2802
Cdd:PRK12316 3437 DGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDG----RQLVAYVVPEDEAGDlrEALKAHLKASLPE 3512
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2803 YMIPAHFVQLERMPLTPNGKIDRKALPAPQGnASAGADYVAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDSIKSI 2882
Cdd:PRK12316 3513 YMVPAHLLFLERMPLTPNGKLDRKALPRPDA-ALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISL 3591
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2883 QVSSRLHQAGYKLEIRDLFKYPTVAQLSKHIRPVARMA-DQGEVSGDVSLTPIQHWFFEPQFAEPHHFNQSVMLHRRDGF 2961
Cdd:PRK12316 3592 QVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAvDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREAL 3671
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2962 DEAAIRKVLQKLVEHHDALRVVFHKSENGYTAWNRAIGEGE--LYGLEVVDlkgieesAQAVEAKANEIQSSIDLEAGPF 3039
Cdd:PRK12316 3672 DAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGalLWRAELDD-------AEELERLGEEAQRSLDLADGPL 3744
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3040 VKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYRTWSEQLAAYAQSPVIERELAY 3118
Cdd:PRK12316 3745 LRALLATLADGSQrLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAY 3824
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3119 WKRVAQTEVQPLPKDEQVDVSLQQDSESISIEWTREETEQLLKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEG 3198
Cdd:PRK12316 3825 WQEQLQGVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEG 3904
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3199 HGRESIMTDIDITRTVGWFTSKYPVvlELEQGKDISYLLKKTKEDLRGIPNKGIGYGICRYL--SAAKNDIAWGAEPEVS 3276
Cdd:PRK12316 3905 HGREDLFADIDLSRTVGWFTSLFPV--RLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLgdEESRRTLAGLPVPRIT 3982
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3277 FNYLGQFDQ--DLQNSDIGVSAHTGGKQSSDRQKRIFVLDINGMIADGTLSLELSYNGKEYRRETMERLAASLQESLRVI 3354
Cdd:PRK12316 3983 FNYLGQFDGsfDEEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTAL 4062
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3355 IAHCVSKERAELTPSDVQFKGLSVEELEQISgqtQHLGDIENIYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGaLNI 3434
Cdd:PRK12316 4063 VEHCCDAERHGVTPSDFPLAGLDQARLDALP---LPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDV 4138
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3435 ELFSRSWNELAARHAVLRTNF-HSGWRGEPLQIVYRYKPVEFAYEDLRhlAEAEWSAYLDQLVNDDKTRGFDLEQDALMR 3513
Cdd:PRK12316 4139 ERFRAAWQAALDRHDVLRSGFvWQGELGRPLQVVHKQVSLPFAELDWR--GRADLQAALDALAAAERERGFDLQRAPLLR 4216
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3514 VKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYeaylrndlSERPAAPS---YSHYIEWLEKQDMEAAARYWTGF 3590
Cdd:PRK12316 4217 LVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY--------SGRPPAQPggrYRDYIAWLQRQDAAASEAFWREQ 4288
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3591 LAGYDSQTTLPQGkLHNKDGEYTE--ANILRSLGKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVS 3668
Cdd:PRK12316 4289 LAALDEPTRLAQA-IARADLRSANgyGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVA 4367
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3669 GRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAALESGGYDYYPLYEIQAQSAQKQD-LITHIMAFENFPM 3747
Cdd:PRK12316 4368 GRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEaLFDSLLVFENYPV 4447
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3748 DEQIEQAGSyedGKLAITDVDIAEQTNYDFTLVVMPGEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSM 3827
Cdd:PRK12316 4448 SEALQQGAP---GGLRFGEVTNHEQTNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGE 4524
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3828 LELVTEAEKAEIIHVFNNTAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLV 3907
Cdd:PRK12316 4525 LQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLV 4604
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3908 GLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADG-SN 3986
Cdd:PRK12316 4605 GIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGfPA 4684
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3987 LEPVVG--PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLY 4064
Cdd:PRK12316 4685 HDPAVRlhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVV 4764
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4065 IPTSTTILDYPLFESyMNENGITATILPPTYAAYL-----NPDRMPSLKKLITGGSAASVEFVQQW--KDKVLY-FNAYG 4136
Cdd:PRK12316 4765 IRDDSLWDPERLYAE-IHEHRVTVLVFPPVYLQQLaehaeRDGEPPSLRVYCFGGEAVAQASYDLAwrALKPVYlFNGYG 4843
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4137 PTEASIVTSIWDEASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPF 4216
Cdd:PRK12316 4844 PTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF 4923
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4217 -EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGqQQLVAYFVAQRE 4295
Cdd:PRK12316 4924 gAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVPQDP 5002
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4296 LTA----------AELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPEGSMhAGGEYVAPRTPTEAKLAHIW 4365
Cdd:PRK12316 5003 ALAdadeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASL-LQQAYVAPRSELEQQVAAIW 5081
                        3610      3620      3630      3640      3650      3660      3670
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 4366 QDVLGLEKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQFPTVE---QLAEAIGQLEQQEFDAI 4434
Cdd:PRK12316 5082 AEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAafvELAAAAGSGDDEKFDDL 5153
PRK05691 PRK05691
peptide synthase; Validated
3863-8018 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 2843.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3863 QALRNPDAVAVVF------EKSQLTYGELNERANRLARTLRDAGVRPDQLVgLMVERSLEMVVGIMAIMKAGGAYIPIDP 3936
Cdd:PRK05691   18 RAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3937 -----EYPEDRIRYMLEDSGAQALLTQRHLRE--------RVSFAGTFVAVDDEQAYHADGSNlEPVVGPNHLAYVIYTS 4003
Cdd:PRK05691   97 pesarRHHQERLLSIIADAEPRLLLTVADLRDsllqmeelAAANAPELLCVDTLDPALAEAWQ-EPALQPDDIAFLQYTS 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4004 GTTGKPKGVMVEHHGLCSLKLMFANT--LQMTEQDRVVQFASLSFDAS-CWEIFKALFFGATLYIPTSTTILDYPL-FES 4079
Cdd:PRK05691  176 GSTALPKGVQVSHGNLVANEQLIRHGfgIDLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYFLERPLrWLE 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4080 YMNENGITATiLPPTYAAYLNPDRMP--SLKKL--------ITGGSAASVEFVQQWKDKVL--------YFNAYGPTEAS 4141
Cdd:PRK05691  256 AISEYGGTIS-GGPDFAYRLCSERVSesALERLdlsrwrvaYSGSEPIRQDSLERFAEKFAacgfdpdsFFASYGLAEAT 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4142 IVTS---------IWDEASDSLGDRKSVP--------IGRPLANHRIYVVD-SHNRMLPVGVAGELCISGVGLARGYLNR 4203
Cdd:PRK05691  335 LFVSggrrgqgipALELDAEALARNRAEPgtgsvlmsCGRSQPGHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRN 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4204 PELTAEKFVDNPfepGERMYRTGDLvRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAK-IDAVQEAIVLARE-DAN 4281
Cdd:PRK05691  415 PEASAKTFVEHD---GRTWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEReVEVVRKGRVAAFAvNHQ 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4282 GQQQL-VAYFVA---QRELTAAELRATMSQELPN--YMIPSYFVQL--AQMPLTPNGKIDRKA--LPAPEGSMHA----- 4346
Cdd:PRK05691  491 GEEGIgIAAEISrsvQKILPPQALIKSIRQAVAEacQEAPSVVLLLnpGALPKTSSGKLQRSAcrLRLADGSLDSyalfp 570
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4347 GGEYVAPRTPT------EAKLAHIWQDVLGLEKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQFPTVEQLA 4420
Cdd:PRK05691  571 ALQAVEAAQTAasgdelQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFS 650
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4421 EAIGQLEQ---QEFDAIPVVEEREYYPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLR 4497
Cdd:PRK05691  651 AAVARQLAgggAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLR 730
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4498 TGFELIDGEPVQRIYPEVDFAVETVQ-----ASEQEAKAIV---RDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHI 4569
Cdd:PRK05691  731 TRFYERDGVALQRIDAQGEFALQRIDlsdlpEAEREARAAQireEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHI 810
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4570 VSDGVSADVLVEEFARLYSGE------ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPA 4643
Cdd:PRK05691  811 VADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSA 890
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4644 VQSYAGDTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAI 4723
Cdd:PRK05691  891 RQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVL 970
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4724 RNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEELVDKLQMARDlsrNPLFDTMFSLQNTENKEM-HLPGLHLTPYPTEY 4802
Cdd:PRK05691  971 RAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQARE---QGLFQVMFNHQQRDLSALrRLPGLLAEELPWHS 1047
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4803 GMSKFDLSLDMMEDSEG-LECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIASLGILTADEKAQIVHVfnPAAP 4881
Cdd:PRK05691 1048 REAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQW--GQAP 1125
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4882 DAPENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAG 4961
Cdd:PRK05691 1126 CAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4962 GAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQwgqtlqaalcLDDEAAYAEDASNVAN--VNEP------HDL 5033
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQ----------AEGVSAIALDSLHLDSwpSQAPglhlhgDNL 1275
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5034 AYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVrLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPA 5113
Cdd:PRK05691 1276 AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDV-LMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQ 1354
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5114 RLHYWISEEKITIFESTPALIIPFMDYVAEHGLdmSSMVLLITSSDSCSVT-DYRVLQERFGSQFRiiNAYGVTEAAIDS 5192
Cdd:PRK05691 1355 RIAELVQQYGVTTLHFVPPLLQLFIDEPLAAAC--TSLRRLFSGGEALPAElRNRVLQRLPQVQLH--NRYGPTETAINV 1430
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5193 SLYDeplAKLPEAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVE-GERLY 5271
Cdd:PRK05691 1431 THWQ---CQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEdGARLY 1507
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5272 RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvLCAHFTAE--SELKLSEL 5349
Cdd:PRK05691 1508 RTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQ-LVGYYTGEagQEAEAERL 1586
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5350 RSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDasMQTGmEYVAPRTPQEAKLVSIWQEVLGLEKVGVKDNFF 5429
Cdd:PRK05691 1587 KAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV--WQQR-EHVEPRTELQQQIAAIWREVLGLPRVGLRDDFF 1663
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5430 ELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVS----IPTVEEREYYPVSSAQKRLYILHQ 5505
Cdd:PRK05691 1664 ALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNsqgaIARVDRSQPVPLSYSQQRMWFLWQ 1743
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5506 LEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKE--VNFAVEHYRTSEAEAGE---- 5579
Cdd:PRK05691 1744 MEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDsgLRMDWQDFSALPADARQqrlq 1823
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5580 --VVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNG-----ES-LAPLRIQYKDYA 5651
Cdd:PRK05691 1824 qlADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAflddrESpLEPLPVQYLDYS 1903
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5652 TWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAAESGATLYMVLLAAY 5731
Cdd:PRK05691 1904 VWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATL 1983
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5732 KVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAYEHQSYPFEELVEKAQ 5811
Cdd:PRK05691 1984 AALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQ 2063
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5812 PARDLSRNPLFDTLFALQNKETGEL-QLDGLRLTPYPAEHTVAKFDLSVDVTEGSEGLELSMEYSTALYTRETIERMAKH 5890
Cdd:PRK05691 2064 PPRSAAYNPLFQVMCNVQRWEFQQSrQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEH 2143
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5891 FEQLLTAIVQAPEAPLASLEMITAEEKEHIQRVFNATEAKYPSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERA 5970
Cdd:PRK05691 2144 WQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARA 2223
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5971 NRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQGHLLDRASFAD 6050
Cdd:PRK05691 2224 NRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELP 2303
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6051 KLVN---LNDDGAY--HEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVV--------RLVKNTNYVELneqtH 6117
Cdd:PRK05691 2304 AGVArwcLEDDAAAlaAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAmhcqavieRFGMRADDCEL----H 2379
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6118 ILqtgAVVFDASTFEIWGALLNGGRLyVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQ--QDSGMFAGLKTLIV 6195
Cdd:PRK05691 2380 FY---SINFDAASERLLVPLLCGARV-VLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQwlAGQGEQLPVRMCIT 2455
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6196 GGDVLSVPHINRVLREHAGLSIVNGYGPTEnTTFSTTHTIVGEQKEA----VPIGKPINNSTAYIVDSKLSLLPVGVWGE 6271
Cdd:PRK05691 2456 GGEALTGEHLQRIRQAFAPQLFFNAYGPTE-TVVMPLACLAPEQLEEgaasVPIGRVVGARVAYILDADLALVPQGATGE 2534
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6272 LIVGGDGVARGYLNRPELTAEKFVESSFLP-GERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVA 6350
Cdd:PRK05691 2535 LYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHP 2614
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6351 SVKEATVIVREDESGqKQLCAYFVAER----ELTIGELRAA----LSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPA 6422
Cdd:PRK05691 2615 AVREAVVLALDTPSG-KQLAGYLVSAVagqdDEAQAALREAlkahLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPA 2693
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6423 PQGNAPVGAeYVAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPT---LA 6499
Cdd:PRK05691 2694 PDPELNRQA-YQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTvqtLA 2772
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6500 QLSQHIQPVARmiDQGEVTGEIGLTPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKS 6579
Cdd:PRK05691 2773 AVATHSEAAQA--EQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQA 2850
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6580 ENGYAAWNRAIGEGE-LYSLEVADFRDVksaeqavEAKANEIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGV 6657
Cdd:PRK05691 2851 DGRWQAEYRAVTAQElLWQVTVADFAEC-------AALFADAQRSLDLQQGPLLRALLVDGPQGQQrLLLAIHHLVVDGV 2923
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6658 SWRILLEDVALGYEQAAKGEEVRLPAKTDSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAPLPKDKQSDRSLQQDSE 6737
Cdd:PRK05691 2924 SWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQ 3003
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6738 SITIQWSRKETEQLLKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDITRTVGWFTSKYPVLL 6817
Cdd:PRK05691 3004 TVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRL 3083
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6818 QMEPGR--SLSTRIKKVKEDLRRIPNKGIGYGLCRYLSAQPDGTVWGAEPE--ISFNYLGQFDQDLSnNDIGLSPY--SS 6891
Cdd:PRK05691 3084 TPAPGDdaARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQapITFNYLGQFDQSFA-SDALFRPLdePA 3162
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6892 GLEMSDRQARSFILDINGMITDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAHCAAKEWTELTPSDVQLKGLTve 6971
Cdd:PRK05691 3163 GPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLT-- 3240
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6972 eLEQISAQTRNVGEIENIYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNfFSGP 7051
Cdd:PRK05691 3241 -QAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRAS-FSWN 3318
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7052 RGEP-LQIVYRDKRIGFVYEDLSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGW 7130
Cdd:PRK05691 3319 AGETmLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAW 3398
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7131 CLPLVVKELFETYEAYVQGDRPEQKAAPAYSQYIEWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKR-----SEGYV 7205
Cdd:PRK05691 3399 CRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERPTPIPSDRPFLRehagdSGGMV 3478
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7206 AEHVVCELDKELSERMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVA 7285
Cdd:PRK05691 3479 VGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQ 3558
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7286 C-QPEE--SFADVMGRMQEAALESGRYDFYPLYEIQTQS--AQKQELINHLLVFENYPmdeqVEQAGGDDSGTLSITDVD 7360
Cdd:PRK05691 3559 LpAAGQrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSelPKGQPLFDSLFVFENAP----VEVSVLDRAQSLNASSDS 3634
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7361 VAEHTNYNFTVTVFPGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHVFNNTAA 7440
Cdd:PRK05691 3635 GRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSER 3714
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7441 EYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLE---MIVGAFaim 7517
Cdd:PRK05691 3715 DYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDllgMIVGSF--- 3791
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7518 KAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRH--------LQECVSFD-GKVIAADDEQAYGEDGSNLEPVVGPNHL 7588
Cdd:PRK05691 3792 KAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAAcreqaralLDELGCANrPRLLVWEEVQAGEVASHNPGIYSGPDNL 3871
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7589 AYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPL 7668
Cdd:PRK05691 3872 AYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQG 3951
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7669 FESYMNENGITA-AILPPTYAIYLSPDR--LPSLKKLITGGSAASVEFVQQWKDkvRY-----FNAYGPTEAS---IVTS 7737
Cdd:PRK05691 3952 LLAHVQAQGITVlESVPSLIQGMLAEDRqaLDGLRWMLPTGEAMPPELARQWLQ--RYpqiglVNAYGPAECSddvAFFR 4029
                        4090      4100      4110      4120      4130      4140      4150      4160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7738 VWAASPDGLDLrsvPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLA-GERMYRT 7816
Cdd:PRK05691 4030 VDLASTRGSYL---PIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGApGERLYRT 4106
                        4170      4180      4190      4200      4210      4220      4230      4240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7817 GDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGqQQLCAYFVA-DRELTVSELRGT 7895
Cdd:PRK05691 4107 GDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLVPhQTVLAQGALLER 4185
                        4250      4260      4270      4280      4290      4300      4310      4320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7896 LSQ----ELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSMQTGADFVEPRTPVEAELARIWQEVLGIGPISVKDNF 7971
Cdd:PRK05691 4186 IKQrlraELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNF 4265
                        4330      4340      4350      4360
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 7972 FELGGHSLRATVLSSKVNKELNVNLPLRDIFRFPTVEALAQVIDGLE 8018
Cdd:PRK05691 4266 FELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLA 4312
PRK12316 PRK12316
peptide synthase; Provisional
4408-8025 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 2827.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4408 RHIFQFPTVEQLAEAIGQ--------------------------LEQQEFDAIPVV--EEREYYPVSSAQKRLYILQQLE 4459
Cdd:PRK12316 1494 REMFAEATVQRLADDYARelqaliehccdernrgvtpsdfplagLSQAQLDALPLPagEIADIYPLSPMQQGMLFHSLYE 1573
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4460 GAAQSYNMPGVMGLEGaLDRERFEETFRKLIARHETLRTGFELIDG--EPVQRIYPEVD--FAVETVQASEQEAKAI--- 4532
Cdd:PRK12316 1574 QEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIHKQVElpFAELDWRGREDLGQALdal 1652
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4533 -VRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGEELPGLRIQYKDYAVWqqseaq 4611
Cdd:PRK12316 1653 aQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAW------ 1726
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4612 keqLKRQEAYWLEAFRGE-LPVLEMPTDYAR----PAVQSYAGDTLDFrMNSEISEGLKRIAAESGATLYMVLLAAYTVL 4686
Cdd:PRK12316 1727 ---LQRQDAAASEAFWKEqLAALEEPTRLAQaartEDGQVGYGDHQQL-LDPAQTRALAEFARAQKVTLNTLVQAAWLLL 1802
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4687 LQKYTAQEDVIVGTPIAGRThADLQSL---IGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEELvdklQ 4763
Cdd:PRK12316 1803 LQRYTGQETVAFGATVAGRP-AELPGIeqqIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDI----Q 1877
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4764 MARDLSRNPLFDTMFSLQN---TENKEMHLP-GLHLTPyPTEYGMSKFDLSLdMMEDSEGLECSLEFATALYKRETIERM 4839
Cdd:PRK12316 1878 RWAGQGGEALFDSLLVFENypvAEALKQGAPaGLVFGR-VSNHEQTNYPLTL-AVTLGETLSLQYSYDRGHFDAAAIERL 1955
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4840 AKHFEQLLTAIVNDPAAKIASLGILTADEKAQIVHVFNPAAPDAPENEAFHALFEKQAECTPEAAAVVYENDRLTYRELN 4919
Cdd:PRK12316 1956 DRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELD 2035
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4920 ERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQ 4999
Cdd:PRK12316 2036 SRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLP 2115
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5000 QWGQTlqAALCLDDEAAYAEDAS-NVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQ 5078
Cdd:PRK12316 2116 LPAGV--ARLPLDRDAEWADYPDtAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPAD-CELQ 2192
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5079 LASFSFDVFVGDIARTLYNGGTMVIcpKDDRI-DPARLHYWISEEKITIFESTPALIIPFMDyVAEHGLDMSSMVLLITS 5157
Cdd:PRK12316 2193 FMSFSFDGAHEQWFHPLLNGARVLI--RDDELwDPEQLYDEMERHGVTILDFPPVYLQQLAE-HAERDGRPPAVRVYCFG 2269
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5158 SDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGEL 5237
Cdd:PRK12316 2270 GEAVPAASLRLAWEALRPV-YLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGEL 2348
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5238 CIGGIGVARGYLNRPELTEEKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEG 5316
Cdd:PRK12316 2349 YLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPA 2428
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5317 VREAVVVVREDAKGQKvLCAHFTAES--ELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASmQT 5394
Cdd:PRK12316 2429 VREAVVVAQDGASGKQ-LVAYVVPDDaaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVS-QL 2506
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5395 GMEYVAPRTPQEAKLVSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARM 5474
Cdd:PRK12316 2507 RQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESG 2586
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5475 EEQAYVSIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGE 5554
Cdd:PRK12316 2587 QTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQ 2666
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5555 PVQRVYKEVNFA---VEHYRTSEAEAGEVVRGFV-RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEE 5630
Cdd:PRK12316 2667 TRQVILPNMSLRivlEDCAGVADAAIRQRVAEEIqRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDE 2746
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5631 FGRMYNGES------LAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQL 5704
Cdd:PRK12316 2747 LVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVAL 2826
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5705 EPKLGEGLQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSF 5784
Cdd:PRK12316 2827 DVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDL 2906
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5785 LDEVKETMLGAYEHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEG 5864
Cdd:PRK12316 2907 LGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWES 2986
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5865 SEGLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEKEHIQRVFNATEAKYPSDKTIHQLFEEQ 5944
Cdd:PRK12316 2987 AEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQ 3066
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK12316 3067 VERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHlLDRASFADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVV-RL 6103
Cdd:PRK12316 3147 AYMLEDSGAQLLLSQSH-LRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSnHL 3225
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6104 VKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLT-APLYNQLSQQ 6182
Cdd:PRK12316 3226 CWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYpSMLQAFLEEE 3305
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6183 DSGMFAGLKTLIVGGDVLSVPHINRVLrehAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLS 6262
Cdd:PRK12316 3306 DAHRCTSLKRIVCGGEALPADLQQQVF---AGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLE 3382
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6263 LLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEI 6342
Cdd:PRK12316 3383 PVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEI 3462
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6343 EEQLLKVASVKEATVIVREDesgqKQLCAYFVAERELTI--GELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK12316 3463 EARLLEHPWVREAVVLAVDG----RQLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6421 PAPQGnAPVGAEYVAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTLaq 6500
Cdd:PRK12316 3539 PRPDA-ALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTI-- 3615
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6501 lsQHIQPVARM-----IDQGEVTGEIGLTPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTV 6575
Cdd:PRK12316 3616 --QGLARVARVgggvaVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLR 3693
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6576 FRKSENGYAAWNRAIGEGELYSLEvadfRDVKSAEqAVEAKANEIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVV 6654
Cdd:PRK12316 3694 FVEDAGGWTAEHLPVELGGALLWR----AELDDAE-ELERLGEEAQRSLDLADGPLLRALLATLADGSQrLLLVIHHLVV 3768
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6655 DGVSWRILLEDVALGYEQAAKGEEVRLPAKTDSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAPLPKDKQSDRSLQQ 6734
Cdd:PRK12316 3769 DGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSELPCDHPQGALQNR 3848
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6735 DSESITIQWSRKETEQLLKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDITRTVGWFTSKYP 6814
Cdd:PRK12316 3849 HAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFP 3928
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6815 VLLQmePGRSLSTRIKKVKEDLRRIPNKGIGYGLCRYLSAQPDGTVWGA--EPEISFNYLGQFDQDLSNNDIGLSPY--S 6890
Cdd:PRK12316 3929 VRLS--PVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGlpVPRITFNYLGQFDGSFDEEMALFVPAgeS 4006
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6891 SGLEMSDRQARSFILDINGMITDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAHCAAKEWTELTPSDVQLKGLTV 6970
Cdd:PRK12316 4007 AGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAERHGVTPSDFPLAGLDQ 4086
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6971 EELEQISAQtrnVGEIENIYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGsLDAEQFARSWNDLVARHAILRTNF-FS 7049
Cdd:PRK12316 4087 ARLDALPLP---LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQ 4162
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7050 GPRGEPLQIVYRDKRIGFVYEDLSHLPadERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDG 7129
Cdd:PRK12316 4163 GELGRPLQVVHKQVSLPFAELDWRGRA--DLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDG 4240
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7130 WCLPLVVKELFETYEAyvqgdRPEQKAAPAYSQYIEWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQ---KRSEGYvA 7206
Cdd:PRK12316 4241 WSNSQLLGEVLERYSG-----RPPAQPGGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARadlRSANGY-G 4314
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7207 EHVVcELDKELSERMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVAC 7286
Cdd:PRK12316 4315 EHVR-ELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATP 4393
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7287 QPEESFADVMGRMQEAALESGRYDFYPLYEIQTQSAQKQE-LINHLLVFENYPMDEQVEQAGgddSGTLSITDVDVAEHT 7365
Cdd:PRK12316 4394 RAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEaLFDSLLVFENYPVSEALQQGA---PGGLRFGEVTNHEQT 4470
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7366 NYNFTVTVFPGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHVFNNTAAEYARE 7445
Cdd:PRK12316 4471 NYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPAT 4550
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7446 QTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVP 7525
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7526 IDPEYPEDRIRYMLEDSGAQVLLTQRHLQE---------CVSFDgkviAADDEQAYGEdgSNLEPVVGPNHLAYVIYTSG 7596
Cdd:PRK12316 4631 LDPEYPRERLAYMMEDSGAALLLTQSHLLQrlpipdglaSLALD----RDEDWEGFPA--HDPAVRLHPDNLAYVIYTSG 4704
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7597 TTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPaKDTILDYPLFESYMNEN 7676
Cdd:PRK12316 4705 STGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIR-DDSLWDPERLYAEIHEH 4783
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7677 GITAAILPPTYAIYLSPD-----RLPSLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASP-DGLD 7747
Cdd:PRK12316 4784 RVTVLVFPPVYLQQLAEHaerdgEPPSLRVYCFGGEAVAQASYDLAWRAlkpVYLFNGYGPTETTVTVLLWKARDgDACG 4863
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7748 LRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLA-GERMYRTGDLARWLPDG 7826
Cdd:PRK12316 4864 AAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGApGGRLYRTGDLARYRADG 4943
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7827 NIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGqQQLCAYFVADRELTVS----------ELRGTL 7896
Cdd:PRK12316 4944 VIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVPQDPALADadeaqaelrdELKAAL 5022
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7897 SQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSMQTGAdFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGG 7976
Cdd:PRK12316 5023 RERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQA-YVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGG 5101
                        3690      3700      3710      3720
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 7977 HSLRATVLSSKVNKELNVNLPLRDIFRFPTVEALAQVIDGLEQEEHSAI 8025
Cdd:PRK12316 5102 HSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKF 5150
PRK05691 PRK05691
peptide synthase; Validated
259-4432 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 2782.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  259 DTTIHRLfEEQAERRPDAVAVTF------EDRQLTYGELNERANRLARTLRNAGVQADQLVgLMVERSLEMIVGIMGILK 332
Cdd:PRK05691    9 LTLVQAL-QRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  333 AGGAYVPIDP-----EYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWIRLDDEEAYHEDGSNLESVNG-------PE 400
Cdd:PRK05691   87 AGVIAVPAYPpesarRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAwqepalqPD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  401 HLTYVIYTSGTTGKPKGNLTTHRNII---RVVKNTNYIDVTGQDKLLQ-LSSYSFDGSTFDIFGALLNGAKLVLVPKETV 476
Cdd:PRK05691  167 DIAFLQYTSGSTALPKGVQVSHGNLVaneQLIRHGFGIDLNPDDVIVSwLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYF 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  477 LD--VAKLAGLIEkqqisvmfittafFNVLVDMNPDC---LRHARAILFGGERVSVSHVRKALG---------------- 535
Cdd:PRK05691  247 LErpLRWLEAISE-------------YGGTISGGPDFayrLCSERVSESALERLDLSRWRVAYSgsepirqdslerfaek 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  536 ----HLGPGKIKHVYGPTESTVF------------------ATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQN-KLQP 592
Cdd:PRK05691  314 faacGFDPDSFFASYGLAEATLFvsggrrgqgipaleldaeALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQSlEVLG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  593 IGVAGELCVAGDGLARGYLNRPDLTAEKFADNPfapGERMYRTGDLArWLPDGTIEYVGRIDDQVKIRGFRIELGEIEah 672
Cdd:PRK05691  394 DNRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-- 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  673 llklEAIEKATVVVRESangekQLCAYYVADRSLP----ANEVRSTLSQELPAYML---------------PSYFVQLE- 732
Cdd:PRK05691  468 ----KTVEREVEVVRKG-----RVAAFAVNHQGEEgigiAAEISRSVQKILPPQALiksirqavaeacqeaPSVVLLLNp 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  733 -QMPLTTNGKVDRRA--LPAPEESMETGVEFVEPRT-----------ELEAGIVNIWKEILKIEKISVKDSFFELGGHSL 798
Cdd:PRK05691  539 gALPKTSSGKLQRSAcrLRLADGSLDSYALFPALQAveaaqtaasgdELQARIAAIWCEQLKVEQVAADDHFFLLGGNSI 618
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  799 RATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISGM---GEQVYSSIPAAEAREYYPLSSAQKRLYILHQLEGAEQSY 875
Cdd:PRK05691  619 AATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQlagGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAY 698
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  876 NLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVEHI---RANEEEADAAVKQfIRA--- 949
Cdd:PRK05691  699 NIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIdlsDLPEAEREARAAQ-IREeea 777
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  950 ---FDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGE------DLPALRIQYKDYAVWQQSEA 1020
Cdd:PRK05691  778 rqpFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWQRQWL 857
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1021 QKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATLYMVLLAAYTILLQKY 1100
Cdd:PRK05691  858 AQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRY 937
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1101 TGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFEELVDKLKLARDlsr 1180
Cdd:PRK05691  938 SGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQARE--- 1014
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1181 NPLFDTMFTLQNTENKEF-RLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFLC-GIEYATALYKRETIERMAKHFEQLLT 1258
Cdd:PRK05691 1015 QGLFQVMFNHQQRDLSALrRLPGLLAEELPWHSREAKFDLQLHSEEDRNGRLTlSFDYAAELFDAATIERLAEHFLALLE 1094
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1259 AIVNNPAAKIASLGILTVEEKAQLVHVfnPAAPDAPENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARM 1338
Cdd:PRK05691 1095 QVCEDPQRALGDVQLLDAAERAQLAQW--GQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHY 1172
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1339 LRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQwgqtlqav 1418
Cdd:PRK05691 1173 LRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQ-------- 1244
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1419 lcLDDEAAYAEDASNVAN--VNEP------HDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVrLLQLA 1490
Cdd:PRK05691 1245 --AEGVSAIALDSLHLDSwpSQAPglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDV-LMQKA 1321
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1491 SFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLdmSSMELLITSSDS 1570
Cdd:PRK05691 1322 PISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAAC--TSLRRLFSGGEA 1399
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1571 CSVT-DYRVLQERFGSQFRiiNAYGVTEAAIDSSLYDeplAKLPEAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCI 1649
Cdd:PRK05691 1400 LPAElRNRVLQRLPQVQLH--NRYGPTETAINVTHWQ---CQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCI 1474
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1650 GGIGVARGYLNRPELTEEKFVDSPFVE-GERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVR 1728
Cdd:PRK05691 1475 GGAGLARGYLGRPALTAERFVPDPLGEdGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVA 1554
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1729 EAVVVVREDAKGQKvLCAYFTAE--SELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDasMQTGm 1806
Cdd:PRK05691 1555 QAAVLVREGAAGAQ-LVGYYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV--WQQR- 1630
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1807 EYVAPRTPQEAKLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIARMEE 1886
Cdd:PRK05691 1631 EHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQA 1710
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1887 QAYVS----IPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN 1962
Cdd:PRK05691 1711 AGERNsqgaIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVD 1790
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1963 GEPVQRVYKE--VNFAVEHYRTSEAEAGE------VVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMST 2034
Cdd:PRK05691 1791 GVPVQQVAEDsgLRMDWQDFSALPADARQqrlqqlADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAM 1870
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2035 DVLTEEFGRLYNG-----ES-LATLRIQYKDYAVWQ-QSEEQLERvKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEG 2107
Cdd:PRK05691 1871 DIFARELGALYEAflddrESpLEPLPVQYLDYSVWQrQWLESGER-QRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRG 1949
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2108 STLSFRLDAGLNEALKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAG 2187
Cdd:PRK05691 1950 ELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDG 2029
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2188 GKTFRSFLEEVKETTLGAYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTE-NEELQLDGLKLAPYPSGNTIARFD 2266
Cdd:PRK05691 2030 QMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQSRQLAGMTVEYLVNDARATKFD 2109
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2267 LTLDVTETGSGLECNLEYATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQTQLHHVFNATAADYEADKT 2346
Cdd:PRK05691 2110 LNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQT 2189
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2347 IHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPID 2426
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2427 PEYPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTV----DDEQAYAG-DGSNLESAVGPNDLAYIIYTSGTTGKPK 2501
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARwcleDDAAALAAySDAPLPFLSLPQHQAYLIYTSGSTGKPK 2349
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2502 GVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKEtildyQW----FERYMSDNGI 2577
Cdd:PRK05691 2350 GVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQG-----QWgaeeICQLIREQQV 2424
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2578 TTATLPPTY----AVYL--NPDHMPdFKRLIAAGSASSLELLQQWKDKVK---YFNAYGPTEdSICTTIWTPSTEDISQ- 2647
Cdd:PRK05691 2425 SILGFTPSYgsqlAQWLagQGEQLP-VRMCITGGEALTGEHLQRIRQAFApqlFFNAYGPTE-TVVMPLACLAPEQLEEg 2502
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2648 LKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEP-GERMYRTGDLAKWLPDG 2726
Cdd:PRK05691 2503 AASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADG 2582
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2727 TIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGqKQLCAYFVADRTMTVGE--------LRGELSG 2798
Cdd:PRK05691 2583 LVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSG-KQLAGYLVSAVAGQDDEaqaalreaLKAHLKQ 2661
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2799 ELPGYMIPAHFVQLERMPLTPNGKIDRKALPAPQgNASAGADYVAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDS 2878
Cdd:PRK05691 2662 QLPDYMVPAHLILLDSLPLTANGKLDRRALPAPD-PELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDS 2740
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2879 IKSIQVSSRLHQAGYKLEIRDLFKYPTVAQLSKHIRPVARM-ADQGEVSGDVSLTPIQHWFFEPQFAEPHHFNQSVMLHR 2957
Cdd:PRK05691 2741 ILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAqAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEP 2820
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2958 RDGFDEAAIRKVLQKLVEHHDALRVVFHKSENGYTAWNRAIGEGELygLEVVDLKGIEEsAQAVEAKAneiQSSIDLEAG 3037
Cdd:PRK05691 2821 RQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQEL--LWQVTVADFAE-CAALFADA---QRSLDLQQG 2894
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3038 PFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYRTWSEQLAAYAQSPVIEREL 3116
Cdd:PRK05691 2895 PLLRALLVDGPQGQQrLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREEL 2974
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3117 AYWKRVAQTEVQPLPKDEQVDVSLQQDSESISIEWTREETEQLLKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNL 3196
Cdd:PRK05691 2975 GWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQL 3054
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3197 EGHGRESIMTDIDITRTVGWFTSKYPVVLELEQGKDISYL--LKKTKEDLRGIPNKGIGYGICRYLSAAKNDIAWGAEPE 3274
Cdd:PRK05691 3055 EGHGREALFDDIDLTRSVGWFTSAYPLRLTPAPGDDAARGesIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQ 3134
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3275 --VSFNYLGQFDQDLQNSDIGVSAHTGGKQSSDRQKRI-FVLDINGMIADGTLSLELSYNGKEYRRETMERLAASLQESL 3351
Cdd:PRK05691 3135 apITFNYLGQFDQSFASDALFRPLDEPAGPAHDPDAPLpNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAEL 3214
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3352 RVIIAHCVSKERAELTPSDVQFKGLSVEELEQISGQTQHlgdIENIYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGA 3431
Cdd:PRK05691 3215 QALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAE---IEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSA 3291
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3432 LNIELFSRSWNELAARHAVLRTNFhsGWR-GEP-LQIVYRYKPVEFAYEDLRHLAEAEWSAYLDQLVNDDKTRGFDLEQD 3509
Cdd:PRK05691 3292 LDPERFAQAWQAVVARHEALRASF--SWNaGETmLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQ 3369
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3510 ALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLRNDLSERPAAPSYSHYIEWLEKQDMEAAARYWTG 3589
Cdd:PRK05691 3370 PPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQD 3449
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3590 FLAGYDSQTTLPQGK--LHNKDGE---------YTEanilrsLGKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGT 3658
Cdd:PRK05691 3450 NLRGFERPTPIPSDRpfLREHAGDsggmvvgdcYTR------LDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGD 3523
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3659 DDAVFGSVVSGRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADV---MKRVQEAALESGGYDYYPLYEIQAQS--AQKQ 3733
Cdd:PRK05691 3524 RDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLPAAGQRCSVrqwLQGLLDSNMELREYEYLPLVAIQECSelPKGQ 3603
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3734 DLITHIMAFENFPMDEQI-EQAGSyedgkLAITDVDIAEQTNYDFTLVVMPGEELAVRFYYNASVYEHSAMERLMGHLIH 3812
Cdd:PRK05691 3604 PLFDSLFVFENAPVEVSVlDRAQS-----LNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKR 3678
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3813 VLEQVTASPNAPVSMLELVTEAEKAEIIHVFNNTAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRL 3892
Cdd:PRK05691 3679 LLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRL 3758
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3893 ARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRE--RVSFAGT 3970
Cdd:PRK05691 3759 GHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREqaRALLDEL 3838
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3971 FVAVDD-----EQAYHADGSNLEPVV--GPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFAS 4043
Cdd:PRK05691 3839 GCANRPrllvwEEVQAGEVASHNPGIysGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTAS 3918
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4044 LSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITA-TILPPTYAAYLNPDRMP--SLKKLITGGSAASVE 4120
Cdd:PRK05691 3919 QSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVlESVPSLIQGMLAEDRQAldGLRWMLPTGEAMPPE 3998
                        4090      4100      4110      4120      4130      4140      4150      4160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4121 FVQQWKDK---VLYFNAYGPTEASIVTSIW--DEASdslgDRKS-VPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGV 4194
Cdd:PRK05691 3999 LARQWLQRypqIGLVNAYGPAECSDDVAFFrvDLAS----TRGSyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGT 4074
                        4170      4180      4190      4200      4210      4220      4230      4240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4195 GLARGYLNRPELTAEKFVDNPF-EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAI 4273
Cdd:PRK05691 4075 GVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA 4154
                        4250      4260      4270      4280      4290      4300      4310      4320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4274 VLAREDANGqQQLVAYFVA-QRELTAAELRATMSQ----ELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPEGSMHAGG 4348
Cdd:PRK05691 4155 VAVQEGVNG-KHLVGYLVPhQTVLAQGALLERIKQrlraELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQ 4233
                        4330      4340      4350      4360      4370      4380      4390      4400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4349 EYVAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQFPTVEQLAEAIGQLEQ 4428
Cdd:PRK05691 4234 AYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAG 4313

                  ....
gi 386647928 4429 QEFD 4432
Cdd:PRK05691 4314 SAID 4317
PRK12316 PRK12316
peptide synthase; Provisional
5449-8459 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 2545.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5449 MNVE--LPLRDVFRCSTVEEMAQAIARMEEQ----AYVSIPT-VEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVL 5521
Cdd:PRK12316    1 MNAEdsLKLARRFIELPLEKRRVFLATLRGEgvdfSLFPIPAgVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5522 EGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYRTS---EAE-----AGEVVRGFVRTFDLAKP 5593
Cdd:PRK12316   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSglpEAEqearlRDEAQRESLQPFDLCEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5594 PLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGES------LAPLRIQYKDYATWQQSEAQQEQMKRQE 5667
Cdd:PRK12316  161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYAtgaepgLPALPIQYADYALWQRSWLEAGEQERQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5668 AYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVG 5747
Cdd:PRK12316  241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5748 TPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAYEHQSYPFEELVEKAQPARDLSRNPLFDTLFA 5827
Cdd:PRK12316  321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5828 LQN---KETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSEGLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAPEA 5904
Cdd:PRK12316  401 HQPlvaDIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5905 PLASLEMITAEEKEHIQRVFNATEAKYPSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQP 5984
Cdd:PRK12316  481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5985 DQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLN-DDGAYHE 6063
Cdd:PRK12316  561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDlDRPAAWL 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6064 DG---SNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVV-RLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLN 6139
Cdd:PRK12316  641 EGyseENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSnRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6140 GGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLsQQDSGM--FAGLKTLIVGGDVLSVPHINRVLREHAGLSI 6217
Cdd:PRK12316  721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAF-LQDEDVasCTSLRRIVCSGEALPADAQEQVFAKLPQAGL 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6218 VNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVES 6297
Cdd:PRK12316  800 YNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPS 879
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6298 SFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREdesgQKQLCAYFVAER 6377
Cdd:PRK12316  880 PFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLES 955
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6378 E--LTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPAPQGNAPvGAEYVAPRTEQEKALAAVWQAVLGAE 6455
Cdd:PRK12316  956 EggDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVA-QQGYVAPRNALERTLAAIWQDVLGVE 1034
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6456 RVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTLAQLSQhiqpVAR-----MIDQGEVTGEIGLTPIQRWF 6530
Cdd:PRK12316 1035 RVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLAL----VAKagqatAADQGPASGEVALAPVQRWF 1110
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6531 FDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGY-AAWNRAIGEGELYSLEVADfrdvksa 6609
Cdd:PRK12316 1111 FEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWqQAYAAPQAGEVLWQRQAAS------- 1183
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6610 EQAVEAKANEIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQAakgeEVRLPAKTDSF 6688
Cdd:PRK12316 1184 EEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQrLLLVIHHLVVDGVSWRILLEDLQRAYADL----DADLPARTSSY 1259
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6689 RTWSEQLAAYAQSPAmeNERAYWEQIAQTAVAPLPKDKQSDRSLQQDSESITIQWSRKETEQLLKKVHRAYNTEMNDILL 6768
Cdd:PRK12316 1260 QAWARRLHEHAGARA--EELDYWQAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLL 1337
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6769 TALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDITRTVGWFTSKYPVLLQmePGRSLSTRIKKVKEDLRRIPNKGIGYGL 6848
Cdd:PRK12316 1338 TALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGWFTSLFPVRLT--PAADLGESIKAIKEQLRAVPDKGIGYGL 1415
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6849 CRYLSAQPDGTVWGA--EPEISFNYLGQFDQDLSNNDIGLSPYSSGLEMSDRQAR-SFILDINGMITDGSLALELSYSRK 6925
Cdd:PRK12316 1416 LRYLAGEEAAARLAAlpQPRITFNYLGQFDRQFDEAALFVPATESAGAAQDPCAPlANWLSIEGQVYGGELSLHWSFSRE 1495
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6926 EYHRETVEELAGMLQESLQEIIAHCAAKEWTELTPSDVQLKGLTVEELEQISAQTrnvGEIENIYTLTPMQKGMWFHTAL 7005
Cdd:PRK12316 1496 MFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDFPLAGLSQAQLDALPLPA---GEIADIYPLSPMQQGMLFHSLY 1572
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7006 DKEAGAYFEQMRFTVQGsLDAEQFARSWNDLVARHAILRTNF-FSGPRGEPLQIVYRDKRIGFVYEDLShlPADERQASV 7084
Cdd:PRK12316 1573 EQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFlWQDGLEQPLQVIHKQVELPFAELDWR--GREDLGQAL 1649
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7085 ERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAyvqgdRPEQKAAPAYSQYI 7164
Cdd:PRK12316 1650 DALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-----QPVAAPGGRYRDYI 1724
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7165 EWLENQDSAAASAYWSNYLAGYEGQTALPQE-KAQKRSEGYvAEHVVcELDKELSERMNRAAKQCRVTVNTLMQAVWGVI 7243
Cdd:PRK12316 1725 AWLQRQDAAASEAFWKEQLAALEEPTRLAQAaRTEDGQVGY-GDHQQ-LLDPAQTRALAEFARAQKVTLNTLVQAAWLLL 1802
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7244 LQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALESGRYDFYPLYEIQTQSAQ 7323
Cdd:PRK12316 1803 LQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQ 1882
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7324 KQE-LINHLLVFENYPMDEQVEQagGDDSGtLSITDVDVAEHTNYNFTVTVFPGDEIVVRFDYNSFVFERADMERLKGHL 7402
Cdd:PRK12316 1883 GGEaLFDSLLVFENYPVAEALKQ--GAPAG-LVFGRVSNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHL 1959
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7403 LHMLEQIVADPQASVGGLELATAAEKVEIIHVFNNTAAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERAN 7482
Cdd:PRK12316 1960 LHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRAN 2039
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7483 RLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQE------- 7555
Cdd:PRK12316 2040 RLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLErlplpag 2119
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7556 --CVSFDgkviAADDEQAYGEdgSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQF 7633
Cdd:PRK12316 2120 vaRLPLD----RDAEWADYPD--TAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQF 2193
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7634 ASLSFDASCWEIFKALFFGATLYIpAKDTILDYPLFESYMNENGITAAILPPTYAIYLSPD-----RLPSLKKLITGGSA 7708
Cdd:PRK12316 2194 MSFSFDGAHEQWFHPLLNGARVLI-RDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHaerdgRPPAVRVYCFGGEA 2272
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7709 ASVEFVQQWK---DKVRYFNAYGPTEASIVTSVWAASP-DGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISG 7784
Cdd:PRK12316 2273 VPAASLRLAWealRPVYLFNGYGPTEAVVTPLLWKCRPqDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGG 2352
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7785 AGLARGYLNRPELTAEKFVDNPFLA-GERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQET 7863
Cdd:PRK12316 2353 EGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREA 2432
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7864 IVIARGDANGqQQLCAYFVAD--RELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSMQTGAdF 7941
Cdd:PRK12316 2433 VVVAQDGASG-KQLVAYVVPDdaAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQA-Y 2510
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7942 VEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVNKELNVNLPLRDIFRFPTVEALAQVIDGLEQEE 8021
Cdd:PRK12316 2511 VAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSR 2590
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8022 HSAIPVIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEmANGEPVQR 8101
Cdd:PRK12316 2591 APVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFV-EVGEQTRQ 2669
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8102 VYSDV---EFAVEYSKADREEAVE--IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSR 8176
Cdd:PRK12316 2670 VILPNmslRIVLEDCAGVADAAIRqrVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQ 2749
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8177 LYAGE------ELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEA 8250
Cdd:PRK12316 2750 AYAGArrgeqpTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVA 2829
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8251 LTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEE 8330
Cdd:PRK12316 2830 LSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQ 2909
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8331 VKETTLGAFEHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTvAAQFDLTLSVAEDDG 8410
Cdd:PRK12316 2910 VKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGA-ATQFDLALDTWESAE 2988
                        3050      3060      3070      3080
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 8411 AIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQLNEPE 8459
Cdd:PRK12316 2989 GLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAE 3037
PRK12467 PRK12467
peptide synthase; Provisional
3404-6009 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1754.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3404 QKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYKPVEFAYEDLRHL 3483
Cdd:PRK12467   56 QERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQD-EEGFRQVIDASLSLTIPLDDLANE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3484 AEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESfHVL-WSFHHILMDGWCLPLIAKELFDTYEAYLRNDLSER 3562
Cdd:PRK12467  135 QGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDE-HVLvVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSL 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3563 PAAP-SYSHYI----EWLEKQDMEAAARYWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERMSRIAKQHQ 3637
Cdd:PRK12467  214 PALPiQYADYAiwqrSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREG 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3638 VTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEiaGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAALESGGY 3717
Cdd:PRK12467  294 VTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--ETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAH 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3718 DYYPlYEIQAQSAQKQDLITHIMAFENFPMDEQIEQAGSYEDGK----LAITDVDIAEQT-NYDFTLVVMPGEE-LAVRF 3791
Cdd:PRK12467  372 QDLP-FEQLVEALQPERSLSHSPLFQVMFNHQNTATGGRDREGAqlpgLTVEELSWARHTaQFDLALDTYESAQgLWAAF 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3792 YYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAEIIHVFNNTAAEYQQeQTIHGLFEEQALRNPDAV 3871
Cdd:PRK12467  451 TYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAP-DCVHQLIEAQARQHPERP 529
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3872 AVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSG 3951
Cdd:PRK12467  530 ALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSG 609
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3952 AQALLTQRHLRERVSFAGTFVAV----DDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 4027
Cdd:PRK12467  610 VRLLLTQSHLLAQLPVPAGLRSLcldePADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA 689
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4028 NTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAYL----NPDR 4103
Cdd:PRK12467  690 ERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALlqasRVAL 769
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4104 MPSLKKLITGGSAASVEFVQQWK---DKVLYFNAYGPTEASIVTSIWdEASDSLGDRKSVPIGRPLANHRIYVVDSHNRM 4180
Cdd:PRK12467  770 PRPQRALVCGGEALQVDLLARVRalgPGARLINHYGPTETTVGVSTY-ELSDEERDFGNVPIGQPLANLGLYILDHYLNP 848
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4181 LPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEP-GERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEV 4259
Cdd:PRK12467  849 VPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEI 928
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4260 ETQLAKIDAVQEAIVLArEDANGQQQLVAYFVAQRELTAA-------ELRATMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK12467  929 EARLLAQPGVREAVVLA-QPGDAGLQLVAYLVPAAVADGAehqatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4333 DRKALPAPEGSMhAGGEYVAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQ 4412
Cdd:PRK12467 1008 DRKALPKPDASA-VQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFE 1086
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4413 FPTVEQLAEAIGQLEQQEFDAIPVVEEREYYPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIAR 4492
Cdd:PRK12467 1087 HQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVAR 1166
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4493 HETLRTGFELIDGEPVQRIYP--EVDFAVETVQAS---EQEAKAIV-RDFIRPFDLAKPPLLRVGLIELAPERCILMLDM 4566
Cdd:PRK12467 1167 HESLRTTFVQEDGRTRQVIHPvgSLTLEEPLLLAAdkdEAQLKVYVeAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTL 1246
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4567 HHIVSDGVSADVLVEEFARLYSGE------ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYA 4640
Cdd:PRK12467 1247 HHIVSDGWSMQVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRP 1326
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4641 RPAVQSYAGDTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNT 4720
Cdd:PRK12467 1327 RPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNT 1406
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4721 LAIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEMH-LPGLHLTPYP 4799
Cdd:PRK12467 1407 QVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAqLPGLSVESLS 1486
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4800 TEYGMSKFDLSLDMMEDSEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIASLGILTADEKAQIVHVFNPA 4879
Cdd:PRK12467 1487 WESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNAT 1566
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4880 APDAPENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWK 4959
Cdd:PRK12467 1567 HTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILK 1646
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4960 AGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQwGQTLQaALCLDDEAAYAE--DASNVANVNEPHDLAYVI 5037
Cdd:PRK12467 1647 AGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPL-PDGLR-SLVLDQEDDWLEgySDSNPAVNLAPQNLAYVI 1724
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5038 YTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVrLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHY 5117
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADV-VLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQ 1803
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5118 WISEEKITIFESTPALIIPFMDyVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQFrIINAYGVTEAAIDSSLYDE 5197
Cdd:PRK12467 1804 LIERQQVTTLHFVPSMLQQLLQ-MDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTG-LFNLYGPTETAVDVTHWTC 1881
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5198 PLAKLPEAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPF-VEGERLYRTGDL 5276
Cdd:PRK12467 1882 RRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDL 1961
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5277 ARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKaEGVREAVVVVREDAKGQKVLCAHFTAESELKL---------- 5346
Cdd:PRK12467 1962 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLRE-QGGVREAVVIAQDGANGKQLVAYVVPTDPGLVdddeaqvalr 2040
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5347 SELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDAS-MQTGmeYVAPRTPQEAKLVSIWQEVLGLEKVGVK 5425
Cdd:PRK12467 2041 AILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASeLQQA--YVAPQSELEQRLAAIWQDVLGLEQVGLH 2118
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5426 DNFFELGGHSLRATLLVGKVhKEMNVELPLRDVFRCSTVEEMAqAIARmEEQAYVSIPTVEEREYYPVSSAQKRLYILHQ 5505
Cdd:PRK12467 2119 DNFFELGGDSIISIQVVSRA-RQAGIRFTPKDLFQHQTVQSLA-AVAQ-EGDGTVSIDQGPVTGDLPLLPIQQMFFADDI 2195
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5506 LEgaEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGE------PVQRVYKEVNFAVEHYRTSEAEA-G 5578
Cdd:PRK12467 2196 PE--RHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGwsamhrAPEQERRPLLWQVVVADKEELEAlC 2273
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5579 EVVRgfvRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEE----FGRMYNGESLA-PLRIQ-YKDYAT 5652
Cdd:PRK12467 2274 EQAQ---RSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDlqtaYRQLQGGQPVKlPAKTSaFKAWAE 2350
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5653 WQQSEAQQEQMKRQEAYWLDMFRGeLPVlELPTDYPRPAV-RKFEGSL---LQRQLEPKLgegLQRIAAESGATLYMVLL 5728
Cdd:PRK12467 2351 RLQTYAASAALADELGYWQAQLQG-AST-ELPCDHPQGGLqRRHAASVtthLDSEWTRRL---LQEAPAAYRTQVNDLLL 2425
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5729 AAYKVLLQKYTGQEDIVVGTPIAGRTH----SDLQPIIGMFVNTLAIRSYPDDK-----KTFRSFLDEV--KETMLGAYE 5797
Cdd:PRK12467 2426 TALARVIARWTGQASTLIQLEGHGREDlfdeIDLTRTVGWFTSLYPVKLSPTASlatsiKTIKEQLRAVpnKGLGFGVLR 2505
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5798 HQSYPFEELVEKAQPARDLSRNPL--FDTLFalqnkETGELQLDGLRLTPYPAEHT-VAKFD--LSVDVTEGSEGLELSM 5872
Cdd:PRK12467 2506 YLGSEAARQTLQALPVPRITFNYLgqFDGSF-----DAEKQALFVPSGEFSGAEQSeEAPLGnwLSINGQVYGGELNLGW 2580
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5873 EYSTALYTRETIERMAKHFEQLLTAIVqapeaplaslemitaeekEHIqrVFNATEAKYPSDKTIHQLFEEQAERIPdhl 5952
Cdd:PRK12467 2581 TFSQEMFDEATIQRLADAYAEELRALI------------------EHC--CSNDQRGVTPSDFPLAGLSQEQLDRLP--- 2637
                        2650      2660      2670      2680      2690      2700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 5953 aVTFEDKQLTYGELNERANRLARTL--RNAGVQPDQMV----GLMVER---SLEMVVGMIAILKAG 6009
Cdd:PRK12467 2638 -VAVGDIEDIYPLSPMQQGMLFHTLyeGGAGDYINQMRvdveGLDVERfrtAWQAVIDRHEILRSG 2702
PRK12467 PRK12467
peptide synthase; Provisional
7-2156 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1613.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    7 ERETAFWNKIFeGEENPPTALPyskAQKQAPALV----RRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYT 82
Cdd:PRK12467  237 ERQLAYWQEQL-GGEHTVLELP---TDRPRPAVPsyrgARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYS 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   83 SSSSILVGMPVVtkpNENRRPVNQLV-------ILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYAD 155
Cdd:PRK12467  313 GQSDIRIGVPNA---NRNRVETERLIgffvntqVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  156 G-------------------VPVVNTLVALKQLHITDYRQSAVSDVLFEFELDKDEVRLHLTYNGNLYTESFIAQAVDHL 216
Cdd:PRK12467  390 ShsplfqvmfnhqntatggrDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHW 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  217 NRLFSVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTtIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERAN 296
Cdd:PRK12467  470 RNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDC-VHQLIEAQARQHPERPALVFGEQVLSYAELNRQAN 548
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  297 RLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQER----VS 372
Cdd:PRK12467  549 RLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQlpvpAG 628
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  373 FSGTWIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNT-NYIDVTGQDKLLQLSSYSF 451
Cdd:PRK12467  629 LRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIaERLQLAADDSMLMVSTFAF 708
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  452 DGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLV-DMNPDCLRHARAILFGGERVSVSHV 530
Cdd:PRK12467  709 DLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLqASRVALPRPQRALVCGGEALQVDLL 788
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  531 RKALgHLGPG-KIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARG 609
Cdd:PRK12467  789 ARVR-ALGPGaRLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARG 867
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  610 YLNRPDLTAEKFADNPFAP-GERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKAtVVVRE 688
Cdd:PRK12467  868 YHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREA-VVLAQ 946
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  689 SANGEKQLCAYYVADRSLPA-------NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGVeFV 761
Cdd:PRK12467  947 PGDAGLQLVAYLVPAAVADGaehqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQAT-FV 1025
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  762 EPRTELEAGIVNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISGMGEQVY 841
Cdd:PRK12467 1026 APQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQ 1105
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  842 SSIPAAEAREYYPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRI 921
Cdd:PRK12467 1106 PALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVI 1185
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  922 YPEVEFAVEH-IRANEEEADAAVKQFI-----RAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFAR 995
Cdd:PRK12467 1186 HPVGSLTLEEpLLLAADKDEAQLKVYVeaearQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVA 1265
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  996 LYGGE------DLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQ 1069
Cdd:PRK12467 1266 LYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPA 1345
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1070 KREGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLED 1149
Cdd:PRK12467 1346 LAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQ 1425
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1150 VKETTLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEFR-LPGLQLTPYPVEEHTSKFDLSLDIMESGD 1228
Cdd:PRK12467 1426 VKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAqLPGLSVESLSWESQTAQFDLTLDTYESSE 1505
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1229 GFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEEKAQLVHVFNPAAPDAPENEVFHALFEKQAE 1308
Cdd:PRK12467 1506 GLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAA 1585
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1309 RTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQF 1388
Cdd:PRK12467 1586 ATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAY 1665
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1389 MLEDSAASVLLTQTHLQERAQQwGQTLQAVLcLDDEAAYAE--DASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSL 1466
Cdd:PRK12467 1666 MIEDSGIELLLTQSHLQARLPL-PDGLRSLV-LDQEDDWLEgySDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL 1743
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1467 VNTAAGYRREYRLDQFPVrLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIP 1546
Cdd:PRK12467 1744 VNRLCATQEAYQLSAADV-VLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQ 1822
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1547 FMDyVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQFrIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALN 1626
Cdd:PRK12467 1823 LLQ-MDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTG-LFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIAN 1900
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1627 AKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQA 1705
Cdd:PRK12467 1901 LSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQV 1980
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1706 KIRGYRIETGEIETQLLKaEGVREAVVVVREDAKGQKVLCAYFTAESELKL----------SELRSSLSQELPGYMIPSY 1775
Cdd:PRK12467 1981 KIRGFRIELGEIEARLRE-QGGVREAVVIAQDGANGKQLVAYVVPTDPGLVdddeaqvalrAILKNHLKASLPEYMVPAH 2059
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1776 FVQLEQLPLTANGKIDRKALPAPDAS-MQTGmeYVAPRTPQEAKLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGK 1854
Cdd:PRK12467 2060 LVFLARMPLTPNGKLDRKALPAPDASeLQQA--YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSR 2137
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1855 VhKEMNVELPLRDVFRCSTVEEMAqAIARmEEQAYVSIPTVEEREYYPVSSAQKRLYILHQLEgaEQSYNMTGELVLEGI 1934
Cdd:PRK12467 2138 A-RQAGIRFTPKDLFQHQTVQSLA-AVAQ-EGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPE--RHHWNQSVLLEPREA 2212
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1935 LDRGKLEEAFRQLIARHETLRTGFELVNGE------PVQRVYKEVNFAVEHYRTSEAEA-GEVVRgfvRTFDLAKPPLLR 2007
Cdd:PRK12467 2213 LDAELLEAALQALLVHHDALRLGFVQEDGGwsamhrAPEQERRPLLWQVVVADKEELEAlCEQAQ---RSLDLEEGPLLR 2289
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2008 VGLVELAEDLHILLLDMHHIVSDGMSTDVLTEE----FGRLYNGESLAtLRIQYKDYAVWQQSEEQLERVKRQE---AYW 2080
Cdd:PRK12467 2290 AVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDlqtaYRQLQGGQPVK-LPAKTSAFKAWAERLQTYAASAALAdelGYW 2368
                        2170      2180      2190      2200      2210      2220      2230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 2081 LDMFRGeLPVlEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAESGAT-LYMVLLAAYNVMLQKYTGQEDIVI 2156
Cdd:PRK12467 2369 QAQLQG-AST-ELPCDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTqVNDLLLTALARVIARWTGQASTLI 2443
PRK12316 PRK12316
peptide synthase; Provisional
191-2186 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1447.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  191 DEVRLHLTYNGNLYTESFIAQAVDHLNRLFSVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQA 270
Cdd:PRK12316 1934 ETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQA 2013
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  271 ERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIR 350
Cdd:PRK12316 2014 ARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLA 2093
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  351 YMLEDSGTQVLLSQGHLQERVSFSGTWIRLD-DEEAYHED--GSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNII- 426
Cdd:PRK12316 2094 YMLEDSGAALLLTQRHLLERLPLPAGVARLPlDRDAEWADypDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVa 2173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  427 RVVKNTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPkETVLDVAKLAGLIEKQQISVMFITTAFFNVL-- 504
Cdd:PRK12316 2174 HCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRD-DELWDPEQLYDEMERHGVTILDFPPVYLQQLae 2252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  505 ---VDMNPDCLrhaRAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDV-HEVEEGAVSIPIGGPISNTA 580
Cdd:PRK12316 2253 haeRDGRPPAV---RVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCrPQDPCGAAYVPIGRALGNRR 2329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  581 IYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKI 659
Cdd:PRK12316 2330 AYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKI 2409
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  660 RGFRIELGEIEAHLLKLEAIEKATVVVRESANGeKQLCAYYVAD--RSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLT 737
Cdd:PRK12316 2410 RGFRIELGEIEARLQAHPAVREAVVVAQDGASG-KQLVAYVVPDdaAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLN 2488
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  738 TNGKVDRRALPAPEESMETGVeFVEPRTELEAGIVNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPL 817
Cdd:PRK12316 2489 PNGKLDRKALPKPDVSQLRQA-YVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPL 2567
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  818 RDVFRYPTVEKLAEAISGMGEQVYSSIPAAEAREYYPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFR 897
Cdd:PRK12316 2568 RILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFD 2647
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  898 ALIARHETLRTGIEMVGGEPMQRIYPEV---EFAVEHIRANEEEADAAVKQFI-RAFDLAKPPLLRVGLIELAPERHLLM 973
Cdd:PRK12316 2648 ALVLRHETLRTRFVEVGEQTRQVILPNMslrIVLEDCAGVADAAIRQRVAEEIqRPFDLARGPLLRVRLLALDGQEHVLV 2727
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  974 FDMHHIVSDGISMDVLVEEFARLYGGED------LPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPT 1047
Cdd:PRK12316 2728 ITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPL 2807
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1048 DYARPAVQSYAGNALRFELDAQKREGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMF 1127
Cdd:PRK12316 2808 DRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFF 2887
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1128 VNTLAIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEFRLPGLQLTP 1207
Cdd:PRK12316 2888 VNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIES 2967
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1208 YPVEEHTSKFDLSLDIMESGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEEKAQLVHVFN 1287
Cdd:PRK12316 2968 FAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWN 3047
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1288 PAAPDAPENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAV 1367
Cdd:PRK12316 3048 ATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAI 3127
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1368 WKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQtlqaVLCLDDEAAYAEDAsNVANVNEPHDLAYVI 1447
Cdd:PRK12316 3128 LKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQ----VLDLDRGDENYAEA-NPAIRTMPENLAYVI 3202
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1448 YTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHY 1527
Cdd:PRK12316 3203 YTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGV-GDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVE 3281
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1528 WISEEKITIFESTPALIIPFMDYVAEHglDMSSMELLITSSDSCSVTdyrvLQERFGSQFRIINAYGVTEAAIDSSLYDe 1607
Cdd:PRK12316 3282 LINSEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPAD----LQQQVFAGLPLYNLYGPTEATITVTHWQ- 3354
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1608 plAKLPEAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLA 1687
Cdd:PRK12316 3355 --CVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLA 3432
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1688 RWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGvreAVVVVREDAKGQKVLCAYFTAESELKLSE-LRSSLSQE 1766
Cdd:PRK12316 3433 RYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPW---VREAVVLAVDGRQLVAYVVPEDEAGDLREaLKAHLKAS 3509
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1767 LPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASM-QTGmeYVAPRTPQEAKLASIWQEVLGLEKVGVKDNFFELGGHS 1845
Cdd:PRK12316 3510 LPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALlQQD--YVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDS 3587
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1846 LRATLLVGKVhKEMNVELPLRDVFRCSTVEEMAQAI----ARMEEQAYVSIPTV---EEREYYPVSSAQKRLYILHQLeg 1918
Cdd:PRK12316 3588 IISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLARVArvggGVAVDQGPVSGETLllpIQQQFFEEPVPERHHWNQSLL-- 3664
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1919 aeqsynmtgeLVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGE-PVQRVYKEVNFAVE-HYRTSEAEA----GEVVR 1992
Cdd:PRK12316 3665 ----------LKPREALDAAALEAALQALVEHHDALRLRFVEDAGGwTAEHLPVELGGALLwRAELDDAEElerlGEEAQ 3734
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1993 gfvRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLY----NGE--SLATLRIQYKDYAVWQQS 2066
Cdd:PRK12316 3735 ---RSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYqqllQGEapRLPAKTSSFKAWAERLQE 3811
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2067 EEQLERVKRQEAYWLDMFRGELPvlEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAESGAT-LYMVLLAAYNVML 2145
Cdd:PRK12316 3812 HARGEALKAELAYWQEQLQGVSS--ELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTqVNDLLLTALARVV 3889
                        2010      2020      2030      2040
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 2146 QKYTGQEDIVIGTPIAGR----THGDLQPLIGMFVNTLAIRNYPA 2186
Cdd:PRK12316 3890 CRWTGEASALVQLEGHGRedlfADIDLSRTVGWFTSLFPVRLSPV 3934
PRK05691 PRK05691
peptide synthase; Validated
3401-5900 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1437.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3401 TPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYKPVEFAYEDL 3480
Cdd:PRK05691  679 SLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYER-DGVALQRIDAQGEFALQRIDL 757
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3481 RHLAEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLRNDLS 3560
Cdd:PRK05691  758 SDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTA 837
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3561 ERPAAP-SYSHYI----EWLEKQDMEAAARYWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERMSRIAKQ 3635
Cdd:PRK05691  838 ELAPLPlGYADYGawqrQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQA 917
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3636 HQVTVNTLMQAAWGIILQKYNGTDDAVFGsvVSGRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAALESG 3715
Cdd:PRK05691  918 HQATLFMVLLAAFQALLHRYSGQGDIRIG--VPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQ 995
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3716 GYDYYPLYE-IQAQSAQKQDLITHIMafenFPMDEQIEQAGSYEDGKLAITDVDIAEQTNYDFTLvvmPGEE-----LAV 3789
Cdd:PRK05691  996 AHQDLPFEQlVEALPQAREQGLFQVM----FNHQQRDLSALRRLPGLLAEELPWHSREAKFDLQL---HSEEdrngrLTL 1068
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3790 RFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAEIiHVFNNTAAEYQQeQTIHGLFEEQALRNPD 3869
Cdd:PRK05691 1069 SFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQL-AQWGQAPCAPAQ-AWLPELLNEQARQTPE 1146
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3870 AVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLED 3949
Cdd:PRK05691 1147 RIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLAD 1226
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3950 SGAQALLTQRHLRERVSFAGTFVAVDDEQaYHADGSnlePVVGP------NHLAYVIYTSGTTGKPKGVMVEHHGLCSLK 4023
Cdd:PRK05691 1227 SGVELLLTQSHLLERLPQAEGVSAIALDS-LHLDSW---PSQAPglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERL 1302
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4024 LMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITAT-ILPPTYAAYLNPD 4102
Cdd:PRK05691 1303 QWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLhFVPPLLQLFIDEP 1382
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4103 RMP---SLKKLITGGSAASVEF---VQQWKDKVLYFNAYGPTEASIVTSIWD-EASDslGDRksVPIGRPLANHRIYVVD 4175
Cdd:PRK05691 1383 LAAactSLRRLFSGGEALPAELrnrVLQRLPQVQLHNRYGPTETAINVTHWQcQAED--GER--SPIGRPLGNVLCRVLD 1458
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4176 SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPF-EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRI 4254
Cdd:PRK05691 1459 AELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRV 1538
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4255 ELGEVETQLAKIDAVQEAIVLAREDANGqQQLVAYFV--AQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK05691 1539 EPEEIQARLLAQPGVAQAAVLVREGAAG-AQLVGYYTgeAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKL 1617
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4333 DRKALPAPEGSMhagGEYVAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQ 4412
Cdd:PRK05691 1618 DRRALPEPVWQQ---REHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFE 1694
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4413 ------FPTVEQLAEAIGQLEQQEfdAIPVVEEREYYPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETF 4486
Cdd:PRK05691 1695 aselgaFAEQVARIQAAGERNSQG--AIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAAL 1772
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4487 RKLIARHETLRTGFELIDGEPVQRIYPEV-------DFAVETVQASEQEAKAIV-RDFIRPFDLAKPPLLRVGLIELAPE 4558
Cdd:PRK05691 1773 QALILRHETLRTTFPSVDGVPVQQVAEDSglrmdwqDFSALPADARQQRLQQLAdSEAHQPFDLERGPLLRACLVKAAER 1852
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4559 RCILMLDMHHIVSDGVSADVLVEEFARLY----SGEELP--GLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPV 4632
Cdd:PRK05691 1853 EHYFVLTLHHIVTEGWAMDIFARELGALYeaflDDRESPlePLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPL 1932
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4633 LEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQS 4712
Cdd:PRK05691 1933 LELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEG 2012
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4713 LIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTE-NKEMHLP 4791
Cdd:PRK05691 2013 LIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQSRQLA 2092
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4792 GLHLTPYPTEYGMSKFDLSLDMMEDSEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIASLGILTADEKAQ 4871
Cdd:PRK05691 2093 GMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQ 2172
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4872 IVHVFNPAAPDAPENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLL 4951
Cdd:PRK05691 2173 LLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMV 2252
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4952 VGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLqAALCLDDEAAY--AEDASNVANVNE 5029
Cdd:PRK05691 2253 VGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGV-ARWCLEDDAAAlaAYSDAPLPFLSL 2331
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 PHDLAYVIYTSGTTGRPKGVMIEHRSL-VNTAAGYRReyrldqFPVRL----LQLASFSFDVFVGDIARTLYNGGTMVIc 5104
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIaMHCQAVIER------FGMRAddceLHFYSINFDAASERLLVPLLCGARVVL- 2404
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5105 PKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGlDMSSMVLLITSSDSCSVTDYRVLQERFGSQFrIINAYG 5184
Cdd:PRK05691 2405 RAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQG-EQLPVRMCITGGEALTGEHLQRIRQAFAPQL-FFNAYG 2482
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5185 VTEAAIdsslydEPLAKL-PE-----AGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEK 5258
Cdd:PRK05691 2483 PTETVV------MPLACLaPEqleegAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAER 2556
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5259 FVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGvREAVVVVREDAKGQKVLCAH 5337
Cdd:PRK05691 2557 FVADPFaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPA-VREAVVLALDTPSGKQLAGY 2635
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5338 F-------TAESELKLSE-LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASMQTgMEYVAPRTPQEAKL 5409
Cdd:PRK05691 2636 LvsavagqDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNR-QAYQAPRSELEQQL 2714
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5410 VSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVhKEMNVELPLRDVFRCSTVEEMAqAIARMEEQAyvsiptveERE 5489
Cdd:PRK05691 2715 AQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRA-RQLGIHFSPRDLFQHQTVQTLA-AVATHSEAA--------QAE 2784
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5490 YYPVSSAQKRLYILH---QLEGAE-QSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGE--------PVQ 5557
Cdd:PRK05691 2785 QGPLQGASGLTPIQHwffDSPVPQpQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRwqaeyravTAQ 2864
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5558 RVYKEVNFAvehyrtSEAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMY-- 5635
Cdd:PRK05691 2865 ELLWQVTVA------DFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYrq 2938
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5636 ----NGESLAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGelPVLELPTDYPRPAVRKFEGSLLQRQLEP-KLGE 5710
Cdd:PRK05691 2939 lsagAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGG--PRAELPCDRPQGGNLNRHAQTVSVRLDAeRTRQ 3016
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5711 GLQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHS----DLQPIIGMFVNTLAIRSYPDDK-------- 5778
Cdd:PRK05691 3017 LLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALfddiDLTRSVGWFTSAYPLRLTPAPGddaarges 3096
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5779 -KTFRSFLDEVKETMLGaYEHQSYPFEELVEKAQPARDLSR---NPL--FDTLFAlqnkETGELQLDGLRLTPYPAEHTV 5852
Cdd:PRK05691 3097 iKAIKEQLRAVPHKGLG-YGVLRYLADAAVREAMAALPQAPitfNYLgqFDQSFA----SDALFRPLDEPAGPAHDPDAP 3171
                        2570      2580      2590      2600
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 5853 AKFDLSVDVTEGSEGLELSMEYSTALYTRETIERMAKHFEQLLTAIVQ 5900
Cdd:PRK05691 3172 LPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIA 3219
PRK05691 PRK05691
peptide synthase; Validated
7-2188 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1323.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    7 ERETAFWNKIFeGEENPPTALPYSK---AQKQAPAlvRRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTS 83
Cdd:PRK05691  863 ARQLAYWKAQL-GDEQPVLELATDHprsARQAHSA--ARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSG 939
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   84 SSSILVGMPVVTKPnenRRPVNQLV-------ILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYADG 156
Cdd:PRK05691  940 QGDIRIGVPNANRP---RLETQGLVgffintqVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG 1016
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  157 VPVV------NTLVALKQL------HITDYRQSAVSDVLFEFELDKD-EVRLHLTYNGNLYTESFIAQAVDHLNRLFSVV 223
Cdd:PRK05691 1017 LFQVmfnhqqRDLSALRRLpgllaeELPWHSREAKFDLQLHSEEDRNgRLTLSFDYAAELFDAATIERLAEHFLALLEQV 1096
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  224 LFQPDLALGQADLLSEAEKHQLLDAFNKTGTdyPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLR 303
Cdd:PRK05691 1097 CEDPQRALGDVQLLDAAERAQLAQWGQAPCA--PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLR 1174
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  304 NAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSG--TWIRLD 381
Cdd:PRK05691 1175 DKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEgvSAIALD 1254
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  382 ----DEEAYHEDGSNLESvngpEHLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDKLLQLSSYSFDGSTF 456
Cdd:PRK05691 1255 slhlDSWPSQAPGLHLHG----DNLAYVIYTSGSTGQPKGVGNTHAALAeRLQWMQATYALDDSDVLMQKAPISFDVSVW 1330
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  457 DIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVD--MNPDClRHARAILFGGERVSVSHVRKAL 534
Cdd:PRK05691 1331 ECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDepLAAAC-TSLRRLFSGGEALPAELRNRVL 1409
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  535 GHLGPGKIKHVYGPTESTVFATSYDVhEVEEGAVSiPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRP 614
Cdd:PRK05691 1410 QRLPQVQLHNRYGPTETAINVTHWQC-QAEDGERS-PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRP 1487
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  615 DLTAEKFADNPFA-PGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGE 693
Cdd:PRK05691 1488 ALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGA 1567
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  694 kQLCAYYVAD--RSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMEtgvEFVEPRTELEAGI 771
Cdd:PRK05691 1568 -QLVGYYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQR---EHVEPRTELQQQI 1643
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  772 VNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAE---AISGMGEQ-VYSSIPAA 847
Cdd:PRK05691 1644 AAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEqvaRIQAAGERnSQGAIARV 1723
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  848 EAREYYPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEF 927
Cdd:PRK05691 1724 DRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGL 1803
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  928 AVEHIRANEEEADA--------AVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY-- 997
Cdd:PRK05691 1804 RMDWQDFSALPADArqqrlqqlADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYea 1883
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  998 ---GGED-LPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREG 1073
Cdd:PRK05691 1884 fldDRESpLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAAR 1963
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1074 LQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKET 1153
Cdd:PRK05691 1964 VRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQT 2043
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1154 TLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEFR-LPGLQLTPYPVEEHTSKFDLSLDIMESgDGFL- 1231
Cdd:PRK05691 2044 VIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRqLAGMTVEYLVNDARATKFDLNLEVTDL-DGRLg 2122
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1232 CGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEEKAQLVHVFNPAAPDAPENEVFHALFEKQAERTP 1311
Cdd:PRK05691 2123 CCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTP 2202
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1312 EVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLE 1391
Cdd:PRK05691 2203 QAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIE 2282
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1392 DSAASVLLTQTHLQERAQQWGQTLqAVLCLDDEAAY--AEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSL-VN 1468
Cdd:PRK05691 2283 DSGIGLLLSDRALFEALGELPAGV-ARWCLEDDAAAlaAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIaMH 2361
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1469 TAAGYRReyrldqFPVRL----LQLASFSFDVFVGDIARTLYNGGTMVIcPKDDRIDPARLHYWISEEKITIFESTPALI 1544
Cdd:PRK05691 2362 CQAVIER------FGMRAddceLHFYSINFDAASERLLVPLLCGARVVL-RAQGQWGAEEICQLIREQQVSILGFTPSYG 2434
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1545 IPFMDYVAEHGlDMSSMELLITSSDSCSVTDYRVLQERFGSQFrIINAYGVTEAAIdsslydEPLAKL-PE-----AGNV 1618
Cdd:PRK05691 2435 SQLAQWLAGQG-EQLPVRMCITGGEALTGEHLQRIRQAFAPQL-FFNAYGPTETVV------MPLACLaPEqleegAASV 2506
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1619 PIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPF-VEGERLYRTGDLARWMPDGNVDF 1697
Cdd:PRK05691 2507 PIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFaADGGRLYRTGDLVRLRADGLVEY 2586
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1698 IGRIDNQAKIRGYRIETGEIETQLLKAEGvREAVVVVREDAKGQKVLCAYF-------TAESELKLSE-LRSSLSQELPG 1769
Cdd:PRK05691 2587 VGRIDHQVKIRGFRIELGEIESRLLEHPA-VREAVVLALDTPSGKQLAGYLvsavagqDDEAQAALREaLKAHLKQQLPD 2665
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1770 YMIPSYFVQLEQLPLTANGKIDRKALPAPDASMQTgMEYVAPRTPQEAKLASIWQEVLGLEKVGVKDNFFELGGHSLRAT 1849
Cdd:PRK05691 2666 YMVPAHLILLDSLPLTANGKLDRRALPAPDPELNR-QAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSI 2744
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1850 LLVGKVhKEMNVELPLRDVFRCSTVEEMAqAIARMEEQAyvsiptveEREYYPVSSAQKRLYILH---QLEGAE-QSYNM 1925
Cdd:PRK05691 2745 QVVSRA-RQLGIHFSPRDLFQHQTVQTLA-AVATHSEAA--------QAEQGPLQGASGLTPIQHwffDSPVPQpQHWNQ 2814
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1926 TGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGE--------PVQRVYKEVNFAvehyrtSEAEAGEVVRGFVRT 1997
Cdd:PRK05691 2815 ALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRwqaeyravTAQELLWQVTVA------DFAECAALFADAQRS 2888
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1998 FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLY------NGESLATLRIQYKDYAVWQQSEEQLE 2071
Cdd:PRK05691 2889 LDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYrqlsagAEPALPAKTSAFRDWAARLQAYAGSE 2968
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2072 RVKRQEAYWLDMFRGelPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAESGAT-LYMVLLAAYNVMLQKYTG 2150
Cdd:PRK05691 2969 SLREELGWWQAQLGG--PRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTqVNDLLLTALARVLCRWSG 3046
                        2250      2260      2270      2280
                  ....*....|....*....|....*....|....*....|..
gi 386647928 2151 QEDIVIGTPIAGRTHG----DLQPLIGMFVNTLAIRNYPAGG 2188
Cdd:PRK05691 3047 QPSVLVQLEGHGREALfddiDLTRSVGWFTSAYPLRLTPAPG 3088
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1891-3183 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1169.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1891 SIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVY 1970
Cdd:COG1020     8 ALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1971 KEVNFAVEHYRTS--------EAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFG 2042
Cdd:COG1020    88 PVVAAPLPVVVLLvdlealaeAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2043 RLYN------GESLATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDA 2116
Cdd:COG1020   168 RLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2117 GLNEALKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLE 2196
Cdd:COG1020   248 ELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2197 EVKETTLGAYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEELQLDGLKLAPYPSGNTIARFDLTLDVTETGS 2276
Cdd:COG1020   328 RVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2277 GLECNLEYATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQTQLHHVFNATAADYEADKTIHQLFEEQAE 2356
Cdd:COG1020   408 GLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAA 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2357 RIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISY 2436
Cdd:COG1020   488 RTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY 567
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2437 MLEDSSAQVLLAQRRLQERV-SFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQ 2515
Cdd:COG1020   568 MLEDAGARLVLTQSALAARLpELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2516 MFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYA---VYLNP 2592
Cdd:COG1020   648 WMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLralLDAAP 727
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2593 DHMPDFKRLIAAGSASSLELLQQWKDK---VKYFNAYGPTEDSICTTIWTPSTEDISQlKSVPIGGPIVNHRIYIVDAHY 2669
Cdd:COG1020   728 EALPSLRLVLVGGEALPPELVRRWRARlpgARLVNLYGPTETTVDSTYYEVTPPDADG-GSVPIGRPIANTRVYVLDAHL 806
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2670 QPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELG 2748
Cdd:COG1020   807 QPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELG 886
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2749 EIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGE--LSGELPGYMIPAHFVQLERMPLTPNGKIDRK 2826
Cdd:COG1020   887 EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRlaLALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2827 ALPAPQgnASAGADYVAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTV 2906
Cdd:COG1020   967 ALPAPA--AAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAA 1044
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2907 AQLSKHIRPVARMADQGEVSGDVSLTPIQHWFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHK 2986
Cdd:COG1020  1045 AAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAA 1124
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2987 SENGYTAWNRAIGEGEL--YGLEVVDLKGIEESAQAVEAKANEIQSSIDLEAGPFVKAGLFQCADG----DHLLIVIHHG 3060
Cdd:COG1020  1125 LRARRAVRQEGPRLRLLvaLAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLllllLLLLLLLLLL 1204
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3061 VVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYRTWSEQLAAYAQSPVIERELAYWKRVAQTEVQPLPKDEQVDVSL 3140
Cdd:COG1020  1205 LLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALA 1284
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|...
gi 386647928 3141 QQDSESISIEWTREETEQLLKGVHRAYNTEMNDILLAALGMAV 3183
Cdd:COG1020  1285 RARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
5481-6775 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1157.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5481 SIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVY 5560
Cdd:COG1020     8 ALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5561 KEVNFAVEHYRTS--------EAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFG 5632
Cdd:COG1020    88 PVVAAPLPVVVLLvdlealaeAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5633 RMYN------GESLAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEP 5706
Cdd:COG1020   168 RLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5707 KLGEGLQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLD 5786
Cdd:COG1020   248 ELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5787 EVKETMLGAYEHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSE 5866
Cdd:COG1020   328 RVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5867 GLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEKEHIQRVFNATEAKYPSDKTIHQLFEEQAE 5946
Cdd:COG1020   408 GLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAA 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5947 RIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRY 6026
Cdd:COG1020   488 RTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY 567
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6027 MLEDSGAKLLLVQGHLLDR-ASFADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVK 6105
Cdd:COG1020   568 MLEDAGARLVLTQSALAARlPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6106 NTN-YVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDS 6184
Cdd:COG1020   648 WMQrRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP 727
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6185 GMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEA--VPIGKPINNSTAYIVDSKLS 6262
Cdd:COG1020   728 EALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsVPIGRPIANTRVYVLDAHLQ 807
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6263 LLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGE 6341
Cdd:COG1020   808 PVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGE 887
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTI--GELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRA 6419
Cdd:COG1020   888 IEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAaaALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6420 LPAPQgnAPVGAEYVAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTLA 6499
Cdd:COG1020   968 LPAPA--AAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAA 1045
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6500 QLSQHIQPVARMIDQGEVTGEIGLTPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKS 6579
Cdd:COG1020  1046 AAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAAL 1125
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6580 ENGYAAWNRAIGEGELYSLEVADFRDVKSAEQAVEAKANE--IQSSIDLEVGPLFKAGLFQCADGDHLLLVIHHGVVDGV 6657
Cdd:COG1020  1126 RARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAelLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLL 1205
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6658 SWRILLEDVALG----YEQAAKGEEVRLPAKTDSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAPLPKDKQSDRSLQ 6733
Cdd:COG1020  1206 LLLLLLLLLLLLllllLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALAR 1285
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|..
gi 386647928 6734 QDSESITIQWSRKETEQLLKKVHRAYNTEMNDILLTALGMAV 6775
Cdd:COG1020  1286 ARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
843-2140 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1131.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  843 SIPAAEAREYYPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIY 922
Cdd:COG1020     8 ALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  923 PEVEFAVEHI--------RANEEEADAAVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFA 994
Cdd:COG1020    88 PVVAAPLPVVvllvdleaLAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  995 RLYG------GEDLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDA 1068
Cdd:COG1020   168 RLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1069 QKREGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLE 1148
Cdd:COG1020   248 ELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1149 DVKETTLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEFRLPGLQLTPYPVEEHTSKFDLSLDIMESGD 1228
Cdd:COG1020   328 RVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1229 GFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEEKAQLVHVFNPAAPDAPENEVFHALFEKQAE 1308
Cdd:COG1020   408 GLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAA 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1309 RTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQF 1388
Cdd:COG1020   488 RTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY 567
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1389 MLEDSAASVLLTQTHLQERAQQWGQTlqaVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVN 1468
Cdd:COG1020   568 MLEDAGARLVLTQSALAARLPELGVP---VLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVN 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1469 TAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFM 1548
Cdd:COG1020   645 LLAWMQRRYGLGP-GDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALL 723
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1549 DYVAEhglDMSSMELLITSSDSCSVTDYRVLQERFGsQFRIINAYGVTEAAIDSSLYdEPLAKLPEAGNVPIGKAALNAK 1628
Cdd:COG1020   724 DAAPE---ALPSLRLVLVGGEALPPELVRRWRARLP-GARLVNLYGPTETTVDSTYY-EVTPPDADGGSVPIGRPIANTR 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1629 FYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVE-GERLYRTGDLARWMPDGNVDFIGRIDNQAKI 1707
Cdd:COG1020   799 VYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpGARLYRTGDLARWLPDGNLEFLGRADDQVKI 878
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1708 RGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESE--LKLSELRSSLSQELPGYMIPSYFVQLEQLPLT 1785
Cdd:COG1020   879 RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGaaAAAALLRLALALLLPPYMVPAAVVLLLPLPLT 958
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1786 ANGKIDRKALPAPDAsmQTGMEYVAPRTPQEAKLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPL 1865
Cdd:COG1020   959 GNGKLDRLALPAPAA--AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLL 1036
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1866 RDVFRCSTVEEMAQAIARMEEQAYVSIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFR 1945
Cdd:COG1020  1037 LLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLA 1116
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1946 QLIARHETLRTGFELVNGEPVQRVYKEVNFA------VEHYRTSEAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHI 2019
Cdd:COG1020  1117 LLLALLAALRARRAVRQEGPRLRLLVALAAAlalaalLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLL 1196
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2020 LLLDMHHIVSDGMSTDVLTEEFGRLY------NGESLATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGELPVLE- 2092
Cdd:COG1020  1197 LLLLLLLLLLLLLLLLLLLLLLLLLLllaaaaAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLAl 1276
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 2093 -MPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAESGATLYMVLLAA 2140
Cdd:COG1020  1277 aLLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLL 1325
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
4426-5730 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1125.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4426 LEQQEFDAIPVVEEREYYPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDG 4505
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4506 EPVQRIYPEVDFAVETV--------QASEQEAKAIVRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSAD 4577
Cdd:COG1020    81 RPVQVIQPVVAAPLPVVvllvdleaLAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4578 VLVEEFARLYS------GEELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDT 4651
Cdd:COG1020   161 LLLAELLRLYLaayagaPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4652 LDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADK 4731
Cdd:COG1020   241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4732 TFLSYLEDVKETTLGAFEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEMHLPGLHLTPYPTEYGMSKFDLSL 4811
Cdd:COG1020   321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4812 DMMEDSEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIASLGILTADEKAQIVHVFNPAAPDAPENEAFHA 4891
Cdd:COG1020   401 TVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4892 LFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 4971
Cdd:COG1020   481 LFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4972 PSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLqaaLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMI 5051
Cdd:COG1020   561 PAERLAYMLEDAGARLVLTQSALAARLPELGVPV---LALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMV 637
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5052 EHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTP 5131
Cdd:COG1020   638 EHRALVNLLAWMQRRYGLGP-GDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTP 716
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 ALIIPFMDYVAEhglDMSSMVLLITSSDSCSVTDYRVLQERFGsQFRIINAYGVTEAAIDSSLYdEPLAKLPEAGNVPIG 5211
Cdd:COG1020   717 SLLRALLDAAPE---ALPSLRLVLVGGEALPPELVRRWRARLP-GARLVNLYGPTETTVDSTYY-EVTPPDADGGSVPIG 791
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5212 KAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVE-GERLYRTGDLARWMPDGNVDFIGR 5290
Cdd:COG1020   792 RPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpGARLYRTGDLARWLPDGNLEFLGR 871
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5291 IDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESE--LKLSELRSSLSQELPGYMIPSYFVQ 5368
Cdd:COG1020   872 ADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGaaAAAALLRLALALLLPPYMVPAAVVL 951
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5369 LEQLPLTANGKIDRKALPAPDAsmQTGMEYVAPRTPQEAKLVSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVHKE 5448
Cdd:COG1020   952 LLPLPLTGNGKLDRLALPAPAA--AAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARL 1029
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5449 MNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRG 5528
Cdd:COG1020  1030 LLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLL 1109
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5529 KLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFA------VEHYRTSEAEAGEVVRGFVRTFDLAKPPLLRVGLVE 5602
Cdd:COG1020  1110 ALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAAlalaalLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLL 1189
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5603 LAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMY------NGESLAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRG 5676
Cdd:COG1020  1190 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLllaaaaAALLALALLLALLALAALLALAALAALAAALLALALALLAL 1269
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 5677 ELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAAESGATLYMVLLAA 5730
Cdd:COG1020  1270 ALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLAL 1323
PRK12467 PRK12467
peptide synthase; Provisional
6996-8459 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1122.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6996 QKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSgPRGEPLQIVYRDKRIGFVYEDLSHL 7075
Cdd:PRK12467   56 QERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQ-DEEGFRQVIDASLSLTIPLDDLANE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7076 PADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDRPEQK 7155
Cdd:PRK12467  135 QGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLP 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7156 AAP-AYSQYI----EWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAKQCRV 7230
Cdd:PRK12467  215 ALPiQYADYAiwqrSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGV 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7231 TVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEipGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALESGRYD 7310
Cdd:PRK12467  295 TLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--ETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQ 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7311 FYPlYEIQTQSAQKQELINH----LLVFENYPMDEQVEQAGGDDSGTLSITDVDVAEHT-NYNFTVTVFPGDE-IVVRFD 7384
Cdd:PRK12467  373 DLP-FEQLVEALQPERSLSHsplfQVMFNHQNTATGGRDREGAQLPGLTVEELSWARHTaQFDLALDTYESAQgLWAAFT 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7385 YNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHVFNNTAAEYAReQTIHGLFEEQAERMPEKAA 7464
Cdd:PRK12467  452 YATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAP-DCVHQLIEAQARQHPERPA 530
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7465 VVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGA 7544
Cdd:PRK12467  531 LVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGV 610
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7545 QVLLTQRHLQE----CVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAE 7620
Cdd:PRK12467  611 RLLLTQSHLLAqlpvPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAE 690
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7621 TLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAIYL----SPDRL 7696
Cdd:PRK12467  691 RLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALlqasRVALP 770
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7697 PSLKKLITGGSAASVEFVQQWK---DKVRYFNAYGPTEASIVTSVWAASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLP 7773
Cdd:PRK12467  771 RPQRALVCGGEALQVDLLARVRalgPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVP 850
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7774 VGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLA-GERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEE 7852
Cdd:PRK12467  851 VGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEA 930
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7853 QLLKIASVQETIVIARGDANGQQqLCAYFV-------ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:PRK12467  931 RLLAQPGVREAVVLAQPGDAGLQ-LVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDR 1009
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7926 NALPAPEGSmQTGADFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVNKELNVNLPLRDIFRFP 8005
Cdd:PRK12467 1010 KALPKPDAS-AVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQ 1088
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8006 TVEALAQVIDGLEQEEHSAIPVIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHE 8085
Cdd:PRK12467 1089 TLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHE 1168
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8086 TLRTGFEMANGEPVQRVYS--DVEFAVEYSKADREEAVEI----AQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHH 8159
Cdd:PRK12467 1169 SLRTTFVQEDGRTRQVIHPvgSLTLEEPLLLAADKDEAQLkvyvEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHH 1248
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8160 IISDGASVGILQEEFSRLYAGE------ELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERT 8233
Cdd:PRK12467 1249 IVSDGWSMQVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRP 1328
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8234 STRSFEGAELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLA 8313
Cdd:PRK12467 1329 AVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQV 1408
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8314 IRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNPVFDTMFVLQnTEDRGIEAD--AFSLTPFVF 8391
Cdd:PRK12467 1409 LRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQ-RDDHQAQAQlpGLSVESLSW 1487
                        1450      1460      1470      1480      1490      1500
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 8392 D-QTvaAQFDLTLSVAEDDGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQLNEPE 8459
Cdd:PRK12467 1488 EsQT--AQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEA 1554
PRK12316 PRK12316
peptide synthase; Provisional
813-2187 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1016.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  813 ISLPL--RDVFryptveklAEAISGMGEQVYS-SIPAA-EAREYYPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALD 888
Cdd:PRK12316   14 IELPLekRRVF--------LATLRGEGVDFSLfPIPAGvSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  889 RNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVEHI------RANEEEA--DAAVKQFIRAFDLAKPPLLRV 960
Cdd:PRK12316   86 RQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEdcsglpEAEQEARlrDEAQRESLQPFDLCEGPLLRV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  961 GLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGE------DLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLE 1034
Cdd:PRK12316  166 RLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYatgaepGLPALPIQYADYALWQRSWLEAGEQERQLEYWRA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1035 VFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAG 1114
Cdd:PRK12316  246 QLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIAN 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1115 RTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNT- 1193
Cdd:PRK12316  326 RNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLv 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1194 --ENKEFRLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASL 1271
Cdd:PRK12316  406 adIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDEL 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1272 GILTVEEKAQLVHVFNPAAPDAPENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVG 1351
Cdd:PRK12316  486 PMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVG 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1352 ILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAqQWGQTLQaVLCLDDEAAYAEDA 1431
Cdd:PRK12316  566 VAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-PLAAGVQ-VLDLDRPAAWLEGY 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1432 SNVANVNE--PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTLYNGG 1509
Cdd:PRK12316  644 SEENPGTElnPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGD-TVLQKTPFSFDVSVWEFFWPLMSGA 722
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1510 TMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDyvAEHGLDMSSMELLITSSDSCSVTdyrvLQER-FG--SQ 1586
Cdd:PRK12316  723 RLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLRRIVCSGEALPAD----AQEQvFAklPQ 796
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1587 FRIINAYGVTEAAIDSSLYdeplAKLPEAGN-VPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELT 1665
Cdd:PRK12316  797 AGLYNLYGPTEAAIDVTHW----TCVEEGGDsVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLT 872
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1666 EEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVvredAKGQKVLC 1745
Cdd:PRK12316  873 AERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLV 948
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1746 AYFTAESELKL--SELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASMQTgMEYVAPRTPQEAKLASIW 1823
Cdd:PRK12316  949 GYVVLESEGGDwrEALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQ-QGYVAPRNALERTLAAIW 1027
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1824 QEVLGLEKVGVKDNFFELGGHSLRATLLVGKVhKEMNVELPLRDVFRCSTVEEMAQAiARMEEQAYVSI-PTVEEREYYP 1902
Cdd:PRK12316 1028 QDVLGVERVGLDDNFFELGGDSIVSIQVVSRA-RQAGIQLSPRDLFQHQTIRSLALV-AKAGQATAADQgPASGEVALAP 1105
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1903 VssaQKRLYilHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYRT 1982
Cdd:PRK12316 1106 V---QRWFF--EQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQ 1180
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1983 --SEAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNgESLATLRIQYKDY 2060
Cdd:PRK12316 1181 aaSEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYA-DLDADLPARTSSY 1259
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2061 AVW-QQSEEQLERVKRQEAYWLDMFRGELPvlEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAESGAT-LYMVLL 2138
Cdd:PRK12316 1260 QAWaRRLHEHAGARAEELDYWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTqVNDLLL 1337
                        1370      1380      1390      1400      1410
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2139 AAYNVMLQKYTGQEDIVIGTPIAGRTH----GDLQPLIGMFVNTLAIRNYPAG 2187
Cdd:PRK12316 1338 TALARVTCRWSGQASVLVQLEGHGREDlfedIDLSRTVGWFTSLFPVRLTPAA 1390
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3399-4688 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1014.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3399 ALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSgWRGEPLQIVYRYKPVEFAYE 3478
Cdd:COG1020    19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRT-RAGRPVQVIQPVVAAPLPVV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3479 DLRHLAEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLRND 3558
Cdd:COG1020    98 VLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3559 LSERPAAPS-----YSHYIEWLEKQDMEAAARYWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERMSRIA 3633
Cdd:COG1020   178 PLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3634 KQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAeiAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAALE 3713
Cdd:COG1020   258 RRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3714 SGGYDYYPLYEIQAQSAQKQD-----LITHIMAFENFPMDEQiEQAGsyedgkLAITDVDIAEQT-NYDFTLVVMP-GEE 3786
Cdd:COG1020   336 AYAHQDLPFERLVEELQPERDlsrnpLFQVMFVLQNAPADEL-ELPG------LTLEPLELDSGTaKFDLTLTVVEtGDG 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3787 LAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAEIIHVFNNTAAEYQQEQTIHGLFEEQALR 3866
Cdd:COG1020   409 LRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAAR 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3867 NPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYM 3946
Cdd:COG1020   489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3947 LEDSGAQALLTQRHLRERV-SFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLM 4025
Cdd:COG1020   569 LEDAGARLVLTQSALAARLpELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAW 648
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4026 FANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAYL---NPD 4102
Cdd:COG1020   649 MQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALldaAPE 728
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4103 RMPSLKKLITGGSAASVEFVQQWKDK---VLYFNAYGPTEASIVTSIWdEASDSLGDRKSVPIGRPLANHRIYVVDSHNR 4179
Cdd:COG1020   729 ALPSLRLVLVGGEALPPELVRRWRARlpgARLVNLYGPTETTVDSTYY-EVTPPDADGGSVPIGRPIANTRVYVLDAHLQ 807
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4180 MLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPF-EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGE 4258
Cdd:COG1020   808 PVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGE 887
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4259 VETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKA 4336
Cdd:COG1020   888 IEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLA 967
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4337 LPAPEGSmhAGGEYVAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQFPTV 4416
Cdd:COG1020   968 LPAPAAA--AAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAA 1045
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4417 EQLAEAIGQLEQQEFDAIPVVEEREYYPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETL 4496
Cdd:COG1020  1046 AAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAAL 1125
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4497 RTGFELIDGEPVQRIYPEVDFAVET------VQASEQEAKAIVRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIV 4570
Cdd:COG1020  1126 RARRAVRQEGPRLRLLVALAAALALaallalLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLL 1205
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4571 SDGVSADVLVEEFARLY------SGEELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAV 4644
Cdd:COG1020  1206 LLLLLLLLLLLLLLLLLllaaaaAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALAR 1285
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|....
gi 386647928 4645 QSYAGDTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQ 4688
Cdd:COG1020  1286 ARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
6992-8278 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1014.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSgPRGEPLQIVYRDKRIGFVYED 7071
Cdd:COG1020    20 LSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRT-RAGRPVQVIQPVVAAPLPVVV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7072 LSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQG-D 7150
Cdd:COG1020    99 LLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGaP 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7151 RPEQKAAPAYSQY----IEWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAK 7226
Cdd:COG1020   179 LPLPPLPIQYADYalwqREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALAR 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7227 QCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAeiPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALES 7306
Cdd:COG1020   259 RHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAA 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7307 GRYDFYPLYEIQ-----TQSAQKQELINHLLVFENYPMDEQveQAGGddsgtLSITDVDVA-EHTNYNFTVTVFP-GDEI 7379
Cdd:COG1020   337 YAHQDLPFERLVeelqpERDLSRNPLFQVMFVLQNAPADEL--ELPG-----LTLEPLELDsGTAKFDLTLTVVEtGDGL 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7380 VVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHVFNNTAAEYAREQTIHGLFEEQAERM 7459
Cdd:COG1020   410 RLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAART 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:COG1020   490 PDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYML 569
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQRHLQECV-SFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMF 7618
Cdd:COG1020   570 EDAGARLVLTQSALAARLpELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM 649
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7619 AETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYA---IYLSPDR 7695
Cdd:COG1020   650 QRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLralLDAAPEA 729
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7696 LPSLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDGLDLRSVPIGRPIANHQIFIVDSQNHML 7772
Cdd:COG1020   730 LPSLRLVLVGGEALPPELVRRWRARlpgARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPV 809
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7773 PVGVAGELCISGAGLARGYLNRPELTAEKFVDNPF-LAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIE 7851
Cdd:COG1020   810 PVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIE 889
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7852 EQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAP 7931
Cdd:COG1020   890 AALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7932 EGSMQTGADFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVNKELNVNLPLRDIFRFPTVEALA 8011
Cdd:COG1020   970 APAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAA 1049
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8012 QVIDGLEQEEHSAIPVIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGF 8091
Cdd:COG1020  1050 AAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARR 1129
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8092 EMANGEPVQRVYSDVEFAVEYSKADREEAVEIAQ----------RFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHII 8161
Cdd:COG1020  1130 AVRQEGPRLRLLVALAAALALAALLALLLAAAAAaaellaaaalLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLL 1209
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8162 SDGASVGILQEEFSRLYAGEELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGA 8241
Cdd:COG1020  1210 LLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAA 1289
                        1290      1300      1310
                  ....*....|....*....|....*....|....*..
gi 386647928 8242 ELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLL 8278
Cdd:COG1020  1290 RTARALALLLLLALLLLLALALALLLLLLLLLALLLL 1326
PRK05691 PRK05691
peptide synthase; Validated
4890-6713 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 981.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4890 HALfEKQAECTPEAAAVVYENDR------LTYRELNERANRLARTLRAQGVKPNQLVgILADRSADLLVGALAVWKAGGA 4963
Cdd:PRK05691   13 QAL-QRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4964 YVPLDPDYPS-----DRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAA----LCLDD-EAAYAEDASNVANvnEPHDL 5033
Cdd:PRK05691   91 AVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANapelLCVDTlDPALAEAWQEPAL--QPDDI 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5034 AYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFP----VRLLQLASfsfDV-FVGDIARTLYNGGTMVI-CPKD 5107
Cdd:PRK05691  169 AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddviVSWLPLYH---DMgLIGGLLQPIFSGVPCVLmSPAY 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5108 DRIDPARLHYWISEEKITIFEStpaliiPFMDY------VAE---HGLDMSSMVLLITSSDSCSVTDYRVLQERF-GSQF 5177
Cdd:PRK05691  246 FLERPLRWLEAISEYGGTISGG------PDFAYrlcserVSEsalERLDLSRWRVAYSGSEPIRQDSLERFAEKFaACGF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5178 R---IINAYGVTEAAIDSS------------LYDEPLAK---LPEAGNVPI--GKAALNAKFYIVD-AHLNPVPVGVLGE 5236
Cdd:PRK05691  320 DpdsFFASYGLAEATLFVSggrrgqgipaleLDAEALARnraEPGTGSVLMscGRSQPGHAVLIVDpQSLEVLGDNRVGE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5237 LCIGGIGVARGYLNRPELTEEKFVDspfVEGERLYRTGDLArWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQL----- 5311
Cdd:PRK05691  400 IWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVereve 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5312 -----------LKAEGVREAVVVVREDAKGQKVLcahfTAESELK-LSELRSSLSQElpgymIPSYFVQLE--QLPLTAN 5377
Cdd:PRK05691  476 vvrkgrvaafaVNHQGEEGIGIAAEISRSVQKIL----PPQALIKsIRQAVAEACQE-----APSVVLLLNpgALPKTSS 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5378 GKIDRKA--LPAPDASMQTGMEYVAPRTPQ-----------EAKLVSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGK 5444
Cdd:PRK05691  547 GKLQRSAcrLRLADGSLDSYALFPALQAVEaaqtaasgdelQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVAR 626
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5445 VHKEMNVELPLRDVFRCSTVEEMAQAIARMEE---QAYVSIPTVEEREYYPVSSAQKRLYILHQLEGAEQSYNMTGELVL 5521
Cdd:PRK05691  627 LRDELGIDLNLRQLFEAPTLAAFSAAVARQLAgggAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHL 706
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5522 EGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYRTS-------EAEAGEVVRGFVRT-FDLAKP 5593
Cdd:PRK05691  707 RGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSdlpeaerEARAAQIREEEARQpFDLEKG 786
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5594 PLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGE------SLAPLRIQYKDYATWQQSEAQQEQMKRQE 5667
Cdd:PRK05691  787 PLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWQRQWLAQGEAARQL 866
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5668 AYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVG 5747
Cdd:PRK05691  867 AYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIG 946
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5748 TPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAYEHQSYPFEELVEKAQPARDlsrNPLFDTLFA 5827
Cdd:PRK05691  947 VPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQARE---QGLFQVMFN 1023
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5828 LQNKETGEL-QLDGLRLTPYPAEHTVAKFDLSVDVTEGSEG-LELSMEYSTALYTRETIERMAKHFEQLLTAIVQAPEAP 5905
Cdd:PRK05691 1024 HQQRDLSALrRLPGLLAEELPWHSREAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRA 1103
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5906 LASLEMITAEEKEHIQRVFNATEAkyPSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPD 5985
Cdd:PRK05691 1104 LGDVQLLDAAERAQLAQWGQAPCA--PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPD 1181
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5986 QMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDgAYHEDG 6065
Cdd:PRK05691 1182 VCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALD-SLHLDS 1260
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6066 SnlePVNGP------EHLTYVIYTSGTTGRPKGVMVEHRNVV-RLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALL 6138
Cdd:PRK05691 1261 W---PSQAPglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAeRLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLI 1337
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6139 NGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQ-DSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSI 6217
Cdd:PRK05691 1338 TGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEpLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQL 1417
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6218 VNGYGPTEnTTFSTTH-TIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVE 6296
Cdd:PRK05691 1418 HNRYGPTE-TAINVTHwQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP 1496
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6297 SSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQkQLCAYFVA 6375
Cdd:PRK05691 1497 DPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGA-QLVGYYTG 1575
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6376 E--RELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPAPQGNApvgAEYVAPRTEQEKALAAVWQAVLG 6453
Cdd:PRK05691 1576 EagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ---REHVEPRTELQQQIAAIWREVLG 1652
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6454 AERVGVTDHFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYptlAQLSQHIQPVARMIDQGEVTGEIGLTPIQR---- 6528
Cdd:PRK05691 1653 LPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEA---SELGAFAEQVARIQAAGERNSQGAIARVDRsqpv 1729
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6529 ---------WFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFrKSENGyAAWNRAIGEGELySLE 6599
Cdd:PRK05691 1730 plsysqqrmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTF-PSVDG-VPVQQVAEDSGL-RMD 1806
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6600 VADFR--DVKSAEQAVEAKAN-EIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQAAK 6675
Cdd:PRK05691 1807 WQDFSalPADARQQRLQQLADsEAHQPFDLERGPLLRACLVKAAEREHyFVLTLHHIVTEGWAMDIFARELGALYEAFLD 1886
                        1930      1940      1950      1960
                  ....*....|....*....|....*....|....*....|.
gi 386647928 6676 GEE---VRLPAKTDSFRTWSEQlaaYAQSPAMENERAYWEQ 6713
Cdd:PRK05691 1887 DREsplEPLPVQYLDYSVWQRQ---WLESGERQRQLDYWKA 1924
PRK05691 PRK05691
peptide synthase; Validated
6993-8459 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 922.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6993 TPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSgPRGEPLQIVYRDKRIGFVYEDL 7072
Cdd:PRK05691  679 SLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYE-RDGVALQRIDAQGEFALQRIDL 757
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7073 SHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDRP 7152
Cdd:PRK05691  758 SDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTA 837
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7153 EQKAAP-AYSQYI----EWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAKQ 7227
Cdd:PRK05691  838 ELAPLPlGYADYGawqrQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQA 917
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7228 CRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAeiPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALESG 7307
Cdd:PRK05691  918 HQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQ 995
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7308 RYD---FYPLYEIQTQSAQK---QELINHL------------LVFENYP-------MDEQVeQAGGDDSGTLSITdvdva 7362
Cdd:PRK05691  996 AHQdlpFEQLVEALPQAREQglfQVMFNHQqrdlsalrrlpgLLAEELPwhsreakFDLQL-HSEEDRNGRLTLS----- 1069
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7363 ehtnynftvtvfpgdeivvrFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIiHVFNNTAAEy 7442
Cdd:PRK05691 1070 --------------------FDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQL-AQWGQAPCA- 1127
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7443 AREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGA 7522
Cdd:PRK05691 1128 PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGA 1207
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7523 YVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVG--PNHLAYVIYTSGTTGK 7600
Cdd:PRK05691 1208 YVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWPSQAPGLHlhGDNLAYVIYTSGSTGQ 1287
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7601 PKGVMVEHHGLCS-LKLMFAeTLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGIT 7679
Cdd:PRK05691 1288 PKGVGNTHAALAErLQWMQA-TYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVT 1366
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7680 AA-ILPPTYAIYLSPDRLP---SLKKLITGGSAASVEF---VQQWKDKVRYFNAYGPTEASIVTSVWAASPDglDLRSVP 7752
Cdd:PRK05691 1367 TLhFVPPLLQLFIDEPLAAactSLRRLFSGGEALPAELrnrVLQRLPQVQLHNRYGPTETAINVTHWQCQAE--DGERSP 1444
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7753 IGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPF-LAGERMYRTGDLARWLPDGNIEYL 7831
Cdd:PRK05691 1445 IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYL 1524
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7832 GRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQqLCAYFVAD--RELTVSELRGTLSQELPGYMIPSYF 7909
Cdd:PRK05691 1525 GRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQ-LVGYYTGEagQEAEAERLKAALAAELPEYMVPAQL 1603
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7910 VQLEQMPLTPNGKIDRNALPAPEgsMQTGaDFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVN 7989
Cdd:PRK05691 1604 IRLDQMPLGPSGKLDRRALPEPV--WQQR-EHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTR 1680
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7990 KELNVNLPLRDIFRFPTVEALAQVIDGLEQE----EHSAIPVIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATIE 8065
Cdd:PRK05691 1681 QACDVELPLRALFEASELGAFAEQVARIQAAgernSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLS 1760
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8066 GPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEYSKADREEAVEIAQRFV--------RPFDLRKPP 8137
Cdd:PRK05691 1761 GVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQqladseahQPFDLERGP 1840
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8138 LLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLY----AGEELP--PLRIQYKDYAAWQRSEAYAKRVKQQEG 8211
Cdd:PRK05691 1841 LLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYeaflDDRESPlePLPVQYLDYSVWQRQWLESGERQRQLD 1920
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8212 YWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGT 8291
Cdd:PRK05691 1921 YWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGA 2000
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8292 PVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNPVFDTMFVL 8371
Cdd:PRK05691 2001 PVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNV 2080
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8372 QNTEDRGIEADAFSLTPFVFDQTVAAQFDLTLSVAEDDGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLS 8451
Cdd:PRK05691 2081 QRWEFQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLA 2160

                  ....*....
gi 386647928 8452 QIQ-LNEPE 8459
Cdd:PRK05691 2161 ELPlLAAAE 2169
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
5-1098 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 874.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    5 AFERETAFWNKIFEGEENPPTALPYSKAQKQAPALVRRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSS 84
Cdd:COG1020   203 ELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQ 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   85 SSILVGMPVVtkpneNRRP----------VNQLViLREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYA 154
Cdd:COG1020   283 DDVVVGTPVA-----GRPRpeleglvgffVNTLP-LRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERD 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  155 DG-VPVVNTLVA----------LKQLHITDY---RQSAVSDVLFEFELDKDEVRLHLTYNGNLYTESFIAQAVDHLNRLF 220
Cdd:COG1020   357 LSrNPLFQVMFVlqnapadeleLPGLTLEPLeldSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLL 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  221 SVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLAR 300
Cdd:COG1020   437 EALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAH 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  301 TLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERV-SFSGTWIR 379
Cdd:COG1020   517 HLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLpELGVPVLA 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  380 LDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN-YIDVTGQDKLLQLSSYSFDGSTFDI 458
Cdd:COG1020   597 LDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQrRYGLGPGDRVLQFASLSFDASVWEI 676
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  459 FGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRHARAILFGGERVSVSHVRKALGHLG 538
Cdd:COG1020   677 FGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLP 756
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  539 PGKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTA 618
Cdd:COG1020   757 GARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTA 836
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  619 EKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLC 697
Cdd:COG1020   837 ERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLV 916
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  698 AYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGVEFVEPRTELEAGIVNIWKE 777
Cdd:COG1020   917 AYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALL 996
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  778 ILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISGMGEQVYSSIPAAEAREYYPLSS 857
Cdd:COG1020   997 LLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLL 1076
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  858 AQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFA------VEH 931
Cdd:COG1020  1077 LSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAAlalaalLAL 1156
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IRANEEEADAAVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY------GGEDLPAL 1005
Cdd:COG1020  1157 LLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLllaaaaAALLALAL 1236
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1006 RIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATL 1085
Cdd:COG1020  1237 LLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLL 1316
                        1130
                  ....*....|...
gi 386647928 1086 YMVLLAAYTILLQ 1098
Cdd:COG1020  1317 LLLLLALLLLALL 1329
PRK12467 PRK12467
peptide synthase; Provisional
6996-8289 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 825.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6996 QKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSgPRGEPLQIVYRDKRIGFvYEDLSHL 7075
Cdd:PRK12467 1123 QERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ-EDGRTRQVIHPVGSLTL-EEPLLLA 1200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7076 PADERQASVERLEQEdIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDRPEQK 7155
Cdd:PRK12467 1201 ADKDEAQLKVYVEAE-ARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLP 1279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7156 AAP-AYSQYI----EWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAKQCRV 7230
Cdd:PRK12467 1280 ALPiQYADYAvwqrQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGV 1359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7231 TVNTLMQAVWGVILQKYNATDDVVYGSVVSGRP-AEIpgiEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALESGRY 7309
Cdd:PRK12467 1360 TLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNrAET---EGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAH 1436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7310 DFYPlYEIQTQSAQKQELINHLLVFENYPMDEQVEQAGGDDSGTLSITDVDVAEHT-NYNFTVTVFPGDE-IVVRFDYNS 7387
Cdd:PRK12467 1437 QDLP-FEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPGLSVESLSWESQTaQFDLTLDTYESSEgLQASLTYAT 1515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7388 FVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHVFNNTAAEYAREQTIHGLFEEQAERMPEKAAVVF 7467
Cdd:PRK12467 1516 DLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVF 1595
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7468 ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVL 7547
Cdd:PRK12467 1596 GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELL 1675
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7548 LTQRHLQECVSFDGKV--IAADDEQAY--GEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLR 7623
Cdd:PRK12467 1676 LTQSHLQARLPLPDGLrsLVLDQEDDWleGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQ 1755
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7624 ITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTY-AIYLSPD----RLPS 7698
Cdd:PRK12467 1756 LSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMlQQLLQMDeqveHPLS 1835
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7699 LKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDGLDLR-SVPIGRPIANHQIFIVDSQNHMLPV 7774
Cdd:PRK12467 1836 LRRVVCGGEALEVEALRPWLERlpdTGLFNLYGPTETAVDVTHWTCRRKDLEGRdSVPIGQPIANLSTYILDASLNPVPI 1915
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7775 GVAGELCISGAGLARGYLNRPELTAEKFVDNPF-LAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQ 7853
Cdd:PRK12467 1916 GVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEAR 1995
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7854 LLKIASVQETIVIARGDANGQQqLCAYFVADRELTV----------SELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:PRK12467 1996 LREQGGVREAVVIAQDGANGKQ-LVAYVVPTDPGLVdddeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKL 2074
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7924 DRNALPAPEGS-MQTgaDFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVnKELNVNLPLRDIF 8002
Cdd:PRK12467 2075 DRKALPAPDASeLQQ--AYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRA-RQAGIRFTPKDLF 2151
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8003 RFPTVEALAQVidGLEQEEHSAI---PVIGEreyYPVSSAQKRLFILHQLEgaQQSYNIPGFATIEGPLDRDRFEAVFRQ 8079
Cdd:PRK12467 2152 QHQTVQSLAAV--AQEGDGTVSIdqgPVTGD---LPLLPIQQMFFADDIPE--RHHWNQSVLLEPREALDAELLEAALQA 2224
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8080 LIERHETLRTGFEMANGEpVQRVYSDVEFAVE-----YSKADREEAVEIAQRFVRPFDLRKPPLLRVGLIEVEPERHILM 8154
Cdd:PRK12467 2225 LLVHHDALRLGFVQEDGG-WSAMHRAPEQERRpllwqVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLL 2303
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8155 LDMHHIISDGASVGI----LQEEFSRLYAGEelpPLRIQYKDYA--AW-QRSEAYAKRVKQQE--GYWLQTLAGElpVIE 8225
Cdd:PRK12467 2304 LVIHHLVVDGVSWRIlledLQTAYRQLQGGQ---PVKLPAKTSAfkAWaERLQTYAASAALADelGYWQAQLQGA--STE 2378
                        1290      1300      1310      1320      1330      1340
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 8226 LPTDYERTSTRSFEGAELEFEADEALTQR-LNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIV 8289
Cdd:PRK12467 2379 LPCDHPQGGLQRRHAASVTTHLDSEWTRRlLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLI 2443
PRK12316 PRK12316
peptide synthase; Provisional
6992-8321 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 814.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSgpRGEPLQIVYRDKrigfvyED 7071
Cdd:PRK12316 2605 LSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVE--VGEQTRQVILPN------MS 2676
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7072 LSHLPADERQASVERLEQ---EDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQ 7148
Cdd:PRK12316 2677 LRIVLEDCAGVADAAIRQrvaEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARR 2756
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7149 GDRPEQKAAP-AYSQYIE----WLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNR 7223
Cdd:PRK12316 2757 GEQPTLPPLPlQYADYAAwqraWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLA 2836
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7224 AAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRpaEIPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAA 7303
Cdd:PRK12316 2837 LARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQA 2914
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7304 LESGRYDFYPLyEIQTQSAQKQELINHLLVFENYPMDEQVEQAGGDDSG--TLSITDVDVAEHTNYNFTVTVFPgDEIVV 7381
Cdd:PRK12316 2915 LGAQAHQDLPF-EQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGlhIESFAWDGAATQFDLALDTWESA-EGLGA 2992
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7382 RFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEIIHVFNNTAAEYAREQTIHGLFEEQAERMPE 7461
Cdd:PRK12316 2993 SLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPD 3072
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7462 KAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLED 7541
Cdd:PRK12316 3073 AVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLED 3152
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7542 SGAQVLLTQRHLQECVSfDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAET 7621
Cdd:PRK12316 3153 SGAQLLLSQSHLRLPLA-QGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA 3231
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7622 LRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGI-TAAILPPTYAIYLS---PDRLP 7697
Cdd:PRK12316 3232 YGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVdVLHAYPSMLQAFLEeedAHRCT 3311
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7698 SLKKLITGGSAASVEFVQQWKDKVRYFNAYGPTEASIVTSVWAASPDGLDlrSVPIGRPIANHQIFIVDSQNHMLPVGVA 7777
Cdd:PRK12316 3312 SLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKD--AVPIGRPIANRACYILDGSLEPVPVGAL 3389
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7778 GELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKI 7857
Cdd:PRK12316 3390 GELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEH 3469
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7858 ASVQETIVIArgdaNGQQQLCAYFVADRELTV--SELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSM 7935
Cdd:PRK12316 3470 PWVREAVVLA----VDGRQLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7936 QTgADFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVnKELNVNLPLRDIFRFPTVEALAQVID 8015
Cdd:PRK12316 3546 LQ-QDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLARVAR 3623
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8016 GLEQEEHSAIPVIGEReyyPVSSAQKRLFILHQLEgaQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGF-EMA 8094
Cdd:PRK12316 3624 VGGGVAVDQGPVSGET---LLLPIQQQFFEEPVPE--RHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFvEDA 3698
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8095 NGEPVQRVYSDVEFAVEYSK--ADREEAVEIAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQE 8172
Cdd:PRK12316 3699 GGWTAEHLPVELGGALLWRAelDDAEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLE 3778
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8173 EFSRLYA----GE--ELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYW---LQTLAGELPVIELPTDYERTSTRSFEGAeL 8243
Cdd:PRK12316 3779 DLQQAYQqllqGEapRLPAKTSSFKAWAERLQEHARGEALKAELAYWqeqLQGVSSELPCDHPQGALQNRHAASVQTR-L 3857
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8244 EFEADEALTQrlnELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGR----THADVEPIIGMFVNTLAIRNYPA 8319
Cdd:PRK12316 3858 DRELTRRLLQ---QAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGRedlfADIDLSRTVGWFTSLFPVRLSPV 3934

                  ..
gi 386647928 8320 GD 8321
Cdd:PRK12316 3935 ED 3936
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
7451-7932 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 755.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 7610
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7611 LCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAIY 7690
Cdd:cd17655   162 VVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7691 LSPDRL---PSLKKLITGGSAASVEFVQQWKDK----VRYFNAYGPTEASIVTSVWAASPDGLDLRSVPIGRPIANHQIF 7763
Cdd:cd17655   242 LDAADDsegLSLKHLIVGGEALSTELAKKIIELfgtnPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRIY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7764 IVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGY 7843
Cdd:cd17655   322 ILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7844 RIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:cd17655   402 RIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKV 481

                  ....*....
gi 386647928 7924 DRNALPAPE 7932
Cdd:cd17655   482 DRKALPEPD 490
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
5939-6420 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 748.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5939 QLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPD 6018
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6019 YPEDRIRYMLEDSGAKLLLVQGHLLDRASfADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHR 6098
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAG-GLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6099 NVVRLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQ 6178
Cdd:cd12117   160 GVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6179 LSQQDSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEA--VPIGKPINNSTAYI 6256
Cdd:cd12117   240 LADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAgsIPIGRPIANTRVYV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6257 VDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYR 6336
Cdd:cd12117   320 LDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6337 IELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:cd12117   400 IELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVD 479

                  ....
gi 386647928 6417 RRAL 6420
Cdd:cd12117   480 RRAL 483
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
264-747 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 743.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  264 RLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPE 343
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  344 YPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTwIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHR 423
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEV-AVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  424 NIIRVVKNTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNV 503
Cdd:cd12117   160 GVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  504 LVDMNPDCLRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAIYI 583
Cdd:cd12117   240 LADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANTRVYV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  584 VNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFR 663
Cdd:cd12117   320 LDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  664 IELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVD 743
Cdd:cd12117   400 IELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVD 479

                  ....
gi 386647928  744 RRAL 747
Cdd:cd12117   480 RRAL 483
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
3859-4341 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 740.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY 3938
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 PEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 4018
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4019 LCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAY 4098
Cdd:cd17655   162 VVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4099 LNPDRM---PSLKKLITGGSAASVEFVQQWKDK----VLYFNAYGPTEASIVTSIW--DEASDSLGdrkSVPIGRPLANH 4169
Cdd:cd17655   242 LDAADDsegLSLKHLIVGGEALSTELAKKIIELfgtnPTITNAYGPTETTVDASIYqyEPETDQQV---SVPIGKPLGNT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4170 RIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKI 4249
Cdd:cd17655   319 RIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKI 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4250 RGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPN 4329
Cdd:cd17655   399 RGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPN 478
                         490
                  ....*....|..
gi 386647928 4330 GKIDRKALPAPE 4341
Cdd:cd17655   479 GKVDRKALPEPD 490
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
2349-2831 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 737.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2349 QLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPE 2428
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2429 YPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHH 2508
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2509 GLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAV 2588
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2589 YLNP-DHMPDF--KRLIAAGSASSLELLQQWKDK----VKYFNAYGPTEDSICTTIWTPSTEDISQlKSVPIGGPIVNHR 2661
Cdd:cd17655   241 LLDAaDDSEGLslKHLIVGGEALSTELAKKIIELfgtnPTITNAYGPTETTVDASIYQYEPETDQQ-VSVPIGKPLGNTR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2662 IYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIR 2741
Cdd:cd17655   320 IYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2742 GYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNG 2821
Cdd:cd17655   400 GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNG 479
                         490
                  ....*....|
gi 386647928 2822 KIDRKALPAP 2831
Cdd:cd17655   480 KVDRKALPEP 489
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
264-751 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 710.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  264 RLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPE 343
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  344 YPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHR 423
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  424 NIIRVVKN-TNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFN 502
Cdd:cd17655   161 GVVNLVEWaNKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  503 VLVDMNPDCLRHARAILFGGERVSVSHVRKALGHLGPG-KIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAI 581
Cdd:cd17655   241 LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  582 YIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRG 661
Cdd:cd17655   321 YILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  662 FRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGK 741
Cdd:cd17655   401 YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGK 480
                         490
                  ....*....|
gi 386647928  742 VDRRALPAPE 751
Cdd:cd17655   481 VDRKALPEPD 490
PRK12316 PRK12316
peptide synthase; Provisional
7-1140 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 707.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    7 ERETAFWNKIFeGEENPPTALPYSKAQKQAPALV-RRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSSS 85
Cdd:PRK12316  237 ERQLEYWRAQL-GEEHPVLELPTDHPRPAVPSYRgSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQT 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   86 SILVGMPVVtkpNENRRPVNQLV-------ILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYA---- 154
Cdd:PRK12316  316 DIRVGVPIA---NRNRAEVEGLIgffvntqVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSlshs 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  155 -------DGVPVVNTLVALKQ---LHITDY-RQSAVSDvlFEFELDKDEV--RLH--LTYNGNLYTESFIAQAVDHLNRL 219
Cdd:PRK12316  393 plfqvmyNHQPLVADIEALDTvagLEFGQLeWKSRTTQ--FDLTLDTYEKggRLHaaLTYATDLFEARTVERMARHWQNL 470
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  220 FSVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLA 299
Cdd:PRK12316  471 LRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLA 550
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  300 RTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSG--TW 377
Cdd:PRK12316  551 HALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAgvQV 630
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  378 IRLDDEEAYHEDGS--NLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIrvvkntNYIDVTGQ-------DKLLQLSS 448
Cdd:PRK12316  631 LDLDRPAAWLEGYSeeNPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALS------NRLCWMQQayglgvgDTVLQKTP 704
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  449 YSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVM-FITTAFFNVLVDMNPDCLRHARAILFGGERVSV 527
Cdd:PRK12316  705 FSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLhFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPA 784
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  528 SHVRKALGHLGPGKIKHVYGPTESTVFATSYDVheVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLA 607
Cdd:PRK12316  785 DAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLA 862
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  608 RGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVvr 687
Cdd:PRK12316  863 RGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL-- 940
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  688 esANGEKQLCAYYVADRslPANEVRSTLSQ----ELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGvEFVEP 763
Cdd:PRK12316  941 --AVDGKQLVGYVVLES--EGGDWREALKAhlaaSLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ-GYVAP 1015
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  764 RTELEAGIVNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLhKELNISLPLRDVFRYPTVEKLAEAISGMGEQVYSS 843
Cdd:PRK12316 1016 RNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRA-RQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQ 1094
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  844 IPAAEAreyYPLSSAQKRLYilHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYP 923
Cdd:PRK12316 1095 GPASGE---VALAPVQRWFF--EQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAA 1169
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  924 EVEFAVEHIR--ANEEEADAAVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY--GG 999
Cdd:PRK12316 1170 PQAGEVLWQRqaASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYadLD 1249
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1000 EDLPALRIQYKDYAVWQQSEAQKEqlKRQEAYWLEVFRGELPvlEMPTDYARPAVQSYAGNALRFELDA-QKREGLQRIA 1078
Cdd:PRK12316 1250 ADLPARTSSYQAWARRLHEHAGAR--AEELDYWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAeRTRQLLQEAP 1325
                        1130      1140      1150      1160      1170      1180
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1079 SENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTH----GDLHPLIGMFVNTLAIRNYPAAD 1140
Cdd:PRK12316 1326 AAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDlfedIDLSRTVGWFTSLFPVRLTPAAD 1391
PRK05691 PRK05691
peptide synthase; Validated
3383-4729 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 700.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3383 QISGQTQHLGDIENI-----YALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHS 3457
Cdd:PRK05691 1709 QAAGERNSQGAIARVdrsqpVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPS 1788
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3458 gWRGEPLQIVYRYKPVEFAYEDLRHLAEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDG 3537
Cdd:PRK05691 1789 -VDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEG 1867
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3538 WCLPLIAKELFDTYEAYLrnDLSERPAAPSYSHYI-------EWLEKQDMEAAARYWTGFLAGYDSQTTLP--------- 3601
Cdd:PRK05691 1868 WAMDIFARELGALYEAFL--DDRESPLEPLPVQYLdysvwqrQWLESGERQRQLDYWKAQLGNEHPLLELPadrprppvq 1945
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3602 --QGKLHNKDgeyteanilrsLGKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAgiEE 3679
Cdd:PRK05691 1946 shRGELYRFD-----------LSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPES--EG 2012
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3680 MIGLFINTIPVRVSCEAEQSFADVMKRVQEAALESGGYDYYPLYEI-----QAQSAQKQDLITHIMAFENFPMDEQIEQA 3754
Cdd:PRK05691 2013 LIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLvealqPPRSAAYNPLFQVMCNVQRWEFQQSRQLA 2092
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3755 GSYEDgklaiTDVDIAEQTNYDFTLVVMP-GEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTE 3833
Cdd:PRK05691 2093 GMTVE-----YLVNDARATKFDLNLEVTDlDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAA 2167
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3834 AEKAEIIHVFNNTAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVER 3913
Cdd:PRK05691 2168 AEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALER 2247
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3914 SLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVA---VDDEQAYHADGSNLEP- 3989
Cdd:PRK05691 2248 SLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVArwcLEDDAAALAAYSDAPLp 2327
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3990 -VVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTS 4068
Cdd:PRK05691 2328 fLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQ 2407
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4069 TTiLDYPLFESYMNENGITATILPPTYAAYL------NPDRMPsLKKLITGGSAASVEFVQQWKDKV---LYFNAYGPTE 4139
Cdd:PRK05691 2408 GQ-WGAEEICQLIREQQVSILGFTPSYGSQLaqwlagQGEQLP-VRMCITGGEALTGEHLQRIRQAFapqLFFNAYGPTE 2485
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4140 aSIVTSIWDEASDSL-GDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEP 4218
Cdd:PRK05691 2486 -TVVMPLACLAPEQLeEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAA 2564
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4219 -GERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAReDANGQQQLVAYFV------ 4291
Cdd:PRK05691 2565 dGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVsavagq 2643
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4292 ---AQRELTAAeLRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPEGSMhAGGEYVAPRTPTEAKLAHIWQDV 4368
Cdd:PRK05691 2644 ddeAQAALREA-LKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPEL-NRQAYQAPRSELEQQLAQIWREV 2721
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4369 LGLEKVGVKDNFFELGGHSLRATALASKVRkELNMELPLRHIFQFPTVEQLAEAIGQLEQQEFDAIPVVEEREYYPVSSA 4448
Cdd:PRK05691 2722 LNVERVGLGDNFFELGGDSILSIQVVSRAR-QLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGLTPIQHW 2800
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4449 QKRLYILQQlegaaQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGE-PVQRIYPEVDFAVETVQ-ASE 4526
Cdd:PRK05691 2801 FFDSPVPQP-----QHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRwQAEYRAVTAQELLWQVTvADF 2875
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4527 QEAKAIVRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLY------SGEELPGLRIQYK 4600
Cdd:PRK05691 2876 AECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYrqlsagAEPALPAKTSAFR 2955
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4601 DYAVWQQSEAQKEQLKRQEAYWLEAFRGelPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAESGAT-LYMVL 4679
Cdd:PRK05691 2956 DWAARLQAYAGSESLREELGWWQAQLGG--PRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTqVNDLL 3033
                        1370      1380      1390      1400      1410
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4680 LAAYTVLLQKYTAQEDVIVGTPIAGRTHA----DLQSLIGMFVNTLAIRNYPAA 4729
Cdd:PRK05691 3034 LTALARVLCRWSGQPSVLVQLEGHGREALfddiDLTRSVGWFTSAYPLRLTPAP 3087
PRK12316 PRK12316
peptide synthase; Provisional
7-1140 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 694.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    7 ERETAFWNKIFEGEEnPPTALPYSKAQ-KQAPALVRRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSSS 85
Cdd:PRK12316 2786 ARQLDYWRERLGGEQ-PVLELPLDRPRpALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQS 2864
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   86 SILVGMPVVtkpNENRRPVNQLV-------ILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLE-------- 150
Cdd:PRK12316 2865 DIRVGVPIA---NRNRAETERLIgffvntqVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQperslshs 2941
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  151 ------LQYADGVPVVNTLVALKQLHITDYRQSAVSDVLFEFELDKDEVRLHLTYNGNLYTESFIAQAVDHLNRLFSVVL 224
Cdd:PRK12316 2942 plfqvmYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMV 3021
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  225 FQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRN 304
Cdd:PRK12316 3022 ENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIE 3101
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  305 AGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWIRLD-DE 383
Cdd:PRK12316 3102 RGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDrGD 3181
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  384 EAYHEdgSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNI-IRVVKNTNYIDVTGQDKLLQLSSYSFDGSTFDIFGAL 462
Cdd:PRK12316 3182 ENYAE--ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALsNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPL 3259
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  463 LNGAKLVLVPKETVLDVAKLAGLIEKQQISVM-FITTAFFNVLVDMNPDCLRHARAILFGGERVSVSHVRKALGHLgpgK 541
Cdd:PRK12316 3260 MSGARVVLAGPEDWRDPALLVELINSEGVDVLhAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGL---P 3336
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  542 IKHVYGPTESTVFATSYDVheVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKF 621
Cdd:PRK12316 3337 LYNLYGPTEATITVTHWQC--VEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERF 3414
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  622 ADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVvresANGEKQLCAYYV 701
Cdd:PRK12316 3415 VPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVV 3490
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  702 ADRSLPA--NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETgVEFVEPRTELEAGIVNIWKEIL 779
Cdd:PRK12316 3491 PEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQ-QDYVAPVNELERRLAAIWADVL 3569
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  780 KIEKISVKDSFFELGGHSLRATTMVSRLhKELNISLPLRDVFRYPTVEKLAEAISGMGEQVYSSIPAAEAReyyPLSSAQ 859
Cdd:PRK12316 3570 KLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGET---LLLPIQ 3645
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  860 KRLYILHQLEgaEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYP-----EVEFAVEHIRA 934
Cdd:PRK12316 3646 QQFFEEPVPE--RHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPvelggALLWRAELDDA 3723
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  935 NEEEADAAVKQfiRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYG----GE--DLPALRIQ 1008
Cdd:PRK12316 3724 EELERLGEEAQ--RSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQqllqGEapRLPAKTSS 3801
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1009 YKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPvlEMPTDYARPAVQSYAGNALRFELDAQ-KREGLQRIASENGATLYM 1087
Cdd:PRK12316 3802 FKAWAERLQEHARGEALKAELAYWQEQLQGVSS--ELPCDHPQGALQNRHAASVQTRLDRElTRRLLQQAPAAYRTQVND 3879
                        1130      1140      1150      1160      1170
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1088 VLLAAYTILLQKYTGQEDVVIGTPIAGR----THGDLHPLIGMFVNTLAIRNYPAAD 1140
Cdd:PRK12316 3880 LLLTALARVVCRWTGEASALVQLEGHGRedlfADIDLSRTVGWFTSLFPVRLSPVED 3936
PRK05691 PRK05691
peptide synthase; Validated
6975-8319 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 694.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6975 QISAQTRNVGEIENIYTLTPM-----QKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFS 7049
Cdd:PRK05691 1709 QAAGERNSQGAIARVDRSQPVplsysQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPS 1788
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7050 gPRGEPLQIVYRDKRIGFVYEDLSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDG 7129
Cdd:PRK05691 1789 -VDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEG 1867
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7130 WCLPLVVKELFETYEAYVQGDrpEQKAAPAYSQYI-------EWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSE 7202
Cdd:PRK05691 1868 WAMDIFARELGALYEAFLDDR--ESPLEPLPVQYLdysvwqrQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQ 1945
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7203 GYVAEHVVCELDKELSERMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAeiPGIEEMIGLFINTIPV 7282
Cdd:PRK05691 1946 SHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIR--PESEGLIGAFLNTQVL 2023
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7283 RVACQPEESFADVMGRMQEAALESGRYDFYPLYEI-----QTQSAQKQELINHLLVFENYPMDEQVEQAG-------GDD 7350
Cdd:PRK05691 2024 RCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLvealqPPRSAAYNPLFQVMCNVQRWEFQQSRQLAGmtveylvNDA 2103
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7351 SGT-----LSITDVDvaehtnynftvtvfpgDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATA 7425
Cdd:PRK05691 2104 RATkfdlnLEVTDLD----------------GRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAA 2167
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7426 AEKVEIIHVFNNTAAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIER 7505
Cdd:PRK05691 2168 AEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALER 2247
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7506 SLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQE------------CVSFDGKVIAAddeqayg 7573
Cdd:PRK05691 2248 SLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEalgelpagvarwCLEDDAAALAA------- 2320
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7574 EDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGA 7653
Cdd:PRK05691 2321 YSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGA 2400
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7654 TLYIPAKDTiLDYPLFESYMNENGITAAILPPTY----AIYLSP--DRLPsLKKLITGGSAASVEFVQQWKDKVR---YF 7724
Cdd:PRK05691 2401 RVVLRAQGQ-WGAEEICQLIREQQVSILGFTPSYgsqlAQWLAGqgEQLP-VRMCITGGEALTGEHLQRIRQAFApqlFF 2478
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7725 NAYGPTEaSIVTSVWAASPDGL--DLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKF 7802
Cdd:PRK05691 2479 NAYGPTE-TVVMPLACLAPEQLeeGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERF 2557
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7803 VDNPFLA-GERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARgDANGQQQLCAYF 7881
Cdd:PRK05691 2558 VADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYL 2636
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7882 VADRELTVSE--------LRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSMQTGAdFVEPRTPVEAELA 7953
Cdd:PRK05691 2637 VSAVAGQDDEaqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQA-YQAPRSELEQQLA 2715
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7954 RIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVnKELNVNLPLRDIFRFPTVEALAQVIDGLEQEEHSAIPVIGEREY 8033
Cdd:PRK05691 2716 QIWREVLNVERVGLGDNFFELGGDSILSIQVVSRA-RQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGL 2794
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8034 YPVssaQKRLFILHQLEgaQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGE--PVQRVYSDVEFAVE 8111
Cdd:PRK05691 2795 TPI---QHWFFDSPVPQ--PQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRwqAEYRAVTAQELLWQ 2869
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8112 YSKADREEAVEIAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLY------AGEELPP 8185
Cdd:PRK05691 2870 VTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYrqlsagAEPALPA 2949
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8186 LRIQYKDYAAwqRSEAYA--KRVKQQEGYWLQTLAGelPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELA-ARH 8262
Cdd:PRK05691 2950 KTSAFRDWAA--RLQAYAgsESLREELGWWQAQLGG--PRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQApAAY 3025
                        1370      1380      1390      1400      1410      1420
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 8263 ESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHA----DVEPIIGMFVNTLAIRNYPA 8319
Cdd:PRK05691 3026 RTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALfddiDLTRSVGWFTSAYPLRLTPA 3086
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
5939-6423 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 692.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5939 QLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPD 6018
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6019 YPEDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHR 6098
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6099 NVVRLVKN-TNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYN 6177
Cdd:cd17655   161 GVVNLVEWaNKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6178 QLSQQDSGMFAGLKTLIVGGDVLSVPHINRVL-REHAGLSIVNGYGPTENTTFSTTHTIVGE--QKEAVPIGKPINNSTA 6254
Cdd:cd17655   241 LLDAADDSEGLSLKHLIVGGEALSTELAKKIIeLFGTNPTITNAYGPTETTVDASIYQYEPEtdQQVSVPIGKPLGNTRI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6255 YIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRG 6334
Cdd:cd17655   321 YILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6335 YRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGK 6414
Cdd:cd17655   401 YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGK 480

                  ....*....
gi 386647928 6415 IDRRALPAP 6423
Cdd:cd17655   481 VDRKALPEP 489
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
3868-4337 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 668.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQrhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 4027
Cdd:cd05930    81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4028 NTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAA----YLNPDR 4103
Cdd:cd05930   127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRlllqELELAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4104 MPSLKKLITGGSAASVEFVQQWKD---KVLYFNAYGPTEASIVTSIWDEASDSLGDRkSVPIGRPLANHRIYVVDSHNRM 4180
Cdd:cd05930   207 LPSLRLVLVGGEALPPDLVRRWREllpGARLVNLYGPTEATVDATYYRVPPDDEEDG-RVPIGRPIPNTRVYVLDENLRP 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4181 LPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVE 4260
Cdd:cd05930   286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 4261 TQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQR--ELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05930   366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
7460-7928 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 666.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQrhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 7619
Cdd:cd05930    81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7620 ETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYA----IYLSPDR 7695
Cdd:cd05930   127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLrlllQELELAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7696 LPSLKKLITGGSAASVEFVQQWKD---KVRYFNAYGPTEASIVTSVWAASPDGLDLRSVPIGRPIANHQIFIVDSQNHML 7772
Cdd:cd05930   207 LPSLRLVLVGGEALPPDLVRRWREllpGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPV 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7773 PVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEE 7852
Cdd:cd05930   287 PPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7853 QLLKIASVQETIVIARGDANGQQQLCAYFVADR--ELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05930   367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
4901-5385 0e+00

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 654.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTQthlqeraqqwgqtlqaalclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd17650    81 EDSGAKLLLTQ--------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 5140
Cdd:cd17650   123 HAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5141 VAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALNAKFY 5220
Cdd:cd17650   203 VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMY 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5221 IVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGY 5300
Cdd:cd17650   283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5301 RIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:cd17650   363 RIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442

                  ....*
gi 386647928 5381 DRKAL 5385
Cdd:cd17650   443 DRRAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1311-1795 0e+00

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 654.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1311 PEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 1390
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1391 EDSAASVLLTQthlqeraqqwgqtlqavlclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 1470
Cdd:cd17650    81 EDSGAKLLLTQ--------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 1550
Cdd:cd17650   123 HAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1551 VAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALNAKFY 1630
Cdd:cd17650   203 VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMY 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1631 IVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGY 1710
Cdd:cd17650   283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1711 RIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:cd17650   363 RIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442

                  ....*
gi 386647928 1791 DRKAL 1795
Cdd:cd17650   443 DRRAL 447
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
274-747 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 652.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN 433
Cdd:cd05930    81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  434 -YIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCL 512
Cdd:cd05930   127 eAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  513 RHA-RAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQ 591
Cdd:cd05930   207 LPSlRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPV 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  592 PIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEA 671
Cdd:cd05930   287 PPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  672 HLLKLEAIEKATVVVRESANGEKQLCAYYVADR--SLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05930   367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
2359-2828 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 651.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQrrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA 2518
Cdd:cd05930    81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAV----YLNPDH 2594
Cdd:cd05930   127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRlllqELELAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2595 MPDFKRLIAAGSASSLELLQQWKD---KVKYFNAYGPTEDSICTTIWTPSTEDIsQLKSVPIGGPIVNHRIYIVDAHYQP 2671
Cdd:cd05930   207 LPSLRLVLVGGEALPPDLVRRWREllpGARLVNLYGPTEATVDATYYRVPPDDE-EDGRVPIGRPIPNTRVYVLDENLRP 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2672 VPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIE 2751
Cdd:cd05930   286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2752 EQLLKVASVQEAIVIAHDDASGQKQLCAYFVADR--TMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05930   366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1302-1799 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 639.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1302 LFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 1381
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1382 PSDRIQFMLEDSAASVLLTQTHLQERAQQwgqtLQAVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMI 1461
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIAF----IGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1462 EHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTP 1541
Cdd:cd17655   158 EHRGVVNLVEWANKVIYQGE-HLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 ALI--IPFMDYVAEHgldmsSMELLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYD-EPlaKLPEAGNV 1618
Cdd:cd17655   237 AHLklLDAADDSEGL-----SLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQyEP--ETDQQVSV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1619 PIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFI 1698
Cdd:cd17655   310 PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1699 GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQ 1778
Cdd:cd17655   390 GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIK 469
                         490       500
                  ....*....|....*....|.
gi 386647928 1779 LEQLPLTANGKIDRKALPAPD 1799
Cdd:cd17655   470 LDEIPLTPNGKVDRKALPEPD 490
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
5949-6420 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 637.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQghlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTN 6108
Cdd:cd05930    81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6109 -YVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQ-DSGM 6186
Cdd:cd05930   127 eAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQElELAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6187 FAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTI--VGEQKEAVPIGKPINNSTAYIVDSKLSLL 6264
Cdd:cd05930   207 LPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVppDDEEDGRVPIGRPIPNTRVYVLDENLRPV 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6265 PVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEE 6344
Cdd:cd05930   287 PPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 6345 QLLKVASVKEATVIVREDESGQKQLCAYFVAER--ELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05930   367 ALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
4892-5389 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 633.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4892 LFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 4971
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4972 PSDRIQFMLEDSAASVLLTQTHLQERAQQwgqtLQAALCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMI 5051
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIAF----IGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5052 EHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTP 5131
Cdd:cd17655   158 EHRGVVNLVEWANKVIYQGE-HLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 ALI--IPFMDYVAEHgldmsSMVLLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYD-EPlaKLPEAGNV 5208
Cdd:cd17655   237 AHLklLDAADDSEGL-----SLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQyEP--ETDQQVSV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5209 PIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFI 5288
Cdd:cd17655   310 PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5289 GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQ 5368
Cdd:cd17655   390 GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIK 469
                         490       500
                  ....*....|....*....|.
gi 386647928 5369 LEQLPLTANGKIDRKALPAPD 5389
Cdd:cd17655   470 LDEIPLTPNGKVDRKALPEPD 490
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1902-2913 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 633.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1902 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYR 1981
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEII 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1982 --TSEAEAGEVVRGFVRTfDLAKP-------PLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNG----- 2047
Cdd:PRK10252   89 dlRTQPDPHAAAQALMQA-DLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrge 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2048 ----ESLATLRIQYKDYAVWQQSEeqleRVKRQEAYWLDMFRGeLPvlEMPTDYPRPAVRRFEGST---LSFRLDAGLNE 2120
Cdd:PRK10252  168 ptpaSPFTPFADVVEEYQRYRASE----AWQRDAAFWAEQRRQ-LP--PPASLSPAPLPGRSASADilrLKLEFTDGAFR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2121 ALkrVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKE 2200
Cdd:PRK10252  241 QL--AAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2201 TTLGAYEHQTYPFEELVeklqvpRDLSR----NPIFDAMFVLQNTEnEELQLDGLK-----LAPYPsgntIARFDLTLDV 2271
Cdd:PRK10252  319 QLKKMRRHQRYDAEQIV------RDSGRaagdEPLFGPVLNIKVFD-YQLDFPGVQaqthtLATGP----VNDLELALFP 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2272 TETGsGLECNLEYATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQTQLHHVfNATAADYeADKTIHQLF 2351
Cdd:PRK10252  388 DEHG-GLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQV-NATAVEI-PETTLSALV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2352 EEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPE 2431
Cdd:PRK10252  465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2432 DRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLC 2511
Cdd:PRK10252  545 DRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2512 S-LKQMfANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPT----Y 2586
Cdd:PRK10252  625 NrLLWM-QNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSmlaaF 703
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2587 AVYLNPDHMPD----FKRLIAAGSASSLELLQQWKD--KVKYFNAYGPTEDSICTTIWTPSTEDISQLK--SVPIGGPIV 2658
Cdd:PRK10252  704 VASLTPEGARQscasLRQVFCSGEALPADLCREWQQltGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRgsSVPIGYPVW 783
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2659 NHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQV 2738
Cdd:PRK10252  784 NTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2739 KIRGYRIELGEIEEQLLKVASVQEAIVIA----HDDASG--QKQLCAYFVADRTMT--VGELRGELSGELPGYMIPAHFV 2810
Cdd:PRK10252  864 KIRGQRIELGEIDRAMQALPDVEQAVTHAcvinQAAATGgdARQLVGYLVSQSGLPldTSALQAQLRERLPPHMVPVVLL 943
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2811 QLERMPLTPNGKIDRKALPAPQGNASAGADyvAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDSIKSIQVSSRLHQ 2890
Cdd:PRK10252  944 QLDQLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSR 1021
                        1050      1060
                  ....*....|....*....|....
gi 386647928 2891 A-GYKLEIRDLFKYPTVAQLSKHI 2913
Cdd:PRK10252 1022 QfARQVTPGQVMVASTVAKLATLL 1045
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
852-1264 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 623.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  852 YYPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVEH 931
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 I-------RANEEEADAAVKQFI-RAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGE--- 1000
Cdd:cd19531    81 VdlsglpeAEREAEAQRLAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1001 ---DLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRI 1077
Cdd:cd19531   161 rpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1078 ASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGA 1157
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1158 FERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEFRLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFLCGIEYA 1237
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
                         410       420
                  ....*....|....*....|....*..
gi 386647928 1238 TALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19531   401 TDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
3859-4337 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 621.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY 3938
Cdd:cd12117     2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 PEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVaVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 4018
Cdd:cd12117    82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAV-VIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4019 LCSLKLMfANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILppTYA-- 4096
Cdd:cd12117   161 VVRLVKN-TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWL--TAAlf 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4097 ---AYLNPDRMPSLKKLITGGSAASVEFVQQWKDK---VLYFNAYGPTEASIVTSIWDEASDSLGDRkSVPIGRPLANHR 4170
Cdd:cd12117   238 nqlADEDPECFAGLRELLTGGEVVSPPHVRRVLAAcpgLRLVNGYGPTENTTFTTSHVVTELDEVAG-SIPIGRPIANTR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4171 IYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIR 4250
Cdd:cd12117   317 VYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4251 GYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNG 4330
Cdd:cd12117   397 GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANG 476

                  ....*..
gi 386647928 4331 KIDRKAL 4337
Cdd:cd12117   477 KVDRRAL 483
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
4442-4854 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 618.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4442 YYPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAVET 4521
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4522 VQAS-------EQEAKAIVRDFI-RPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGE--- 4590
Cdd:cd19531    81 VDLSglpeaerEAEAQRLAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4591 ---ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRI 4667
Cdd:cd19531   161 rpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4668 AAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGA 4747
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4748 FEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEMHLPGLHLTPYPTEYGMSKFDLSLDMMEDSEGLECSLEFA 4827
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
                         410       420
                  ....*....|....*....|....*..
gi 386647928 4828 TALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19531   401 TDLFDAATIERMAGHFQTLLEAIVADP 427
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
854-1882 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 617.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  854 PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVEHIR 933
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEII 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  934 ANEEEAD--AAVKQFIRAfDLAKP-------PLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGG----- 999
Cdd:PRK10252   89 DLRTQPDphAAAQALMQA-DLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrge 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1000 ----EDLPALRIQYKDYAVWQQSEAQKeqlkRQEAYWLEVFRGELPVLEMPTdyARPAVQSYAGNALRFELDAQKREGLQ 1075
Cdd:PRK10252  168 ptpaSPFTPFADVVEEYQRYRASEAWQ----RDAAFWAEQRRQLPPPASLSP--APLPGRSASADILRLKLEFTDGAFRQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1076 RIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTL 1155
Cdd:PRK10252  242 LAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLK 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1156 GAFERQDYPFEELVDKLKLARDlsRNPLFDTMFTLQNTEnKEFRLPGLQ-----LTPYPVEehtskfDLSLDIMESGDGF 1230
Cdd:PRK10252  322 KMRRHQRYDAEQIVRDSGRAAG--DEPLFGPVLNIKVFD-YQLDFPGVQaqthtLATGPVN------DLELALFPDEHGG 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1231 L-CGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEEkAQLVHVFNPAAPDAPEnEVFHALFEKQAER 1309
Cdd:PRK10252  393 LsIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGE-YAQLAQVNATAVEIPE-TTLSALVAQQAAK 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1310 TPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFM 1389
Cdd:PRK10252  471 TPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1390 LEDSAASVLLTQTHLQERAQqwGQTLQAVLCLDdeAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNt 1469
Cdd:PRK10252  551 LEDARPSLLITTADQLPRFA--DVPDLTSLCYN--APLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN- 625
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1470 aagyRREYRLDQFPV----RLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALII 1545
Cdd:PRK10252  626 ----RLLWMQNHYPLtaddVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLA 701
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1546 PFMDYVAEHGLDMS--SMELLITSSDSCSVTDYRVLQERFGSQFRiiNAYGVTEAAIDSSLYD---EPLAKLPEAgNVPI 1620
Cdd:PRK10252  702 AFVASLTPEGARQScaSLRQVFCSGEALPADLCREWQQLTGAPLH--NLYGPTEAAVDVSWYPafgEELAAVRGS-SVPI 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1621 GKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGR 1700
Cdd:PRK10252  779 GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGR 858
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1701 IDNQAKIRGYRIETGEIETQLLK----AEGVREAVVVVREDAKG--QKVLCAYFTAESELKL--SELRSSLSQELPGYMI 1772
Cdd:PRK10252  859 SDDQLKIRGQRIELGEIDRAMQAlpdvEQAVTHACVINQAAATGgdARQLVGYLVSQSGLPLdtSALQAQLRERLPPHMV 938
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1773 PSYFVQLEQLPLTANGKIDRKALPAPDASMQTGMEyvAPRTPQEAKLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLV 1852
Cdd:PRK10252  939 PVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLA 1016
                        1050      1060      1070
                  ....*....|....*....|....*....|
gi 386647928 1853 GKVHKEMNVELPLRDVFRCSTVEEMAQAIA 1882
Cdd:PRK10252 1017 AQLSRQFARQVTPGQVMVASTVAKLATLLD 1046
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
6991-8028 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 612.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6991 TLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPrGEPLQIVYRDKRIGFV-Y 7069
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDN-GEVWQWVDPALTFPLPeI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7070 EDLSHLPADERQASVerLEQEDIARGFDLEQD-ALVRVAVIRTQETsyRVLW--SFHHILMDGWCLPLVVKELFETYEAY 7146
Cdd:PRK10252   88 IDLRTQPDPHAAAQA--LMQADLQQDLRVDSGkPLVFHQLIQLGDN--RWYWyqRYHHLLVDGFSFPAITRRIAAIYCAW 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7147 VQGDRPEQKAAPAYS----QYIEWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMN 7222
Cdd:PRK10252  164 LRGEPTPASPFTPFAdvveEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQLA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7223 RAAKQCRVT-VNTLMQAVWgviLQKYNATDDVVYGSVVSGR----PAEIPGieeMIglfINTIPVRVACQPEESFADVMG 7297
Cdd:PRK10252  244 AQASGVQRPdLALALVALW---LGRLCGRMDYAAGFIFMRRlgsaALTATG---PV---LNVLPLRVHIAAQETLPELAT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7298 RmQEAALES----GRYDFYPLYEIQTQSAQKQELinHLLVFENYPMDEQVEQAGGD-DSGTLSITDVDvaehtnyNFTVT 7372
Cdd:PRK10252  315 R-LAAQLKKmrrhQRYDAEQIVRDSGRAAGDEPL--FGPVLNIKVFDYQLDFPGVQaQTHTLATGPVN-------DLELA 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7373 VFPGDE--IVVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKvEIIHVFNNTAAEYArEQTIHG 7450
Cdd:PRK10252  385 LFPDEHggLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNATAVEIP-ETTLSA 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:PRK10252  463 LVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 7610
Cdd:PRK10252  543 PDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7611 LCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAA-ILPPTYAI 7689
Cdd:PRK10252  623 IVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPSMLAA 702
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7690 Y---LSPDRLP----SLKKLITGGSAASVEFVQQWKD--KVRYFNAYGPTEASIVTSVWAASPDGLDL---RSVPIGRPI 7757
Cdd:PRK10252  703 FvasLTPEGARqscaSLRQVFCSGEALPADLCREWQQltGAPLHNLYGPTEAAVDVSWYPAFGEELAAvrgSSVPIGYPV 782
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7758 ANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQ 7837
Cdd:PRK10252  783 WNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQ 862
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7838 VKIRGYRIELGEIEEQLLKIASVQETIVIAR----GDANG--QQQLCAYFVA--DRELTVSELRGTLSQELPGYMIPSYF 7909
Cdd:PRK10252  863 LKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqAAATGgdARQLVGYLVSqsGLPLDTSALQAQLRERLPPHMVPVVL 942
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7910 VQLEQMPLTPNGKIDRNALPAPEGSMQTGADfvEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVN 7989
Cdd:PRK10252  943 LQLDQLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLS 1020
                        1050      1060      1070
                  ....*....|....*....|....*....|....*....
gi 386647928 7990 KELNVNLPLRDIFRFPTVEALAQVIDGLEQEEHSAIPVI 8028
Cdd:PRK10252 1021 RQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLGFGT 1059
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
7451-7928 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 606.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:cd12117     2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLLTQRHLQECVSFDGkVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 7610
Cdd:cd12117    82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLE-VAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7611 LCSLKLmfaET--LRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILppTYA 7688
Cdd:cd12117   161 VVRLVK---NTnyVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWL--TAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7689 IY-----LSPDRLPSLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDGLDLRSVPIGRPIANH 7760
Cdd:cd12117   236 LFnqladEDPECFAGLRELLTGGEVVSPPHVRRVLAAcpgLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7761 QIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKI 7840
Cdd:cd12117   316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7841 RGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPN 7920
Cdd:cd12117   396 RGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTAN 475

                  ....*...
gi 386647928 7921 GKIDRNAL 7928
Cdd:cd12117   476 GKVDRRAL 483
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1900-2312 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 605.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1900 YYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEH 1979
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1980 -------YRTSEAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGES-- 2049
Cdd:cd19531    81 vdlsglpEAEREAEAQRLAREEARRpFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2050 ----LATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRV 2125
Cdd:cd19531   161 rpspLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2126 AAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGA 2205
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2206 YEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEELQLDGLKLAPYPSGNTIARFDLTLDVTETGSGLECNLEYA 2285
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
                         410       420
                  ....*....|....*....|....*..
gi 386647928 2286 TSLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19531   401 TDLFDAATIERMAGHFQTLLEAIVADP 427
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
3399-4423 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 604.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3399 ALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYKP-VEFAY 3477
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTED-NGEVWQWVDPALTfPLPEI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3478 EDLRHLAEAEWSA----YLDQLVNDDKTRGFDLEQDALMRVKvvrtqEEsfHVLW--SFHHILMDGWCLPLIAKELFDTY 3551
Cdd:PRK10252   88 IDLRTQPDPHAAAqalmQADLQQDLRVDSGKPLVFHQLIQLG-----DN--RWYWyqRYHHLLVDGFSFPAITRRIAAIY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3552 EAYLRNDlsERPAAP------SYSHYIEWLEKQDMEAAARYWTGFLAGYDSQTTLPQGKLhnkDGEYTEANILR----SL 3621
Cdd:PRK10252  161 CAWLRGE--PTPASPftpfadVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPL---PGRSASADILRlkleFT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3622 GKSLTERMSRIAKQHQVTVNTLMQAAWgiiLQKYNGTDDAVFGSVVSGR--SAEIagieEMIGLFINTIPVRVSCEAEQS 3699
Cdd:PRK10252  236 DGAFRQLAAQASGVQRPDLALALVALW---LGRLCGRMDYAAGFIFMRRlgSAAL----TATGPVLNVLPLRVHIAAQET 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3700 FADVMKRVQeAALES----GGYDYYPLYEIQAQSAQKQDL---ITHIMAFenfpmDEQIEQAGSyeDGK---LAITDVDi 3769
Cdd:PRK10252  309 LPELATRLA-AQLKKmrrhQRYDAEQIVRDSGRAAGDEPLfgpVLNIKVF-----DYQLDFPGV--QAQthtLATGPVN- 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3770 aeqtnyDFTLVVMPGEE--LAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAEIiHVFNNTA 3847
Cdd:PRK10252  380 ------DLELALFPDEHggLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQL-AQVNATA 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3848 AEYQqEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKA 3927
Cdd:PRK10252  453 VEIP-ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3928 GGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFA--GTFVAVDDEQAyhADGSNLEPVVGPNHLAYVIYTSGT 4005
Cdd:PRK10252  532 GAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVpdLTSLCYNAPLA--PQGAAPLQLSQPHHTAYIIFTSGS 609
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4006 TGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENG 4085
Cdd:PRK10252  610 TGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYG 689
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4086 ITAT-ILPPTYAAYLN-------PDRMPSLKKLITGGSAASVEFVQQWKDKV---LYfNAYGPTEASIVTSIWDEASDSL 4154
Cdd:PRK10252  690 VTTThFVPSMLAAFVAsltpegaRQSCASLRQVFCSGEALPADLCREWQQLTgapLH-NLYGPTEAAVDVSWYPAFGEEL 768
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4155 GDRK--SVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWL 4232
Cdd:PRK10252  769 AAVRgsSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWL 848
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4233 PDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAR------EDANGQQQLVAYFVAQRE--LTAAELRAT 4304
Cdd:PRK10252  849 DDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGlpLDTSALQAQ 928
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4305 MSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPEGSMHAGGEyvAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELG 4384
Cdd:PRK10252  929 LRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALG 1006
                        1050      1060      1070
                  ....*....|....*....|....*....|....*....
gi 386647928 4385 GHSLRATALASKVRKELNMELPLRHIFQFPTVEQLAEAI 4423
Cdd:PRK10252 1007 GHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLL 1045
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
2349-2828 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 604.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2349 QLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPE 2428
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2429 YPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVtVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHH 2508
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAV-VIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2509 GLCSLKQMfANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLppTYAV 2588
Cdd:cd12117   160 GVVRLVKN-TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWL--TAAL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2589 Y-----LNPDHMPDFKRLIAAGSASSLELLQQWKDK---VKYFNAYGPTEDSICTTiWTPSTEDISQLKSVPIGGPIVNH 2660
Cdd:cd12117   237 FnqladEDPECFAGLRELLTGGEVVSPPHVRRVLAAcpgLRLVNGYGPTENTTFTT-SHVVTELDEVAGSIPIGRPIANT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2661 RIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKI 2740
Cdd:cd12117   316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2741 RGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPN 2820
Cdd:cd12117   396 RGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTAN 475

                  ....*...
gi 386647928 2821 GKIDRKAL 2828
Cdd:cd12117   476 GKVDRRAL 483
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
6989-7413 0e+00

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 599.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6989 IYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPRGEPLQIVYRDKRIGFV 7068
Cdd:cd19543     1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7069 YEDLSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQ 7148
Cdd:cd19543    81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7149 GDRPEQKAAPAYSQYIEWLENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAKQC 7228
Cdd:cd19543   161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7229 RVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALESGR 7308
Cdd:cd19543   241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELRE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7309 YDFYPLYEIQTQSAQKQELINHLLVFENYPMDEQVEQAGGDDSgtLSITDVDVAEHTNYNFTVTVFPGDEIVVRFDYNSF 7388
Cdd:cd19543   321 HEYVPLYEIQAWSEGKQALFDHLLVFENYPVDESLEEEQDEDG--LRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAE 398
                         410       420
                  ....*....|....*....|....*
gi 386647928 7389 VFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19543   399 VFDEATIERLLGHLRRVLEQVAANP 423
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
5490-5902 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 598.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5490 YYPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEH 5569
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5570 -------YRTSEAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGES-- 5639
Cdd:cd19531    81 vdlsglpEAEREAEAQRLAREEARRpFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5640 ----LAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRI 5715
Cdd:cd19531   161 rpspLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5716 AAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGA 5795
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5796 YEHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSEGLELSMEYS 5875
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
                         410       420
                  ....*....|....*....|....*..
gi 386647928 5876 TALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19531   401 TDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
4901-5385 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 589.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTQthlqeraqqwgqtlqaalclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd05930    81 EDSGAKLVLTD--------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRLdQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 5140
Cdd:cd05930   123 LWMQEAYPL-TPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5141 VAEhgLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYDEPLAKLPEaGNVPIGKAALNAKFY 5220
Cdd:cd05930   202 LEL--AALPSLRLVLVGGEALPPDLVRRWRELLPGA-RLVNLYGPTEATVDATYYRVPPDDEED-GRVPIGRPIPNTRVY 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5221 IVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGY 5300
Cdd:cd05930   278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGY 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5301 RIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLPLTANG 5378
Cdd:cd05930   358 RIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDeeELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437

                  ....*..
gi 386647928 5379 KIDRKAL 5385
Cdd:cd05930   438 KVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1311-1795 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 588.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1311 PEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 1390
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1391 EDSAASVLLTQthlqeraqqwgqtlqavlclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 1470
Cdd:cd05930    81 EDSGAKLVLTD--------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGYRREYRLdQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 1550
Cdd:cd05930   123 LWMQEAYPL-TPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1551 VAEhgLDMSSMELLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYDEPLAKLPEaGNVPIGKAALNAKFY 1630
Cdd:cd05930   202 LEL--AALPSLRLVLVGGEALPPDLVRRWRELLPGA-RLVNLYGPTEATVDATYYRVPPDDEED-GRVPIGRPIPNTRVY 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1631 IVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGY 1710
Cdd:cd05930   278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGY 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1711 RIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLPLTANG 1788
Cdd:cd05930   358 RIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDeeELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437

                  ....*..
gi 386647928 1789 KIDRKAL 1795
Cdd:cd05930   438 KVDRKAL 444
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
3397-3821 0e+00

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 588.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3397 IYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGWRGEPLQIVYRYKPVEFA 3476
Cdd:cd19543     1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3477 YEDLRHLAEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLR 3556
Cdd:cd19543    81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3557 NDLSERPAAPSYSHYIEWLEKQDMEAAARYWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERMSRIAKQH 3636
Cdd:cd19543   161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3637 QVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAALESGG 3716
Cdd:cd19543   241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELRE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3717 YDYYPLYEIQAQSAQKQDLITHIMAFENFPMDEQIEQAGsyEDGKLAITDVDIAEQTNYDFTLVVMPGEELAVRFYYNAS 3796
Cdd:cd19543   321 HEYVPLYEIQAWSEGKQALFDHLLVFENYPVDESLEEEQ--DEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAE 398
                         410       420
                  ....*....|....*....|....*
gi 386647928 3797 VYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19543   399 VFDEATIERLLGHLRRVLEQVAANP 423
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
3868-4338 0e+00

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 583.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQrhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 4027
Cdd:cd17652    81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4028 NTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAYLNPDRMPSL 4107
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPDL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4108 KKLITGGSAASVEFVQQWKDKVLYFNAYGPTEASIVTSIwdeaSDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAG 4187
Cdd:cd17652   207 RTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATM----AGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPG 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4188 ELCISGVGLARGYLNRPELTAEKFVDNPF-EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKI 4266
Cdd:cd17652   283 ELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEH 362
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4267 DAVQEAIVLAREDANGQQQLVAYFVAQRE--LTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALP 4338
Cdd:cd17652   363 PGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
2359-2829 0e+00

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 582.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQrrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA 2518
Cdd:cd17652    81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAVYLNPDHMPDF 2598
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPDL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2599 KRLIAAGSASSLELLQQWKDKVKYFNAYGPTEDSICTTIWTPSTEDisqlKSVPIGGPIVNHRIYIVDAHYQPVPVGVAG 2678
Cdd:cd17652   207 RTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGG----GVPPIGRPVPGTRVYVLDARLRPVPPGVPG 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2679 ELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKV 2757
Cdd:cd17652   283 ELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEH 362
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2758 ASVQEAIVIAHDDASGQKQLCAYFVADR--TMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALP 2829
Cdd:cd17652   363 PGVAEAVVVVRDDRPGDKRLVAYVVPAPgaAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
8033-8446 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 580.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8033 YYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY 8112
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 ------SKADREEAVE--IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGE--- 8181
Cdd:cd19531    81 vdlsglPEAEREAEAQrlAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlag 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8182 ---ELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNEL 8258
Cdd:cd19531   161 rpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8259 AARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGA 8338
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8339 FEHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDqTVAAQFDLTLSVAEDDGAIRGSFQY 8418
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVD-SGTAKFDLTLSLTETDGGLRGSLEY 399
                         410       420
                  ....*....|....*....|....*...
gi 386647928 8419 AAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19531   400 NTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
3855-4338 0e+00

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 576.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3855 TIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPI 3934
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3935 DPEYPEDRIRYMLEDSGAQALLTQrhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMV 4014
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4015 EHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPT 4094
Cdd:cd17644   127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4095 Y----AAYLNPDRMP---SLKKLITGGSAASVEFVQQW----KDKVLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPIG 4163
Cdd:cd17644   207 YwhllVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWqknvGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVPIG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4164 RPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFE--PGERMYRTGDLVRWLPDGNLEYLG 4241
Cdd:cd17644   287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4242 RIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFV 4319
Cdd:cd17644   367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHyeESPSTVELRQFLKAKLPDYMIPSAFV 446
                         490
                  ....*....|....*....
gi 386647928 4320 QLAQMPLTPNGKIDRKALP 4338
Cdd:cd17644   447 VLEELPLTPNGKIDRRALP 465
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
2351-2829 0e+00

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 572.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2351 FEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYP 2430
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2431 EDRISYMLEDSSAQVLLAQRRLQERVSF-AGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHG 2509
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVeLVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2510 LCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAVY 2589
Cdd:cd17651   161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2590 L------NPDHMPDFKRLIAAGSASSL-ELLQQWKDKVKY---FNAYGPTEDSICTTIWTPSTEDiSQLKSVPIGGPIVN 2659
Cdd:cd17651   241 LaehgrpLGVRLAALRYLLTGGEQLVLtEDLREFCAGLPGlrlHNHYGPTETHVVTALSLPGDPA-AWPAPPPIGRPIDN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2660 HRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVK 2739
Cdd:cd17651   320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2740 IRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRT--MTVGELRGELSGELPGYMIPAHFVQLERMPL 2817
Cdd:cd17651   400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEapVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
                         490
                  ....*....|..
gi 386647928 2818 TPNGKIDRKALP 2829
Cdd:cd17651   480 TPNGKLDRRALP 491
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
3860-4338 0e+00

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 571.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3860 FEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYP 3939
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3940 EDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVA-VDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 4018
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTlLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4019 LCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAY 4098
Cdd:cd17651   161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4099 L------NPDRMPSLKKLITGGSAASV-EFVQQWKDKVLY---FNAYGPTEASIVTSIWDEAsDSLGDRKSVPIGRPLAN 4168
Cdd:cd17651   241 LaehgrpLGVRLAALRYLLTGGEQLVLtEDLREFCAGLPGlrlHNHYGPTETHVVTALSLPG-DPAAWPAPPPIGRPIDN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4169 HRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVK 4248
Cdd:cd17651   320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4249 IRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRE--LTAAELRATMSQELPNYMIPSYFVQLAQMPL 4326
Cdd:cd17651   400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEapVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
                         490
                  ....*....|..
gi 386647928 4327 TPNGKIDRKALP 4338
Cdd:cd17651   480 TPNGKLDRRALP 491
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2928-3358 0e+00

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 569.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2928 DVSLTPIQHWFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHKSENGYTAWNRAIGEgELYGLE 3007
Cdd:cd19534     1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVE-ELFRLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3008 VVDLKGiEESAQAVEAKANEIQSSIDLEAGPFVKAGLFQ-CADGDHLLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEE 3086
Cdd:cd19534    80 VVDLSS-LAQAAAIEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3087 LRFPAKTdAYRTWSEQLAAYAQSPVIERELAYWKRVAQTEVQPLPKDeqvDVSLQQDSESISIEWTREETEQLLKGVHRA 3166
Cdd:cd19534   159 IPLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKD---PEQTYGDARTVSFTLDEEETEALLQEANAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3167 YNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGRESIMTDIDITRTVGWFTSKYPVVLELEQGKDISYLLKKTKEDLRG 3246
Cdd:cd19534   235 YRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLRR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3247 IPNKGIGYGICRYLSA-AKNDIAWGAEPEVSFNYLGQFDQDLQNSDIGVSA-HTGGKQSSDRQKRIFVLDINGMIADGTL 3324
Cdd:cd19534   315 IPNKGIGYGILRYLTPeGTKRLAFHPQPEISFNYLGQFDQGERDDALFVSAvGGGGSDIGPDTPRFALLDINAVVEGGQL 394
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 3325 SLELSYNGKEYRRETMERLAASLQESLRVIIAHC 3358
Cdd:cd19534   395 VITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
7460-7929 0e+00

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 567.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 7619
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7620 ETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAIYLSPDR---- 7695
Cdd:cd17656   162 EKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSERefin 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7696 -LPS-LKKLITGGSAASV--EFVQQWKDK-VRYFNAYGPTEASIVTSvWAASPDGLDLRSVPIGRPIANHQIFIVDSQNH 7770
Cdd:cd17656   242 rFPTcVKHIITAGEQLVItnEFKEMLHEHnVHLHNHYGPSETHVVTT-YTINPEAEIPELPPIGKPISNTWIYILDQEQQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7771 MLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEI 7850
Cdd:cd17656   321 LQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEI 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 7851 EEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALP 7929
Cdd:cd17656   401 EAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
6520-6950 0e+00

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 565.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6520 EIGLTPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGYAAWNRAIGEgELYSLE 6599
Cdd:cd19534     1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVE-ELFRLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6600 VADFRDVKSaEQAVEAKANEIQSSIDLEVGPLFKAGLFQ-CADGDHLLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEE 6678
Cdd:cd19534    80 VVDLSSLAQ-AAAIEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6679 VRLPAKTdSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAPLPKDkqsDRSLQQDSESITIQWSRKETEQLLKKVHRA 6758
Cdd:cd19534   159 IPLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKD---PEQTYGDARTVSFTLDEEETEALLQEANAA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6759 YNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDITRTVGWFTSKYPVLLQMEPGRSLSTRIKKVKEDLRR 6838
Cdd:cd19534   235 YRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLRR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6839 IPNKGIGYGLCRYLSAQPDGTVWGA-EPEISFNYLGQFDQDLSNNDIGLSPYS-SGLEMSDRQARSFILDINGMITDGSL 6916
Cdd:cd19534   315 IPNKGIGYGILRYLTPEGTKRLAFHpQPEISFNYLGQFDQGERDDALFVSAVGgGGSDIGPDTPRFALLDINAVVEGGQL 394
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 6917 ALELSYSRKEYHRETVEELAGMLQESLQEIIAHC 6950
Cdd:cd19534   395 VITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
7460-7929 1.48e-180

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 563.03  E-value: 1.48e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQrhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 7619
Cdd:cd17652    81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7620 ETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAIYLSPDRLPSL 7699
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPDL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7700 KKLITGGSAASVEFVQQWKDKVRYFNAYGPTEASIVTSVWAASPDGldlRSVPIGRPIANHQIFIVDSQNHMLPVGVAGE 7779
Cdd:cd17652   207 RTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGG---GVPPIGRPVPGTRVYVLDARLRPVPPGVPGE 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7780 LCISGAGLARGYLNRPELTAEKFVDNPFLA-GERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIA 7858
Cdd:cd17652   284 LYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHP 363
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 7859 SVQETIVIARGDANGQQQLCAYFVADRE--LTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALP 7929
Cdd:cd17652   364 GVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
4444-5472 2.03e-180

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 595.87  E-value: 2.03e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4444 PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAV-ETV 4522
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLpEII 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4523 QASEQ-EAKAIVRDFIRPfDLAKP-------PLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSG----- 4589
Cdd:PRK10252   89 DLRTQpDPHAAAQALMQA-DLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrge 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4590 ----EELPGLRIQYKDYAVWQQSEAQKeqlkRQEAYWLEAFRGeLPvlEMPTDYARPAVQSYAGDTLdFRMNSEISEGLK 4665
Cdd:PRK10252  168 ptpaSPFTPFADVVEEYQRYRASEAWQ----RDAAFWAEQRRQ-LP--PPASLSPAPLPGRSASADI-LRLKLEFTDGAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4666 R--IAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKET 4743
Cdd:PRK10252  240 RqlAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4744 TLGAFEHQTYPFEELVdklqmaRDLSR----NPLFDTMFSLQNTEnKEMHLPGL-----HLTPYPTEygmskfDLSLDMM 4814
Cdd:PRK10252  320 LKKMRRHQRYDAEQIV------RDSGRaagdEPLFGPVLNIKVFD-YQLDFPGVqaqthTLATGPVN------DLELALF 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4815 EDSEG-LECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIASLGILTADEKAQIVHVFNPAAPDAPENEAfhALF 4893
Cdd:PRK10252  387 PDEHGgLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLS--ALV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4894 EKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 4973
Cdd:PRK10252  465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4974 DRIQFMLEDSAASVLLTQTHLQERAQqwGQTLQAALCLDdeAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEH 5053
Cdd:PRK10252  545 DRLKMMLEDARPSLLITTADQLPRFA--DVPDLTSLCYN--APLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5054 RSLVNtaagyRREYRLDQFPV----RLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFES 5129
Cdd:PRK10252  621 TAIVN-----RLLWMQNHYPLtaddVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHF 695
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5130 TPALIIPFMDYVAEHGLDMS--SMVLLITSSDSCSVTDYRVLQERFGSQFRiiNAYGVTEAAIDSSLYD---EPLAKLPE 5204
Cdd:PRK10252  696 VPSMLAAFVASLTPEGARQScaSLRQVFCSGEALPADLCREWQQLTGAPLH--NLYGPTEAAVDVSWYPafgEELAAVRG 773
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5205 AgNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGN 5284
Cdd:PRK10252  774 S-SVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGA 852
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5285 VDFIGRIDNQAKIRGYRIETGEIETQLLK----AEGVREAVVVVREDAKG--QKVLCAHFTAESELKL--SELRSSLSQE 5356
Cdd:PRK10252  853 VEYLGRSDDQLKIRGQRIELGEIDRAMQAlpdvEQAVTHACVINQAAATGgdARQLVGYLVSQSGLPLdtSALQAQLRER 932
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5357 LPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASMQTGMEyvAPRTPQEAKLVSIWQEVLGLEKVGVKDNFFELGGHSL 5436
Cdd:PRK10252  933 LPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSL 1010
                        1050      1060      1070
                  ....*....|....*....|....*....|....*.
gi 386647928 5437 RATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIA 5472
Cdd:PRK10252 1011 LAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLD 1046
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
2346-2829 1.46e-179

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 561.67  E-value: 1.46e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI 2425
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2426 DPEYPEDRISYMLEDSSAQVLLAQrrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMV 2505
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2506 EHHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPT 2585
Cdd:cd17644   127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2586 Y------AVYLNPDHMPDFKRLIAAGSASSL-ELLQQW----KDKVKYFNAYGPTEDSICTTIWTPSTEDISQLKSVPIG 2654
Cdd:cd17644   207 YwhllvlELLLSTIDLPSSLRLVIVGGEAVQpELVRQWqknvGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVPIG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2655 GPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFE--PGERMYRTGDLAKWLPDGTIEYLG 2732
Cdd:cd17644   287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2733 RIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVA--DRTMTVGELRGELSGELPGYMIPAHFV 2810
Cdd:cd17644   367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPhyEESPSTVELRQFLKAKLPDYMIPSAFV 446
                         490
                  ....*....|....*....
gi 386647928 2811 QLERMPLTPNGKIDRKALP 2829
Cdd:cd17644   447 VLEELPLTPNGKIDRRALP 465
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
3857-4337 4.56e-179

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 561.13  E-value: 4.56e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3857 HGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDP 3936
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3937 EYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEH 4016
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4017 HGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPP--- 4093
Cdd:cd17646   161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPsml 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4094 -TYAAYLNPDRMPSLKKLITGGSAASVEFVQQWK---DKVLYfNAYGPTEASIVTSIWdeASDSLGDRKSVPIGRPLANH 4169
Cdd:cd17646   241 rVFLAEPAAGSCASLRRVFCSGEALPPELAARFLalpGAELH-NLYGPTEAAIDVTHW--PVRGPAETPSVPIGRPVPNT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4170 RIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKI 4249
Cdd:cd17646   318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4250 RGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQR---ELTAAELRATMSQELPNYMIPSYFVQLAQMPL 4326
Cdd:cd17646   398 RGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaaGPDTAALRAHLAERLPEYMVPAAFVVLDALPL 477
                         490
                  ....*....|.
gi 386647928 4327 TPNGKIDRKAL 4337
Cdd:cd17646   478 TANGKLDRAAL 488
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
7452-7929 6.46e-179

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 560.81  E-value: 6.46e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7452 FEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYP 7531
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7532 EDRIRYMLEDSGAQVLLTQRHLQECVSFD-GKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 7610
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVElVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7611 LCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAIY 7690
Cdd:cd17651   161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7691 LSPD------RLPSLKKLITGGSAASV-EFVQQWKDKVRY---FNAYGPTEASIVTSVW-AASPDGLDLRsVPIGRPIAN 7759
Cdd:cd17651   241 LAEHgrplgvRLAALRYLLTGGEQLVLtEDLREFCAGLPGlrlHNHYGPTETHVVTALSlPGDPAAWPAP-PPIGRPIDN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7760 HQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVK 7839
Cdd:cd17651   320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7840 IRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRE--LTVSELRGTLSQELPGYMIPSYFVQLEQMPL 7917
Cdd:cd17651   400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEapVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
                         490
                  ....*....|..
gi 386647928 7918 TPNGKIDRNALP 7929
Cdd:cd17651   480 TPNGKLDRRALP 491
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
5492-6505 8.87e-179

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 591.25  E-value: 8.87e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5492 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYR 5571
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEII 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5572 --TSEAEAGEVVRGFVRTfDLAKP-------PLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNG----- 5637
Cdd:PRK10252   89 dlRTQPDPHAAAQALMQA-DLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrge 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5638 ----ESLAPLRIQYKDYATWQQSEAQQeqmkRQEAYWLDMFRGELPVLELPtdyPRPAVRKFEG-SLLQRQLEPKLGEGL 5712
Cdd:PRK10252  168 ptpaSPFTPFADVVEEYQRYRASEAWQ----RDAAFWAEQRRQLPPPASLS---PAPLPGRSASaDILRLKLEFTDGAFR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5713 QRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETM 5792
Cdd:PRK10252  241 QLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5793 LGAYEHQSYPFEELVekaqpaRDLSR----NPLFDTLFALQNKETgELQLDGLRLTpypaEHTVAKF---DLSVDV-TEG 5864
Cdd:PRK10252  321 KKMRRHQRYDAEQIV------RDSGRaagdEPLFGPVLNIKVFDY-QLDFPGVQAQ----THTLATGpvnDLELALfPDE 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5865 SEGLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEKEHIQRVfNATEAKYPsDKTIHQLFEEQ 5944
Cdd:PRK10252  390 HGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQV-NATAVEIP-ETTLSALVAQQ 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK10252  468 AAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVV-RL 6103
Cdd:PRK10252  548 KMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVnRL 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6104 VKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTM-----WLTAPLYNQ 6178
Cdd:PRK10252  628 LWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThfvpsMLAAFVASL 707
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6179 LSQQDSGMFAGLKTLIVGGDVLSVPHINRVLReHAGLSIVNGYGPTENTTFSTTHTIVGEQKEA-----VPIGKPINNST 6253
Cdd:PRK10252  708 TPEGARQSCASLRQVFCSGEALPADLCREWQQ-LTGAPLHNLYGPTEAAVDVSWYPAFGEELAAvrgssVPIGYPVWNTG 786
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6254 AYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIR 6333
Cdd:PRK10252  787 LRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIR 866
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6334 GYRIELGEIEEQLLKVASVKEATVIVR------EDESGQKQLCAYFVAERELTI--GELRAALSQELPNYMIPSHFVPLE 6405
Cdd:PRK10252  867 GQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGLPLdtSALQAQLRERLPPHMVPVVLLQLD 946
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6406 RMPLTPNGKIDRRALPAPQGNAPVGAEyvAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLHQA-G 6484
Cdd:PRK10252  947 QLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQfA 1024
                        1050      1060
                  ....*....|....*....|.
gi 386647928 6485 YKLEIRDLFKYPTLAQLSQHI 6505
Cdd:PRK10252 1025 RQVTPGQVMVASTVAKLATLL 1045
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
7447-7929 3.87e-178

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 557.43  E-value: 3.87e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7447 TIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPI 7526
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7527 DPEYPEDRIRYMLEDSGAQVLLTQrhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMV 7606
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7607 EHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPT 7686
Cdd:cd17644   127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7687 Y----AIYLSPDRLP---SLKKLITGGSAASVEFVQQW----KDKVRYFNAYGPTEASIVTSVW-AASPDGLDLRSVPIG 7754
Cdd:cd17644   207 YwhllVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWqknvGNFIQLINVYGPTEATIAATVCrLTQLTERNITSVPIG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7755 RPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLA--GERMYRTGDLARWLPDGNIEYLG 7832
Cdd:cd17644   287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEYLG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7833 RIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA--DRELTVSELRGTLSQELPGYMIPSYFV 7910
Cdd:cd17644   367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPhyEESPSTVELRQFLKAKLPDYMIPSAFV 446
                         490
                  ....*....|....*....
gi 386647928 7911 QLEQMPLTPNGKIDRNALP 7929
Cdd:cd17644   447 VLEELPLTPNGKIDRRALP 465
PRK12467 PRK12467
peptide synthase; Provisional
191-1021 4.01e-178

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 623.34  E-value: 4.01e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  191 DEVRLHLTYNGNLYTESFIAQAVDHLNRLFSVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQA 270
Cdd:PRK12467 3026 DTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQV 3105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  271 ERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIR 350
Cdd:PRK12467 3106 ARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLA 3185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  351 YMLEDSGTQVLLSQGHLQER--VSFSGTWIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTH---RNI 425
Cdd:PRK12467 3186 YMIEDSGVKLLLTQAHLLEQlpAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHgalANH 3265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  426 IRVVKntNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKEtVLDVAKLAGLIEKQQISVMFITTAFFNVLV 505
Cdd:PRK12467 3266 LCWIA--EAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDND-LWDPEELWQAIHAHRISIACFPPAYLQQFA 3342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  506 -DMNPDCLRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDV-HEVEEGAVSIPIGGPISNTAIYI 583
Cdd:PRK12467 3343 eDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCgGDAVCEAPYAPIGRPVAGRSIYV 3422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  584 VNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFA-PGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGF 662
Cdd:PRK12467 3423 LDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 3502
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  663 RIELGEIEAHLLKLEAIEKATVVVRESANGeKQLCAYYVADRSLPA--NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNG 740
Cdd:PRK12467 3503 RIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  741 KVDRRALPAPEESMETgvEFVEPRTELEAGIVNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDV 820
Cdd:PRK12467 3582 KVDRKALPDPDAKGSR--EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDL 3659
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  821 FRYPTVEKLAeaisgmgeqvyssipaaearEYYPLSSAQKRLyilhqlegaeqsynlpgvtllegALDRNRLEEAFRALI 900
Cdd:PRK12467 3660 MSAPTIAELA--------------------GYSPLGDVPVNL-----------------------LLDLNRLETGFPALF 3696
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  901 ARHETLRTGIEmvgGEPMQRIYPEvefavehiraneeeadaavkqfirafdlakppllrvglielapERHLLMFDMHHIV 980
Cdd:PRK12467 3697 CRHEGLGTVFD---YEPLAVILEG-------------------------------------------DRHVLGLTCRHLL 3730
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|.
gi 386647928  981 SDGismdvlveefarlYGGEDLPALRIQYKDYAVWQQSEAQ 1021
Cdd:PRK12467 3731 DDG-------------WQDTSLQAMAVQYADYILWQQAKGP 3758
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
274-748 1.68e-177

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 556.32  E-value: 1.68e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQGHLQERVSFSGTWIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNT- 432
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  433 NYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMN---- 508
Cdd:cd17656   162 EKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSERefin 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  509 --PDCLRHaraILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVfATSYDVHEVEEGAVSIPIGGPISNTAIYIVNA 586
Cdd:cd17656   242 rfPTCVKH---IITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEIPELPPIGKPISNTWIYILDQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  587 QNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIEL 666
Cdd:cd17656   318 EQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIEL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  667 GEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRA 746
Cdd:cd17656   398 GEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKA 477

                  ..
gi 386647928  747 LP 748
Cdd:cd17656   478 LP 479
PRK12316 PRK12316
peptide synthase; Provisional
11-838 4.57e-176

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 617.35  E-value: 4.57e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   11 AFWnKIFEGEENPPTALPYSKAQKQ--APALVRRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSSSSIL 88
Cdd:PRK12316 4283 AFW-REQLAALDEPTRLAQAIARADlrSANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVA 4361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   89 VGMPVVTKPNEnrRP---------VNQLVILrEEVRDDSTFKALLGEAKNSVTSSINHQNVPFrlmterLELQYADGV-- 157
Cdd:PRK12316 4362 FGATVAGRPAE--LPgiegqiglfINTLPVI-ATPRAQQSVVEWLQQVQRQNLALREHEHTPL------YEIQRWAGQgg 4432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  158 -PVVNTLVALKQLHITDY-RQSAVSDVLFEFELDKDE--------------VRLHLTYNGNLYTESFIAQAVDHLNRLFS 221
Cdd:PRK12316 4433 eALFDSLLVFENYPVSEAlQQGAPGGLRFGEVTNHEQtnypltlavglgetLSLQFSYDRGHFDAATIERLARHLTNLLE 4512
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  222 VVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLART 301
Cdd:PRK12316 4513 AMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHA 4592
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  302 LRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSG--TWIR 379
Cdd:PRK12316 4593 LIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDglASLA 4672
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  380 LDDEEAYHEDGSNLESVN-GPEHLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDKLLQLSSYSFDGSTFD 457
Cdd:PRK12316 4673 LDRDEDWEGFPAHDPAVRlHPDNLAYVIYTSGSTGRPKGVAVSHGSLVnHLHATGERYELTPDDRVLQFMSFSFDGSHEG 4752
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  458 IFGALLNGAKlVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVL-----VDMNPDCLRHaraILFGGERVSVSHVRK 532
Cdd:PRK12316 4753 LYHPLINGAS-VVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLaehaeRDGEPPSLRV---YCFGGEAVAQASYDL 4828
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  533 ALGHLGPGKIKHVYGPTESTVFATSYDVHE-VEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYL 611
Cdd:PRK12316 4829 AWRALKPVYLFNGYGPTETTVTVLLWKARDgDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYL 4908
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  612 NRPDLTAEKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESA 690
Cdd:PRK12316 4909 ERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA 4988
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  691 NGeKQLCAYYVADRS--LPANEVRSTLSQEL--------PAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGVeF 760
Cdd:PRK12316 4989 VG-KQLVGYVVPQDPalADADEAQAELRDELkaalrerlPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQA-Y 5066
                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  761 VEPRTELEAGIVNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISGMGE 838
Cdd:PRK12316 5067 VAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGS 5144
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
5941-6421 4.24e-174

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 546.94  E-value: 4.24e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5941 FEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYP 6020
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6021 EDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDD-GAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRN 6099
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQpGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6100 VVRLVKN-TNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQ 6178
Cdd:cd17651   161 LANLVAWqARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6179 LSQQ---DSGMFAGLKTLIVGGDVLSV-PHINRVLREHAGLSIVNGYGPTEnTTFSTTHTIVGEQK---EAVPIGKPINN 6251
Cdd:cd17651   241 LAEHgrpLGVRLAALRYLLTGGEQLVLtEDLREFCAGLPGLRLHNHYGPTE-THVVTALSLPGDPAawpAPPPIGRPIDN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6252 STAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVK 6331
Cdd:cd17651   320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6332 IRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERE--LTIGELRAALSQELPNYMIPSHFVPLERMPL 6409
Cdd:cd17651   400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEapVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
                         490
                  ....*....|..
gi 386647928 6410 TPNGKIDRRALP 6421
Cdd:cd17651   480 TPNGKLDRRALP 491
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
7449-7928 1.32e-173

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 545.33  E-value: 1.32e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7449 HGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDP 7528
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7529 EYPEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEH 7608
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7609 HGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAA-ILPPTY 7687
Cdd:cd17646   161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTChFVPSML 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7688 AIYLS---PDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEASIVTSVWAASPDGlDLRSVPIGRPIANHQI 7762
Cdd:cd17646   241 RVFLAepaAGSCASLRRVFCSGEALPPELAARFLALpgAELHNLYGPTEAAIDVTHWPVRGPA-ETPSVPIGRPVPNTRL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7763 FIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRG 7842
Cdd:cd17646   320 YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7843 YRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADR---ELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTP 7919
Cdd:cd17646   400 FRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaaGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTA 479

                  ....*....
gi 386647928 7920 NGKIDRNAL 7928
Cdd:cd17646   480 NGKLDRAAL 488
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
2359-2829 6.67e-173

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 543.22  E-value: 6.67e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA 2518
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAVYLNPDH--MP 2596
Cdd:cd17656   162 EKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSERefIN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2597 DF----KRLIAAGSasSLELLQQWKD-----KVKYFNAYGPTEDSICTTiWTPSTEDISQLKSvPIGGPIVNHRIYIVDA 2667
Cdd:cd17656   242 RFptcvKHIITAGE--QLVITNEFKEmlhehNVHLHNHYGPSETHVVTT-YTINPEAEIPELP-PIGKPISNTWIYILDQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2668 HYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIEL 2747
Cdd:cd17656   318 EQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIEL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2748 GEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKA 2827
Cdd:cd17656   398 GEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKA 477

                  ..
gi 386647928 2828 LP 2829
Cdd:cd17656   478 LP 479
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
2348-2828 8.03e-173

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 543.02  E-value: 8.03e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2348 HQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDP 2427
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2428 EYPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEH 2507
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2508 HGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTY- 2586
Cdd:cd17646   161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMl 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2587 AVYLN---PDHMPDFKRLIAAGSASSLELLQQWKDK--VKYFNAYGPTEDSICTTIWTPSTEDISqlKSVPIGGPIVNHR 2661
Cdd:cd17646   241 RVFLAepaAGSCASLRRVFCSGEALPPELAARFLALpgAELHNLYGPTEAAIDVTHWPVRGPAET--PSVPIGRPVPNTR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2662 IYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIR 2741
Cdd:cd17646   319 LYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2742 GYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVG---ELRGELSGELPGYMIPAHFVQLERMPLT 2818
Cdd:cd17646   399 GFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPdtaALRAHLAERLPEYMVPAAFVVLDALPLT 478
                         490
                  ....*....|
gi 386647928 2819 PNGKIDRKAL 2828
Cdd:cd17646   479 ANGKLDRAAL 488
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
3868-4338 8.33e-173

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 542.84  E-value: 8.33e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSL-KLMF 4026
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLlHFER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4027 ANTLQMTEqDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAYL------N 4100
Cdd:cd17656   162 EKTNINFS-DKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIfserefI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4101 PDRMPSLKKLITGGSAASV--EFVQQWKDK-VLYFNAYGPTEASIVTSIWDEASDSLGDRKsvPIGRPLANHRIYVVDSH 4177
Cdd:cd17656   241 NRFPTCVKHIITAGEQLVItnEFKEMLHEHnVHLHNHYGPSETHVVTTYTINPEAEIPELP--PIGKPISNTWIYILDQE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4178 NRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELG 4257
Cdd:cd17656   319 QQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4258 EVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd17656   399 EIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478

                  .
gi 386647928 4338 P 4338
Cdd:cd17656   479 P 479
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
3868-4338 1.48e-170

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 535.03  E-value: 1.48e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQRhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 4027
Cdd:cd17649    81 EDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4028 NTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPtsttilDYPLFES------YMNENGITATILPPTY------ 4095
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLR------PDELWASadelaeMVRELGVTVLDLPPAYlqqlae 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4096 -AAYLNPDRMPSLKKLITGGSAASVEFVQQW-KDKVLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPIGRPLANHRIYV 4173
Cdd:cd17649   202 eADRTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4174 VDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPF-EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGY 4252
Cdd:cd17649   282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4253 RIELGEVETQLAKIDAVQEAIVLAReDANGQQQLVAYFVAQ----RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTP 4328
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRaaaaQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTP 440
                         490
                  ....*....|
gi 386647928 4329 NGKIDRKALP 4338
Cdd:cd17649   441 NGKLDRKALP 450
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3881-4274 5.46e-170

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 531.46  E-value: 5.46e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3881 TYGELNERANRLARTLRDA-GVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQR 3959
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3960 HLRERVSFAGTFVA--VDDEQAYHADGSNLEPV---VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTE 4034
Cdd:TIGR01733   81 ALASRLAGLVLPVIllDPLELAALDDAPAPPPPdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4035 QDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYM-NENGITATILPPTYAAYL---NPDRMPSLKKL 4110
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLaaaLPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4111 ITGGSAASVEFVQQWKDK---VLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAG 4187
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4188 ELCISGVGLARGYLNRPELTAEKFVDNPF--EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAK 4265
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 386647928  4266 IDAVQEAIV 4274
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1301-1795 5.78e-170

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 534.86  E-value: 5.78e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1301 ALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 1380
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1381 YPSDRIQFMLEDSAASVLLTQTHLQERAQQwgqtlQAVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVM 1460
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGG-----LEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1461 IEHRSLVNTAAGyrREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFEST 1540
Cdd:cd12117   156 VTHRGVVRLVKN--TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1541 PALiipFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYdePLAKL-PEAGNVP 1619
Cdd:cd12117   234 AAL---FNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGL-RLVNGYGPTENTTFTTSH--VVTELdEVAGSIP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1620 IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIG 1699
Cdd:cd12117   308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1700 RIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQL 1779
Cdd:cd12117   388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVL 467
                         490
                  ....*....|....*.
gi 386647928 1780 EQLPLTANGKIDRKAL 1795
Cdd:cd12117   468 DELPLTANGKVDRRAL 483
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
5949-6421 2.45e-169

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 532.82  E-value: 2.45e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQGHLLDRASFADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNT- 6107
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6108 NYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLS---QQDS 6184
Cdd:cd17656   162 EKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFserEFIN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6185 GMFAGLKTLIVGGDVLSVPH-INRVLREHaGLSIVNGYGPTEnTTFSTTHTI--VGEQKEAVPIGKPINNSTAYIVDSKL 6261
Cdd:cd17656   242 RFPTCVKHIITAGEQLVITNeFKEMLHEH-NVHLHNHYGPSE-THVVTTYTInpEAEIPELPPIGKPISNTWIYILDQEQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6262 SLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGE 6341
Cdd:cd17656   320 QLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALP 6421
Cdd:cd17656   400 IEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
4891-5385 5.41e-169

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 531.78  E-value: 5.41e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4891 ALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 4970
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4971 YPSDRIQFMLEDSAASVLLTQTHLQERAQQwgqtlQAALCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVM 5050
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGG-----LEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5051 IEHRSLVNTAAGyrREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFEST 5130
Cdd:cd12117   156 VTHRGVVRLVKN--TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5131 PALiipFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYdePLAKL-PEAGNVP 5209
Cdd:cd12117   234 AAL---FNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGL-RLVNGYGPTENTTFTTSH--VVTELdEVAGSIP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5210 IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIG 5289
Cdd:cd12117   308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5290 RIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQL 5369
Cdd:cd12117   388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVL 467
                         490
                  ....*....|....*.
gi 386647928 5370 EQLPLTANGKIDRKAL 5385
Cdd:cd12117   468 DELPLTANGKVDRRAL 483
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
3857-4338 6.57e-168

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 527.12  E-value: 6.57e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3857 HGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDP 3936
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3937 EYPEDRIRYMLEDSGAQALLTQrhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEH 4016
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTN----------------------------------PDDLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4017 HGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYA 4096
Cdd:cd17645   127 HNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4097 AYLNPDRMPSLKKLITGGSAASVEFVQQWKdkvlYFNAYGPTEASIVTSIWdEASDSLGdrkSVPIGRPLANHRIYVVDS 4176
Cdd:cd17645   207 EQFMQLDNQSLRVLLTGGDKLKKIERKGYK----LVNNYGPTENTVVATSF-EIDKPYA---NIPIGKPIDNTRVYILDE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4177 HNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIEL 4256
Cdd:cd17645   279 ALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEP 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4257 GEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKA 4336
Cdd:cd17645   359 GEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKA 438

                  ..
gi 386647928 4337 LP 4338
Cdd:cd17645   439 LP 440
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
3868-4337 8.78e-168

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 527.04  E-value: 8.78e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQrhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 4027
Cdd:cd17650    81 EDSGAKLLLTQ----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4028 NTLQMTEQD-RVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYA------AYLN 4100
Cdd:cd17650   127 REYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIrpvmayVYRN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4101 PDRMPSLKKLITGGSAAS----VEFVQQWKDKVLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPIGRPLANHRIYVVDS 4176
Cdd:cd17650   207 GLDLSAMRLLIVGSDGCKaqdfKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4177 HNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIEL 4256
Cdd:cd17650   287 RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIEL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4257 GEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKA 4336
Cdd:cd17650   367 GEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRA 446

                  .
gi 386647928 4337 L 4337
Cdd:cd17650   447 L 447
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
2348-2829 3.23e-167

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 525.20  E-value: 3.23e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2348 HQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDP 2427
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2428 EYPEDRISYMLEDSSAQVLLAQrrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEH 2507
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTN----------------------------------PDDLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2508 HGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYA 2587
Cdd:cd17645   127 HNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2588 VYLNPDHMPDFKRLIAAGsasslELLQQWKDK-VKYFNAYGPTEDSICTTiwtpSTEDISQLKSVPIGGPIVNHRIYIVD 2666
Cdd:cd17645   207 EQFMQLDNQSLRVLLTGG-----DKLKKIERKgYKLVNNYGPTENTVVAT----SFEIDKPYANIPIGKPIDNTRVYILD 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2667 AHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIE 2746
Cdd:cd17645   278 EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIE 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2747 LGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRK 2826
Cdd:cd17645   358 PGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437

                  ...
gi 386647928 2827 ALP 2829
Cdd:cd17645   438 ALP 440
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
7460-7929 4.81e-167

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 525.01  E-value: 4.81e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQRhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 7619
Cdd:cd17649    81 EDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7620 ETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTY-------AIYLS 7692
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYlqqlaeeADRTG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7693 PDRLPSLKKLITGGSAASVEFVQQW-KDKVRYFNAYGPTEASIVTSVWAASPDGLDL-RSVPIGRPIANHQIFIVDSQNH 7770
Cdd:cd17649   208 DGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAgASMPIGRPLGGRSAYILDADLN 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7771 MLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLA-GERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGE 7849
Cdd:cd17649   288 PVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGE 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7850 IEEQLLKIASVQETIVIARgDANGQQQLCAYFV----ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd17649   368 IEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVlraaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDR 446

                  ....
gi 386647928 7926 NALP 7929
Cdd:cd17649   447 KALP 450
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
261-748 8.27e-167

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 525.08  E-value: 8.27e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPI 340
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  341 DPEYPEERIRYMLEDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLT 420
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  421 THRNIIRVVKNT-NYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTA 499
Cdd:cd17644   127 EHQSLVNLSHGLiKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  500 FFNVLVD----MNPDCLRHARAILFGGERVSVSHVRKALGHLGPgKIK--HVYGPTESTVFATSYDVHEVEEGAV-SIPI 572
Cdd:cd17644   207 YWHLLVLelllSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGN-FIQliNVYGPTEATIAATVCRLTQLTERNItSVPI 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  573 GGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFA--PGERMYRTGDLARWLPDGTIEYV 650
Cdd:cd17644   286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  651 GRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVA--DRSLPANEVRSTLSQELPAYMLPSYF 728
Cdd:cd17644   366 GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPhyEESPSTVELRQFLKAKLPDYMIPSAF 445
                         490       500
                  ....*....|....*....|
gi 386647928  729 VQLEQMPLTTNGKVDRRALP 748
Cdd:cd17644   446 VVLEELPLTPNGKIDRRALP 465
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
2359-2829 1.16e-166

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 523.85  E-value: 1.16e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQRrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA 2518
Cdd:cd17649    81 EDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTY-------AVYLN 2591
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYlqqlaeeADRTG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2592 PDHMPDFKRLIAAGSASSLELLQQW-KDKVKYFNAYGPTEDSICTTIWTPSTEDISQLKSVPIGGPIVNHRIYIVDAHYQ 2670
Cdd:cd17649   208 DGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLN 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2671 PVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGE 2749
Cdd:cd17649   288 PVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGE 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2750 IEEQLLKVASVQEAIVIAHDDAsGQKQLCAYFVADRTMTVGE----LRGELSGELPGYMIPAHFVQLERMPLTPNGKIDR 2825
Cdd:cd17649   368 IEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAAAQPElraqLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDR 446

                  ....
gi 386647928 2826 KALP 2829
Cdd:cd17649   447 KALP 450
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
263-748 1.60e-166

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 522.89  E-value: 1.60e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  263 HRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDP 342
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  343 EYPEERIRYMLEDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTH 422
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTN----------------------------------PDDLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  423 RNIIRVVK-NTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFF 501
Cdd:cd17645   127 HNLVNLCEwHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  502 NVLVDMNPDCLRharAILFGGERVSVShVRKalghlgPGKIKHVYGPTESTVFATSYDVHEVEEgavSIPIGGPISNTAI 581
Cdd:cd17645   207 EQFMQLDNQSLR---VLLTGGDKLKKI-ERK------GYKLVNNYGPTENTVVATSFEIDKPYA---NIPIGKPIDNTRV 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  582 YIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRG 661
Cdd:cd17645   274 YILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRG 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  662 FRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGK 741
Cdd:cd17645   354 YRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGK 433

                  ....*..
gi 386647928  742 VDRRALP 748
Cdd:cd17645   434 VDRKALP 440
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
266-748 1.78e-166

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 524.99  E-value: 1.78e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  266 FEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYP 345
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  346 EERIRYMLEDSGTQVLLSQGHLQERVSF-SGTWIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRN 424
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVeLVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  425 IIRVVKN-TNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNV 503
Cdd:cd17651   161 LANLVAWqARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  504 LV-DMNPDCLRHA--RAILFGGERVSVSH-VRKALGHLGPGKIKHVYGPTESTVfATSY--DVHEVEEGAVSiPIGGPIS 577
Cdd:cd17651   241 LAeHGRPLGVRLAalRYLLTGGEQLVLTEdLREFCAGLPGLRLHNHYGPTETHV-VTALslPGDPAAWPAPP-PIGRPID 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  578 NTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQV 657
Cdd:cd17651   319 NTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  658 KIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADR--SLPANEVRSTLSQELPAYMLPSYFVQLEQMP 735
Cdd:cd17651   399 KIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPeaPVDAAELRAALATHLPEYMVPSAFVLLDALP 478
                         490
                  ....*....|...
gi 386647928  736 LTTNGKVDRRALP 748
Cdd:cd17651   479 LTPNGKLDRRALP 491
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
3868-4337 3.23e-166

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 522.64  E-value: 3.23e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQrhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLklmFA 4027
Cdd:cd17643    81 ADSGPSLLLTD----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLAL---FA 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4028 NT---LQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITatILPPTYAAYL----- 4099
Cdd:cd17643   124 ATqrwFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVT--VLNQTPSAFYqlvea 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4100 ---NPDRMPSLKKLITGGSAASVEFVQQW-----KDKVLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPIGRPLANHRI 4171
Cdd:cd17643   202 adrDGRDPLALRYVIFGGEALEAAMLRPWagrfgLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4172 YVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPF-EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIR 4250
Cdd:cd17643   282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4251 GYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTP 4328
Cdd:cd17643   362 GFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDALPLTV 441

                  ....*....
gi 386647928 4329 NGKIDRKAL 4337
Cdd:cd17643   442 NGKLDRAAL 450
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
3856-4337 1.10e-165

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 522.49  E-value: 1.10e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3856 IHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPID 3935
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3936 PEYPEDRIRYMLEDSGAQALLTQRhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVE 4015
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSS---------------------------------PSDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4016 HHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYplFESYMNENGITATILPPTY 4095
Cdd:cd05918   128 HRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLND--LAGFINRLRVTWAFLTPSV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4096 AAYLNPDRMPSLKKLITGGSAASVEFVQQWKDKVLYFNAYGPTEASIVTSiwdeASDSLGDRKSVPIGRPLANhRIYVVD 4175
Cdd:cd05918   206 ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAAT----VSPVVPSTDPRNIGRPLGA-TCWVVD 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4176 --SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNP-------FEPGERMYRTGDLVRWLPDGNLEYLGRIDHQ 4246
Cdd:cd05918   281 pdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQ 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4247 VKIRGYRIELGEVETQLAKIDAVQE---AIVLAREDANGQQQLVAyFVAQRELT--------------------AAELRA 4303
Cdd:cd05918   361 VKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVA-FVVLDGSSsgsgdgdslflepsdefralVAELRS 439
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 4304 TMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05918   440 KLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
287-684 4.70e-165

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 517.20  E-value: 4.70e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   287 TYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQG 365
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   366 HLQERVSFSGTWIRLDD--EEAYHEDGSNLESVN---GPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVV-KNTNYIDVTG 439
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDplELAALDDAPAPPPPDapsGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLaWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   440 QDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKL-AGLIEKQQISVMFITTAFFNVLVDMNPDCLRHARAI 518
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   519 LFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEE-GAVSIPIGGPISNTAIYIVNAQNKLQPIGVAG 597
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDApRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   598 ELCVAGDGLARGYLNRPDLTAEKFADNPFAP--GERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLK 675
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 386647928   676 LEAIEKATV 684
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
274-747 7.42e-165

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 518.79  E-value: 7.42e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN 433
Cdd:cd17643    81 ADSGPSLLLTD----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  434 YI-DVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVD----MN 508
Cdd:cd17643   127 RWfGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaadrDG 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  509 PDCLRhARAILFGGERVSVSHVR---KALGHLGPGKIkHVYGPTESTVFATSY--DVHEVEEGAVSiPIGGPISNTAIYI 583
Cdd:cd17643   207 RDPLA-LRYVIFGGEALEAAMLRpwaGRFGLDRPQLV-NMYGITETTVHVTFRplDAADLPAAAAS-PIGRPLPGLRVYV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  584 VNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGF 662
Cdd:cd17643   284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  663 RIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVAD--RSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNG 740
Cdd:cd17643   364 RIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443

                  ....*..
gi 386647928  741 KVDRRAL 747
Cdd:cd17643   444 KLDRAAL 450
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
7449-7929 1.51e-164

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 517.49  E-value: 1.51e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7449 HGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDP 7528
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7529 EYPEDRIRYMLEDSGAQVLLTQrhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEH 7608
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTN----------------------------------PDDLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7609 HGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYA 7688
Cdd:cd17645   127 HNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7689 IYLSPDRLPSLKKLITGGSAASVeFVqqwKDKVRYFNAYGPTEASIVTSVWAASPDgldLRSVPIGRPIANHQIFIVDSQ 7768
Cdd:cd17645   207 EQFMQLDNQSLRVLLTGGDKLKK-IE---RKGYKLVNNYGPTENTVVATSFEIDKP---YANIPIGKPIDNTRVYILDEA 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7769 NHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELG 7848
Cdd:cd17645   280 LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPG 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7849 EIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd17645   360 EIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439

                  .
gi 386647928 7929 P 7929
Cdd:cd17645   440 P 440
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
5949-6420 7.67e-164

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 515.71  E-value: 7.67e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQghlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTN 6108
Cdd:cd17643    81 ADSGPSLLLTD----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6109 YV-ELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMF 6187
Cdd:cd17643   127 RWfGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDG 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6188 ---AGLKTLIVGGDVLSVphinRVLR---EHAGLS---IVNGYGPTEnTTFSTTHTIVGEQ----KEAVPIGKPINNSTA 6254
Cdd:cd17643   207 rdpLALRYVIFGGEALEA----AMLRpwaGRFGLDrpqLVNMYGITE-TTVHVTFRPLDAAdlpaAAASPIGRPLPGLRV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6255 YIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIR 6333
Cdd:cd17643   282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6334 GYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVA--ERELTIGELRAALSQELPNYMIPSHFVPLERMPLTP 6411
Cdd:cd17643   362 GFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAddGAAADIAELRALLKELLPDYMVPARYVPLDALPLTV 441

                  ....*....
gi 386647928 6412 NGKIDRRAL 6420
Cdd:cd17643   442 NGKLDRAAL 450
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
3868-4337 1.44e-163

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 515.69  E-value: 1.44e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQRHLRERvsFAGTFVAV-DDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMF 4026
Cdd:cd12116    81 EDAEPALVLTDDALPDR--LPAGLPVLlLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4027 ANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGIT---ATilPPT-----YAAY 4098
Cdd:cd12116   159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITvmqAT--PATwrmllDAGW 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4099 LNPDRMpslkKLITGGSAASVEFVQQWKDKV--LYfNAYGPTEasivTSIWDEASDSLGDRKSVPIGRPLANHRIYVVDS 4176
Cdd:cd12116   237 QGRAGL----TALCGGEALPPDLAARLLSRVgsLW-NLYGPTE----TTIWSTAARVTAAAGPIPIGRPLANTQVYVLDA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4177 HNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPF-EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIE 4255
Cdd:cd12116   308 ALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4256 LGEVETQLAKIDAVQEAIVLAREDaNGQQQLVAYFVAQRE--LTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:cd12116   388 LGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGaaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466

                  ....
gi 386647928 4334 RKAL 4337
Cdd:cd12116   467 RKAL 470
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
274-747 3.21e-163

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 513.94  E-value: 3.21e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVK--N 431
Cdd:cd17650    81 EDSGAKLLLTQ----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHawR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  432 TNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVL---VDMN 508
Cdd:cd17650   127 REYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVmayVYRN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  509 PDCLRHARAILFGGERVSVSHVRKALGHLGPG-KIKHVYGPTESTVFATSYDVHEVE-EGAVSIPIGGPISNTAIYIVNA 586
Cdd:cd17650   207 GLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGmRIINSYGVTEATIDSTYYEEGRDPlGDSANVPIGRPLPNTAMYVLDE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  587 QNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIEL 666
Cdd:cd17650   287 RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIEL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  667 GEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRA 746
Cdd:cd17650   367 GEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRA 446

                  .
gi 386647928  747 L 747
Cdd:cd17650   447 L 447
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
274-747 4.67e-163

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 514.53  E-value: 4.67e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQGHLQERVSFSGTWIrLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIrvvkntN 433
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVL-LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLV------N 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  434 YI-------DVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVD 506
Cdd:cd12116   154 FLhsmrerlGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  507 MNPDCLRHARAiLFGGERVSVSHVRKALGHlgPGKIKHVYGPTESTVFATsydVHEVEEGAVSIPIGGPISNTAIYIVNA 586
Cdd:cd12116   234 AGWQGRAGLTA-LCGGEALPPDLAARLLSR--VGSLWNLYGPTETTIWST---AARVTAAAGPIPIGRPLANTQVYVLDA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  587 QNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFA-PGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIE 665
Cdd:cd12116   308 ALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  666 LGEIEAHLLKLEAIEKATVVVREsANGEKQLCAYYVADRSLPAN--EVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVD 743
Cdd:cd12116   388 LGEIEAALAAHPGVAQAAVVVRE-DGGDRRLVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466

                  ....
gi 386647928  744 RRAL 747
Cdd:cd12116   467 RKAL 470
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
2359-2828 5.34e-163

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 514.15  E-value: 5.34e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQRRLQERVSfAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA 2518
Cdd:cd12116    81 EDAEPALVLTDDALPDRLP-AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPT------YAVYLNP 2592
Cdd:cd12116   160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPAtwrmllDAGWQGR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2593 DHMpdfkRLIAAGSASSLELLQQWKDKV-KYFNAYGPTEdsicTTIWTPSTEDISQLKSVPIGGPIVNHRIYIVDAHYQP 2671
Cdd:cd12116   240 AGL----TALCGGEALPPDLAARLLSRVgSLWNLYGPTE----TTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2672 VPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEI 2750
Cdd:cd12116   312 VPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEI 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2751 EEQLLKVASVQEAIVIAHDDaSGQKQLCAYFVADRTMTV--GELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd12116   392 EAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAAPdaAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
274-748 2.24e-162

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 511.03  E-value: 2.24e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKN-T 432
Cdd:cd17652    81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAqI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  433 NYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAffnVLVDMNPDCL 512
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPA---ALAALPPDDL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  513 RHARAILFGGERVSVSHVRKalghLGPGK-IKHVYGPTESTVFATSYDVhevEEGAVSIPIGGPISNTAIYIVNAQNKLQ 591
Cdd:cd17652   204 PDLRTLVVAGEACPAELVDR----WAPGRrMINAYGPTETTVCATMAGP---LPGGGVPPIGRPVPGTRVYVLDARLRPV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  592 PIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIE 670
Cdd:cd17652   277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  671 AHLLKLEAIEKATVVVRESANGEKQLCAYYVADRS--LPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALP 748
Cdd:cd17652   357 AALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
5936-6421 2.87e-162

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 511.98  E-value: 2.87e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPI 6015
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6016 DPDYPEDRIRYMLEDSGAKLLLVQghlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMV 6095
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6096 EHRNVVRLVKNTNYV-ELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAP 6174
Cdd:cd17644   127 EHQSLVNLSHGLIKEyGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6175 LYNQL----SQQDSGMFAGLKTLIVGGDVLsVPHINRVLREHAGLSI--VNGYGPTENTTFSTTHTIVGEQKEA---VPI 6245
Cdd:cd17644   207 YWHLLvlelLLSTIDLPSSLRLVIVGGEAV-QPELVRQWQKNVGNFIqlINVYGPTEATIAATVCRLTQLTERNitsVPI 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6246 GKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFL--PGERCYRTGDLARWLPDGTLEYK 6323
Cdd:cd17644   286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6324 GRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVA--ERELTIGELRAALSQELPNYMIPSHF 6401
Cdd:cd17644   366 GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPhyEESPSTVELRQFLKAKLPDYMIPSAF 445
                         490       500
                  ....*....|....*....|
gi 386647928 6402 VPLERMPLTPNGKIDRRALP 6421
Cdd:cd17644   446 VVLEELPLTPNGKIDRRALP 465
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
263-747 3.48e-162

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 512.59  E-value: 3.48e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  263 HRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDP 342
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  343 EYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTH 422
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  423 RNII-RVVKNTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFF 501
Cdd:cd17646   161 AGIVnRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSML 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  502 NVLVD-MNPDCLRHARAILFGGERVSVSHVRKALgHLGPGKIKHVYGPTESTVFATSYDVhEVEEGAVSIPIGGPISNTA 580
Cdd:cd17646   241 RVFLAePAAGSCASLRRVFCSGEALPPELAARFL-ALPGAELHNLYGPTEAAIDVTHWPV-RGPAETPSVPIGRPVPNTR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  581 IYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIR 660
Cdd:cd17646   319 LYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  661 GFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADR---SLPANEVRSTLSQELPAYMLPSYFVQLEQMPLT 737
Cdd:cd17646   399 GFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaaGPDTAALRAHLAERLPEYMVPAAFVVLDALPLT 478
                         490
                  ....*....|
gi 386647928  738 TNGKVDRRAL 747
Cdd:cd17646   479 ANGKLDRAAL 488
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1303-1796 3.94e-162

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 512.66  E-value: 3.94e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1303 FEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 1382
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLEDSAASVLLTQTHLQERAqqwGQTLQAVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIE 1462
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGEL---AVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1463 HRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITI-FESTP 1541
Cdd:cd17651   158 HRSLANLVAWQARASSLGP-GARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRvFLPTV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 ALiipfmDYVAEHGLDMS----SMELLITSSDSCSVTDyrVLQERFGSQ--FRIINAYGVTEAAIDSSLY-DEPLAKLPE 1614
Cdd:cd17651   237 AL-----RALAEHGRPLGvrlaALRYLLTGGEQLVLTE--DLREFCAGLpgLRLHNHYGPTETHVVTALSlPGDPAAWPA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1615 AgnVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGN 1694
Cdd:cd17651   310 P--PPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1695 VDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFT--AESELKLSELRSSLSQELPGYMI 1772
Cdd:cd17651   388 LEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVgdPEAPVDAAELRAALATHLPEYMV 467
                         490       500
                  ....*....|....*....|....
gi 386647928 1773 PSYFVQLEQLPLTANGKIDRKALP 1796
Cdd:cd17651   468 PSAFVLLDALPLTPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
7473-7865 5.00e-162

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 508.73  E-value: 5.00e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7473 TYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQR 7551
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7552 HLQECVSFDGKVIA--ADDEQAYGEDGSNLEPV---VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITE 7626
Cdd:TIGR01733   81 ALASRLAGLVLPVIllDPLELAALDDAPAPPPPdapSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7627 EDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYM-NENGITAAILPPTYA---IYLSPDRLPSLKKL 7702
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLallAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7703 ITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDGLDL-RSVPIGRPIANHQIFIVDSQNHMLPVGVAG 7778
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVDPDDAPReSPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7779 ELCISGAGLARGYLNRPELTAEKFVDNPFL--AGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLK 7856
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 386647928  7857 IASVQETIV 7865
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
7460-7928 8.06e-162

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 509.70  E-value: 8.06e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQrhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSlklMFA 7619
Cdd:cd17650    81 EDSGAKLLLTQ----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAH---AAH 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7620 ETLRITEED----RVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAI------ 7689
Cdd:cd17650   124 AWRREYELDsfpvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRpvmayv 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7690 YLSPDRLPSLKKLITGGSAAS----VEFVQQWKDKVRYFNAYGPTEASIVTSVWAASPDGL-DLRSVPIGRPIANHQIFI 7764
Cdd:cd17650   204 YRNGLDLSAMRLLIVGSDGCKaqdfKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLgDSANVPIGRPLPNTAMYV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7765 VDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYR 7844
Cdd:cd17650   284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7845 IELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKID 7924
Cdd:cd17650   364 IELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443

                  ....
gi 386647928 7925 RNAL 7928
Cdd:cd17650   444 RRAL 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
7448-7928 8.14e-162

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 511.32  E-value: 8.14e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7448 IHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPID 7527
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7528 PEYPEDRIRYMLEDSGAQVLLTQRhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVE 7607
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSS---------------------------------PSDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7608 HHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYplFESYMNENGITAAILPPTY 7687
Cdd:cd05918   128 HRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLND--LAGFINRLRVTWAFLTPSV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7688 AIYLSPDRLPSLKKLITGGSAASVEFVQQWKDKVRYFNAYGPTEASIVTSVwaaSPDGLDLRSVPIGRPIANHqIFIVDS 7767
Cdd:cd05918   206 ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATV---SPVVPSTDPRNIGRPLGAT-CWVVDP 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7768 QNH--MLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNP-------FLAGERMYRTGDLARWLPDGNIEYLGRIDHQV 7838
Cdd:cd05918   282 DNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQV 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7839 KIRGYRIELGEIEEQLLKIASVQETIV---IARGDANGQQQLCAYFVADRELT-------------------VSELRGTL 7896
Cdd:cd05918   362 KIRGQRVELGEIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefralVAELRSKL 441
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 7897 SQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05918   442 RQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
5949-6420 1.40e-161

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 508.93  E-value: 1.40e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQghlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKN-T 6107
Cdd:cd17650    81 EDSGAKLLLTQ----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6108 NYVELNEQTH-ILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPL------YNQLS 6180
Cdd:cd17650   127 REYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALirpvmaYVYRN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6181 QQDsgmFAGLKTLIVGGDVLSVPHINRVLRE-HAGLSIVNGYGPTENTTFSTTH--TIVGEQKEA-VPIGKPINNSTAYI 6256
Cdd:cd17650   207 GLD---LSAMRLLIVGSDGCKAQDFKTLAARfGQGMRIINSYGVTEATIDSTYYeeGRDPLGDSAnVPIGRPLPNTAMYV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6257 VDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYR 6336
Cdd:cd17650   284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6337 IELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:cd17650   364 IELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443

                  ....
gi 386647928 6417 RRAL 6420
Cdd:cd17650   444 RRAL 447
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
5962-6357 1.93e-161

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 507.19  E-value: 1.93e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5962 TYGELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQG 6040
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6041 HLLDRASFADKLVNLND--DGAYHEDGSNLEPVN---GPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLV-KNTNYVELNE 6114
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDplELAALDDAPAPPPPDapsGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLaWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6115 QTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKN-AIQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTL 6193
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6194 IVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGE---QKEAVPIGKPINNSTAYIVDSKLSLLPVGVWG 6270
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDdapRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6271 ELIVGGDGVARGYLNRPELTAEKFVESSFLP--GERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLK 6348
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 386647928  6349 VASVKEATV 6357
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
5938-6421 3.08e-161

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 507.86  E-value: 3.08e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5938 HQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDP 6017
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6018 DYPEDRIRYMLEDSGAKLLLVQghlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEH 6097
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTN----------------------------------PDDLAYVIYTSGSTGLPKGVMIEH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6098 RNVVRLVK-NTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLY 6176
Cdd:cd17645   127 HNLVNLCEwHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6177 NQLSQQDSgmfAGLKTLIVGGDVLsvphiNRVLREhaGLSIVNGYGPTENTTFSTTHTIVGEQkEAVPIGKPINNSTAYI 6256
Cdd:cd17645   207 EQFMQLDN---QSLRVLLTGGDKL-----KKIERK--GYKLVNNYGPTENTVVATSFEIDKPY-ANIPIGKPIDNTRVYI 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6257 VDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYR 6336
Cdd:cd17645   276 LDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYR 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6337 IELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:cd17645   356 IEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435

                  ....*
gi 386647928 6417 RRALP 6421
Cdd:cd17645   436 RKALP 440
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
2372-2765 3.25e-161

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 506.42  E-value: 3.25e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2372 TYRELNERANRLARTLQAL-GVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQR 2450
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2451 RLQERVSFAGTVVT--VDDEQAYAGDGSNLE---SAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINA 2525
Cdd:TIGR01733   81 ALASRLAGLVLPVIllDPLELAALDDAPAPPppdAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2526 QDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNG-ITTATLPPTYA---VYLNPDHMPDFKRL 2601
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLallAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2602 IAAGSASSLELLQQWKDK---VKYFNAYGPTEDSICTTIWTPSTEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAG 2678
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2679 ELCIAGVGLARGYLNRPDLTAEKFVDNPF--EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLK 2756
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 386647928  2757 VASVQEAIV 2765
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
2359-2828 4.60e-161

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 507.62  E-value: 4.60e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQrrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLkqmFA 2518
Cdd:cd17643    81 ADSGPSLLLTD----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLAL---FA 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NT---LQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGIT------TATLPPTYAVY 2589
Cdd:cd17643   124 ATqrwFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTvlnqtpSAFYQLVEAAD 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2590 LNPDHMPDFKRLIAAGSASSLELLQQW-----KDKVKYFNAYGPTEDSICTTIWTPSTEDISQLKSVPIGGPIVNHRIYI 2664
Cdd:cd17643   204 RDGRDPLALRYVIFGGEALEAAMLRPWagrfgLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRVYV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2665 VDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGY 2743
Cdd:cd17643   284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2744 RIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVAD--RTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNG 2821
Cdd:cd17643   364 RIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443

                  ....*..
gi 386647928 2822 KIDRKAL 2828
Cdd:cd17643   444 KLDRAAL 450
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
2359-2828 7.13e-161

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 507.01  E-value: 7.13e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQrrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA 2518
Cdd:cd17650    81 EDSGAKLLLTQ----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NTLQINAQD-RVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYA------VYLN 2591
Cdd:cd17650   127 REYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIrpvmayVYRN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2592 PDHMPDFKRLIAaGSASSL-----ELLQQWKDKVKYFNAYGPTEDSICTTIWTPSTEDISQLKSVPIGGPIVNHRIYIVD 2666
Cdd:cd17650   207 GLDLSAMRLLIV-GSDGCKaqdfkTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLD 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2667 AHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIE 2746
Cdd:cd17650   286 ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIE 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2747 LGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRK 2826
Cdd:cd17650   366 LGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445

                  ..
gi 386647928 2827 AL 2828
Cdd:cd17650   446 AL 447
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
4893-5386 3.14e-160

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 507.27  E-value: 3.14e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4893 FEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 4972
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLEDSAASVLLTQTHLQERAqqwGQTLQAALCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIE 5052
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGEL---AVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5053 HRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITI-FESTP 5131
Cdd:cd17651   158 HRSLANLVAWQARASSLGP-GARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRvFLPTV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 ALiipfmDYVAEHGLDMS----SMVLLITSSDSCSVTDyrVLQERFGSQ--FRIINAYGVTEAAIDSSLY-DEPLAKLPE 5204
Cdd:cd17651   237 AL-----RALAEHGRPLGvrlaALRYLLTGGEQLVLTE--DLREFCAGLpgLRLHNHYGPTETHVVTALSlPGDPAAWPA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5205 AgnVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGN 5284
Cdd:cd17651   310 P--PPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5285 VDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFT--AESELKLSELRSSLSQELPGYMI 5362
Cdd:cd17651   388 LEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVgdPEAPVDAAELRAALATHLPEYMV 467
                         490       500
                  ....*....|....*....|....
gi 386647928 5363 PSYFVQLEQLPLTANGKIDRKALP 5386
Cdd:cd17651   468 PSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
5949-6421 1.14e-159

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 502.94  E-value: 1.14e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQghlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKN-T 6107
Cdd:cd17652    81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAqI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6108 NYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLynqLSQQDSGMF 6187
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAA---LAALPPDDL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6188 AGLKTLIVGGDVLSVPhinRVLREHAGLSIVNGYGPTENTTFSTTH-TIVGEQkeAVPIGKPINNSTAYIVDSKLSLLPV 6266
Cdd:cd17652   204 PDLRTLVVAGEACPAE---LVDRWAPGRRMINAYGPTETTVCATMAgPLPGGG--VPPIGRPVPGTRVYVLDARLRPVPP 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6267 GVWGELIVGGDGVARGYLNRPELTAEKFVESSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQ 6345
Cdd:cd17652   279 GVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAA 358
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 6346 LLKVASVKEATVIVREDESGQKQLCAYFVAERE--LTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALP 6421
Cdd:cd17652   359 LTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
7460-7928 4.12e-159

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 502.22  E-value: 4.12e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQrhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLklmFA 7619
Cdd:cd17643    81 ADSGPSLLLTD----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLAL---FA 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7620 ET---LRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGIT------AAILPPTYAIY 7690
Cdd:cd17643   124 ATqrwFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTvlnqtpSAFYQLVEAAD 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7691 LSPDRLPSLKKLITGGSAASVEFVQQW-----KDKVRYFNAYGPTEASIVTSVWAASPDGLDLRSV-PIGRPIANHQIFI 7764
Cdd:cd17643   204 RDGRDPLALRYVIFGGEALEAAMLRPWagrfgLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAAsPIGRPLPGLRVYV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7765 VDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPF-LAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGY 7843
Cdd:cd17643   284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7844 RIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVAD--RELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNG 7921
Cdd:cd17643   364 RIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443

                  ....*..
gi 386647928 7922 KIDRNAL 7928
Cdd:cd17643   444 KLDRAAL 450
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1300-1795 5.88e-159

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 503.35  E-value: 5.88e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1300 HALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 1379
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1380 DYPSDRIQFMLEDSAASVLLTQTHLQERAQQwgqtLQAVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGV 1459
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPA----GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 MIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFES 1539
Cdd:cd17646   157 MVTHAGIVNRLLWMQDEYPLGP-GDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1540 TPALIIPFMDYVAEHGLDmsSMELLITSSDSCSVTDYRVLQERFGSQFRiiNAYGVTEAAIDSSLYdePLAKLPEAGNVP 1619
Cdd:cd17646   236 VPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELH--NLYGPTEAAIDVTHW--PVRGPAETPSVP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1620 IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIG 1699
Cdd:cd17646   310 IGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1700 RIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTA---ESELKLSELRSSLSQELPGYMIPSYF 1776
Cdd:cd17646   390 RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPaagAAGPDTAALRAHLAERLPEYMVPAAF 469
                         490
                  ....*....|....*....
gi 386647928 1777 VQLEQLPLTANGKIDRKAL 1795
Cdd:cd17646   470 VVLDALPLTANGKLDRAAL 488
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1300-1796 1.04e-158

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 501.58  E-value: 1.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1300 HALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 1379
Cdd:cd17644     3 HQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1380 DYPSDRIQFMLEDSAASVLLTQthlqeraqqwgqtlqavlclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGV 1459
Cdd:cd17644    83 NYPQERLTYILEDAQISVLLTQ--------------------------------------PENLAYVIYTSGSTGKPKGV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 MIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFES 1539
Cdd:cd17644   125 MIEHQSLVNLSHGLIKEYGITS-SDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1540 TPALIIPFMDYVAEHGLDM-SSMELLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNV 1618
Cdd:cd17644   204 PPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1619 PIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFV--EGERLYRTGDLARWMPDGNVD 1696
Cdd:cd17644   284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1697 FIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLS--ELRSSLSQELPGYMIPS 1774
Cdd:cd17644   364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPStvELRQFLKAKLPDYMIPS 443
                         490       500
                  ....*....|....*....|..
gi 386647928 1775 YFVQLEQLPLTANGKIDRKALP 1796
Cdd:cd17644   444 AFVVLEELPLTPNGKIDRRALP 465
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
2347-2828 3.44e-158

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 500.92  E-value: 3.44e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2347 IHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPID 2426
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2427 PEYPEDRISYMLEDSSAQVLLAQRrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVE 2506
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSS---------------------------------PSDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2507 HHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYqwFERYMSDNGITTATLPPTY 2586
Cdd:cd05918   128 HRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLND--LAGFINRLRVTWAFLTPSV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2587 AVYLNPDHMPDFKRLIAAGSASSLELLQQWKDKVKYFNAYGPTEDSICTTIWTPSTEDISQLksvpIGGPiVNHRIYIVD 2666
Cdd:cd05918   206 ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRN----IGRP-LGATCWVVD 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2667 A--HYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNP-------FEPGERMYRTGDLAKWLPDGTIEYLGRIDHQ 2737
Cdd:cd05918   281 PdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQ 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2738 VKIRGYRIELGEIEEQLLK---VASVQEAIVIAHDDASGQKQLCAYFVADRTMT-------------------VGELRGE 2795
Cdd:cd05918   361 VKIRGQRVELGEIEHHLRQslpGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefralVAELRSK 440
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 2796 LSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05918   441 LRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
5938-6420 4.41e-158

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 500.65  E-value: 4.41e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5938 HQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDP 6017
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6018 DYPEDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEH 6097
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6098 RNVV-RLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLY 6176
Cdd:cd17646   161 AGIVnRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSML 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6177 NQ-LSQQDSGMFAGLKTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKE-AVPIGKPINNSTA 6254
Cdd:cd17646   241 RVfLAEPAAGSCASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRGPAETpSVPIGRPVPNTRL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6255 YIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRG 6334
Cdd:cd17646   320 YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6335 YRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAER---ELTIGELRAALSQELPNYMIPSHFVPLERMPLTP 6411
Cdd:cd17646   400 FRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaaGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTA 479

                  ....*....
gi 386647928 6412 NGKIDRRAL 6420
Cdd:cd17646   480 NGKLDRAAL 488
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
4890-5385 3.03e-157

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 498.34  E-value: 3.03e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4890 HALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 4969
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4970 DYPSDRIQFMLEDSAASVLLTQTHLQERAQQwgqtLQAALCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGV 5049
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPA----GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5050 MIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFES 5129
Cdd:cd17646   157 MVTHAGIVNRLLWMQDEYPLGP-GDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5130 TPALIIPFMDYVAEHGLDmsSMVLLITSSDSCSVTDYRVLQERFGSQFRiiNAYGVTEAAIDSSLYdePLAKLPEAGNVP 5209
Cdd:cd17646   236 VPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELH--NLYGPTEAAIDVTHW--PVRGPAETPSVP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5210 IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIG 5289
Cdd:cd17646   310 IGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5290 RIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTA---ESELKLSELRSSLSQELPGYMIPSYF 5366
Cdd:cd17646   390 RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPaagAAGPDTAALRAHLAERLPEYMVPAAF 469
                         490
                  ....*....|....*....
gi 386647928 5367 VQLEQLPLTANGKIDRKAL 5385
Cdd:cd17646   470 VVLDALPLTANGKLDRAAL 488
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
5949-6420 1.10e-156

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 496.04  E-value: 1.10e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQGHLLDRASfADKLVNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVR-LVKNT 6107
Cdd:cd12116    81 EDAEPALVLTDDALPDRLP-AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNfLHSMR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6108 NYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMF 6187
Cdd:cd12116   160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6188 AGLkTLIVGGDVLSVPHINRVLREHAglSIVNGYGPTENTTFSTTHTiVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVG 6267
Cdd:cd12116   240 AGL-TALCGGEALPPDLAARLLSRVG--SLWNLYGPTETTIWSTAAR-VTAAAGPIPIGRPLANTQVYVLDAALRPVPPG 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6268 VWGELIVGGDGVARGYLNRPELTAEKFVESSFL-PGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQL 6346
Cdd:cd12116   316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAAL 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 6347 LKVASVKEATVIVREDEsGQKQLCAYFVAERE--LTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd12116   396 AAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGaaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
4890-5386 1.12e-156

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 495.80  E-value: 1.12e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4890 HALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 4969
Cdd:cd17644     3 HQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4970 DYPSDRIQFMLEDSAASVLLTQthlqeraqqwgqtlqaalclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGV 5049
Cdd:cd17644    83 NYPQERLTYILEDAQISVLLTQ--------------------------------------PENLAYVIYTSGSTGKPKGV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5050 MIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFES 5129
Cdd:cd17644   125 MIEHQSLVNLSHGLIKEYGITS-SDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5130 TPALIIPFMDYVAEHGLDM-SSMVLLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNV 5208
Cdd:cd17644   204 PPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5209 PIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFV--EGERLYRTGDLARWMPDGNVD 5286
Cdd:cd17644   284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5287 FIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLS--ELRSSLSQELPGYMIPS 5364
Cdd:cd17644   364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPStvELRQFLKAKLPDYMIPS 443
                         490       500
                  ....*....|....*....|..
gi 386647928 5365 YFVQLEQLPLTANGKIDRKALP 5386
Cdd:cd17644   444 AFVVLEELPLTPNGKIDRRALP 465
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
274-748 1.58e-156

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 494.58  E-value: 1.58e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQGhlqervsfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNT- 432
Cdd:cd17649    81 EDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATa 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  433 NYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFN----VLVDMN 508
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQqlaeEADRTG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  509 PDCLRHARAILFGGERVSVSHVRKALGhlGPGKIKHVYGPTESTVFATSYDVH-EVEEGAVSIPIGGPISNTAIYIVNAQ 587
Cdd:cd17649   208 DGRPPSLRLYIFGGEALSPELLRRWLK--APVRLFNAYGPTEATVTPLVWKCEaGAARAGASMPIGRPLGGRSAYILDAD 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  588 NKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIEL 666
Cdd:cd17649   286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  667 GEIEAHLLKLEAIEKAtVVVRESANGEKQLCAYYV--ADRSLPAN--EVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKV 742
Cdd:cd17649   366 GEIEAALLEHPGVREA-AVVALDGAGGKQLVAYVVlrAAAAQPELraQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444

                  ....*.
gi 386647928  743 DRRALP 748
Cdd:cd17649   445 DRKALP 450
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
5-835 2.02e-156

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 525.38  E-value: 2.02e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    5 AFERETAFWNKIFEGEEnPPTALPYSKAQKQAPAL-VRRMSTALSKEVSERIIQMSKGAPLPAymILLTGVQSLLYKYTS 83
Cdd:PRK10252  192 AWQRDAAFWAEQRRQLP-PPASLSPAPLPGRSASAdILRLKLEFTDGAFRQLAAQASGVQRPD--LALALVALWLGRLCG 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   84 SSSILVGMPVVtkpnenRR----------PVNQLVILREEVRDDSTFKALLGEAKNSVTSSINHQnvpfRLMTERL--EL 151
Cdd:PRK10252  269 RMDYAAGFIFM------RRlgsaaltatgPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQ----RYDAEQIvrDS 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  152 QYADGV-----PVVNTLVALKQLHITDYRQSA-------VSDVLFEFELDKD-EVRLHLTYNGNLYTESFIAQAVDHLNR 218
Cdd:PRK10252  339 GRAAGDeplfgPVLNIKVFDYQLDFPGVQAQThtlatgpVNDLELALFPDEHgGLSIEILANPQRYDEATLIAHAERLKA 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  219 LFSVVLFQPDLALGQADLLSEAEkHQLLDAFNKTGTDYPrDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRL 298
Cdd:PRK10252  419 LIAQFAADPALLCGDVDILLPGE-YAQLAQVNATAVEIP-ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVAL 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  299 ARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWI 378
Cdd:PRK10252  497 ANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLT 576
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  379 RLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDKLLQLSSYSFDGSTFD 457
Cdd:PRK10252  577 SLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVnRLLWMQNHYPLTADDVVLQKTPCSFDVSVWE 656
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  458 IFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVM-FITT---AFFNVL-VDMNPDCLRHARAILFGGERVSVSHVRK 532
Cdd:PRK10252  657 FFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPSmlaAFVASLtPEGARQSCASLRQVFCSGEALPADLCRE 736
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  533 ALGHLGpGKIKHVYGPTESTVFATSYDVHEVEEGAV---SIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARG 609
Cdd:PRK10252  737 WQQLTG-APLHNLYGPTEAAVDVSWYPAFGEELAAVrgsSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQG 815
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  610 YLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVR-- 687
Cdd:PRK10252  816 YLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvi 895
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  688 ----ESANGEKQLCAYYVADRSLP--ANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGVEfv 761
Cdd:PRK10252  896 nqaaATGGDARQLVGYLVSQSGLPldTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGR-- 973
                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928  762 EPRTELEAGIVNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISG 835
Cdd:PRK10252  974 APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDA 1047
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
7460-7928 1.27e-154

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 490.27  E-value: 1.27e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQRHLQECVSFDGKVIaADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 7619
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVL-LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7620 ETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAA-ILPPTYAIYLS--PDRL 7696
Cdd:cd12116   160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMqATPATWRMLLDagWQGR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7697 PSLKKLItGGSAASVEFVQQWKDKVR-YFNAYGPTEASIvtsvWA-ASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPV 7774
Cdd:cd12116   240 AGLTALC-GGEALPPDLAARLLSRVGsLWNLYGPTETTI----WStAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7775 GVAGELCISGAGLARGYLNRPELTAEKFVDNPFL-AGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQ 7853
Cdd:cd12116   315 GVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAA 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 7854 LLKIASVQETIVIARGDaNGQQQLCAYFVADRELTVS--ELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd12116   395 LAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
4914-5316 3.88e-154

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 486.00  E-value: 3.88e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4914 TYRELNERANRLARTLRAQ-GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 4992
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4993 HLQERAQQWGQTlqAALCLDDEAAYAEDASNVANVNE---PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL 5069
Cdd:TIGR01733   81 ALASRLAGLVLP--VILLDPLELAALDDAPAPPPPDApsgPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5070 DQFPvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARL-HYWISEEKITIFESTPALIIPFMdyvAEHGLDM 5148
Cdd:TIGR01733  159 DPDD-RVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVLNLTPSLLALLA---AALPPAL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5149 SSMVLLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALNAKFYIVDAHLNP 5228
Cdd:TIGR01733  235 ASLRLVILGGEALTPALVDRWRARGPGA-RLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRP 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5229 VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFV--EGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGE 5306
Cdd:TIGR01733  314 VPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393
                          410
                   ....*....|
gi 386647928  5307 IETQLLKAEG 5316
Cdd:TIGR01733  394 IEAALLRHPG 403
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1324-1726 5.87e-154

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 485.62  E-value: 5.87e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1324 TYRELNERANRLARMLRAQ-GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 1402
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1403 HLQERAQQWGQTlqAVLCLDDEAAYAEDASNVANVNE---PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL 1479
Cdd:TIGR01733   81 ALASRLAGLVLP--VILLDPLELAALDDAPAPPPPDApsgPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1480 DQFPvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARL-HYWISEEKITIFESTPALIIPFMdyvAEHGLDM 1558
Cdd:TIGR01733  159 DPDD-RVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVLNLTPSLLALLA---AALPPAL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1559 SSMELLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALNAKFYIVDAHLNP 1638
Cdd:TIGR01733  235 ASLRLVILGGEALTPALVDRWRARGPGA-RLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRP 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1639 VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFV--EGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGE 1716
Cdd:TIGR01733  314 VPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393
                          410
                   ....*....|
gi 386647928  1717 IETQLLKAEG 1726
Cdd:TIGR01733  394 IEAALLRHPG 403
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
5949-6421 1.31e-153

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 486.49  E-value: 1.31e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQGhlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNT- 6107
Cdd:cd17649    81 EDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATa 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6108 NYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQ----QD 6183
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEeadrTG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6184 SGMFAGLKTLIVGGDVLSVPHINRVLREHAGLsiVNGYGPTENTTFSTTHTI---VGEQKEAVPIGKPINNSTAYIVDSK 6260
Cdd:cd17649   208 DGRPPSLRLYIFGGEALSPELLRRWLKAPVRL--FNAYGPTEATVTPLVWKCeagAARAGASMPIGRPLGGRSAYILDAD 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6261 LSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFL-PGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIEL 6339
Cdd:cd17649   286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6340 GEIEEQLLKVASVKEATVIVReDESGQKQLCAYFVAERELTIGE----LRAALSQELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:cd17649   366 GEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPElraqLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444

                  ....*.
gi 386647928 6416 DRRALP 6421
Cdd:cd17649   445 DRKALP 450
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1310-1796 2.20e-153

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 486.98  E-value: 2.20e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1310 TPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFM 1389
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1390 LEDSAASVLLTQTHLQERAQQWGQTLQavlcLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNT 1469
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTIL----LEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1470 AAgYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKI-TIFESTPALIIPFM 1548
Cdd:cd17656   157 LH-FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIeVVFLPVAFLKFIFS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1549 DYVAEHGLdMSSMELLITSSDSCSVTD--YRVLQERfgsQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGnvPIGKAALN 1626
Cdd:cd17656   236 EREFINRF-PTCVKHIITAGEQLVITNefKEMLHEH---NVHLHNHYGPSETHVVTTYTINPEAEIPELP--PIGKPISN 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1627 AKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAK 1706
Cdd:cd17656   310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1707 IRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTA 1786
Cdd:cd17656   390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTP 469
                         490
                  ....*....|
gi 386647928 1787 NGKIDRKALP 1796
Cdd:cd17656   470 NGKVDRKALP 479
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
5937-6420 3.27e-153

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 484.90  E-value: 3.27e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5937 IHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPID 6016
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6017 PDYPEDRIRYMLEDSGAKLLLVQghlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVE 6096
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTD----------------------------------PDDLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6097 HRNVVRLVKNTNYVELNEQ-THILQTGAVVFDASTFEIWGALLNGGRLYVVrnETILDAVSLKNAIQQYGINTMWLTApl 6175
Cdd:cd12115   127 HRNAAAFLQWAAAAFSAEElAGVLASTSICFDLSVFELFGPLATGGKVVLA--DNVLALPDLPAAAEVTLINTVPSAA-- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6176 yNQLSQQDsGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAY 6255
Cdd:cd12115   203 -AELLRHD-ALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAY 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6256 IVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGY 6335
Cdd:cd12115   281 VLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGF 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6336 RIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNG 6413
Cdd:cd12115   361 RIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNG 440

                  ....*..
gi 386647928 6414 KIDRRAL 6420
Cdd:cd12115   441 KIDRSAL 447
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
4900-5386 3.30e-153

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 486.60  E-value: 3.30e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4900 TPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFM 4979
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4980 LEDSAASVLLTQTHLQERAQQWGQTLQaalcLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNT 5059
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTIL----LEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5060 AAgYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFeSTPALIIPFMD 5139
Cdd:cd17656   157 LH-FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5140 YVAEHGLDMSSMVL-LITSSDSCSVTD--YRVLQERfgsQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGnvPIGKAALN 5216
Cdd:cd17656   235 SEREFINRFPTCVKhIITAGEQLVITNefKEMLHEH---NVHLHNHYGPSETHVVTTYTINPEAEIPELP--PIGKPISN 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5217 AKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAK 5296
Cdd:cd17656   310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5297 IRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTA 5376
Cdd:cd17656   390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTP 469
                         490
                  ....*....|
gi 386647928 5377 NGKIDRKALP 5386
Cdd:cd17656   470 NGKVDRKALP 479
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
3856-4337 1.72e-152

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 482.97  E-value: 1.72e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3856 IHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPID 3935
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3936 PEYPEDRIRYMLEDSGAQALLTQrhlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVE 4015
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTD----------------------------------PDDLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4016 HHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIptSTTILDYPLFESYMNengitATIL---P 4092
Cdd:cd12115   127 HRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVL--ADNVLALPDLPAAAE-----VTLIntvP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4093 PTYAAYLNPDRMP-SLKKLITGGSAASVEFVQQWKDK---VLYFNAYGPTEA---SIVTSIwdeasdSLGDRKSVPIGRP 4165
Cdd:cd12115   200 SAAAELLRHDALPaSVRVVNLAGEPLPRDLVQRLYARlqvERVVNLYGPSEDttySTVAPV------PPGASGEVSIGRP 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4166 LANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDH 4245
Cdd:cd12115   274 LANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADN 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4246 QVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQ 4323
Cdd:cd12115   354 QVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLGTRLPAYMVPSRFVRLDA 433
                         490
                  ....*....|....
gi 386647928 4324 MPLTPNGKIDRKAL 4337
Cdd:cd12115   434 LPLTPNGKIDRSAL 447
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1311-1796 1.57e-149

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 474.05  E-value: 1.57e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1311 PEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 1390
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1391 EDSAASVLLTQthlqeraqqwgqtlqavlclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 1470
Cdd:cd17652    81 ADARPALLLTT--------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGYRREYRL--DQfpvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALI--IP 1546
Cdd:cd17652   123 AAQIAAFDVgpGS---RVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALaaLP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1547 FMDYVAEHGLdmssmellITSSDSCSvtdyRVLQERFGSQFRIINAYGVTEAAIDSSLYDeplaKLPEAGNVPIGKAALN 1626
Cdd:cd17652   200 PDDLPDLRTL--------VVAGEACP----AELVDRWAPGRRMINAYGPTETTVCATMAG----PLPGGGVPPIGRPVPG 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1627 AKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVE-GERLYRTGDLARWMPDGNVDFIGRIDNQA 1705
Cdd:cd17652   264 TRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQV 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1706 KIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLP 1783
Cdd:cd17652   344 KIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTaaELRAHLAERLPGYMVPAAFVVLDALP 423
                         490
                  ....*....|...
gi 386647928 1784 LTANGKIDRKALP 1796
Cdd:cd17652   424 LTPNGKLDRRALP 436
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
4901-5386 3.23e-149

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 472.89  E-value: 3.23e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTQthlqeraqqwgqtlqaalclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd17652    81 ADARPALLLTT--------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRL--DQfpvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALI--IP 5136
Cdd:cd17652   123 AAQIAAFDVgpGS---RVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALaaLP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5137 FMDYVAEHGLdmssmvllITSSDSCSvtdyRVLQERFGSQFRIINAYGVTEAAIDSSLYDeplaKLPEAGNVPIGKAALN 5216
Cdd:cd17652   200 PDDLPDLRTL--------VVAGEACP----AELVDRWAPGRRMINAYGPTETTVCATMAG----PLPGGGVPPIGRPVPG 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5217 AKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVE-GERLYRTGDLARWMPDGNVDFIGRIDNQA 5295
Cdd:cd17652   264 TRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQV 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5296 KIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLP 5373
Cdd:cd17652   344 KIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTaaELRAHLAERLPGYMVPAAFVVLDALP 423
                         490
                  ....*....|...
gi 386647928 5374 LTANGKIDRKALP 5386
Cdd:cd17652   424 LTPNGKLDRRALP 436
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
7448-7928 8.33e-149

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 472.57  E-value: 8.33e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7448 IHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPID 7527
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7528 PEYPEDRIRYMLEDSGAQVLLTQrhlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVE 7607
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTD----------------------------------PDDLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7608 HHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLyIPAkDTILDYPLFESYMNENGITAaiLPPTY 7687
Cdd:cd12115   127 HRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKV-VLA-DNVLALPDLPAAAEVTLINT--VPSAA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7688 AIYLSPDRLP-SLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVWAASPDglDLRSVPIGRPIANHQIF 7763
Cdd:cd12115   203 AELLRHDALPaSVRVVNLAGEPLPRDLVQRLYARlqvERVVNLYGPSEDTTYSTVAPVPPG--ASGEVSIGRPLANTQAY 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7764 IVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGY 7843
Cdd:cd12115   281 VLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGF 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7844 RIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVAD--RELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNG 7921
Cdd:cd12115   361 RIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNG 440

                  ....*..
gi 386647928 7922 KIDRNAL 7928
Cdd:cd12115   441 KIDRSAL 447
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
853-1283 1.04e-148

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 472.59  E-value: 1.04e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   853 YPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEM-VGGEPMQRIYPEVEFAVEH 931
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   932 I---RANEEEADAAVKQFIRA-----FDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYG----G 999
Cdd:pfam00668   85 IdisDLSESEEEEAIEAFIQRdlqspFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQqllkG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1000 EDLPALRIQ-YKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIA 1078
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1079 SENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAF 1158
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1159 ERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNT-----ENKEFRLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFLCG 1233
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYlgqdsQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTIK 404
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 386647928  1234 IEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEEKAQLV 1283
Cdd:pfam00668  405 IDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
2347-2828 7.18e-146

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 464.10  E-value: 7.18e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2347 IHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPID 2426
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2427 PEYPEDRISYMLEDSSAQVLLaqrrlqervsfagtvvtvddeqayagdgsnlesaVGPNDLAYIIYTSGTTGKPKGVMVE 2506
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVL----------------------------------TDPDDLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2507 HHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIptKETILDYQWFERYMSDNGITTatLPPTY 2586
Cdd:cd12115   127 HRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVL--ADNVLALPDLPAAAEVTLINT--VPSAA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2587 AVYLNPDHMPDFKRLI-AAGSASSLELLQQWKDK---VKYFNAYGPTEDsicTTIWTPSTEDISQLKSVPIGGPIVNHRI 2662
Cdd:cd12115   203 AELLRHDALPASVRVVnLAGEPLPRDLVQRLYARlqvERVVNLYGPSED---TTYSTVAPVPPGASGEVSIGRPLANTQA 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2663 YIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRG 2742
Cdd:cd12115   280 YVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRG 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2743 YRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVAD--RTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPN 2820
Cdd:cd12115   360 FRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPN 439

                  ....*...
gi 386647928 2821 GKIDRKAL 2828
Cdd:cd12115   440 GKIDRSAL 447
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1311-1795 1.06e-145

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 463.70  E-value: 1.06e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1311 PEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 1390
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1391 EDSAASVLLTqthlqeraqqwgqtlqavlclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 1470
Cdd:cd17643    81 ADSGPSLLLT--------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALF 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGYRREYRLDQFPVRLLqLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 1550
Cdd:cd17643   123 AATQRWFGFNEDDVWTL-FHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1551 VAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQF-RIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALNAKF 1629
Cdd:cd17643   202 ADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRpQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1630 YIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFV-EGERLYRTGDLARWMPDGNVDFIGRIDNQAKIR 1708
Cdd:cd17643   282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1709 GYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTA--ESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTA 1786
Cdd:cd17643   362 GFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAddGAAADIAELRALLKELLPDYMVPARYVPLDALPLTV 441

                  ....*....
gi 386647928 1787 NGKIDRKAL 1795
Cdd:cd17643   442 NGKLDRAAL 450
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
4901-5385 1.44e-145

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 463.32  E-value: 1.44e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTqthlqeraqqwgqtlqaalclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd17643    81 ADSGPSLLLT--------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALF 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRLDQFPVRLLqLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 5140
Cdd:cd17643   123 AATQRWFGFNEDDVWTL-FHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5141 VAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQF-RIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALNAKF 5219
Cdd:cd17643   202 ADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRpQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5220 YIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFV-EGERLYRTGDLARWMPDGNVDFIGRIDNQAKIR 5298
Cdd:cd17643   282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5299 GYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTA--ESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTA 5376
Cdd:cd17643   362 GFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAddGAAADIAELRALLKELLPDYMVPARYVPLDALPLTV 441

                  ....*....
gi 386647928 5377 NGKIDRKAL 5385
Cdd:cd17643   442 NGKLDRAAL 450
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1300-1796 8.46e-145

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 460.48  E-value: 8.46e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1300 HALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 1379
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1380 DYPSDRIQFMLEDSAASVLLTQthlqeraqqwgqtlqavlclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGV 1459
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTN--------------------------------------PDDLAYVIYTSGSTGLPKGV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 MIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITI-FE 1538
Cdd:cd17645   123 MIEHHNLVNLCEWHRPYFGVTPAD-KSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsFL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1539 STPaLIIPFMDyvaehgLDMSSMELLITSSDscsvtdyrVLQERFGSQFRIINAYGVTEAAIDSSLYDEPlaklPEAGNV 1618
Cdd:cd17645   202 PTG-AAEQFMQ------LDNQSLRVLLTGGD--------KLKKIERKGYKLVNNYGPTENTVVATSFEID----KPYANI 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1619 PIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFI 1698
Cdd:cd17645   263 PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFL 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1699 GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQ 1778
Cdd:cd17645   343 GRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVH 422
                         490
                  ....*....|....*...
gi 386647928 1779 LEQLPLTANGKIDRKALP 1796
Cdd:cd17645   423 LKALPLTANGKVDRKALP 440
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1311-1795 2.00e-144

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 460.61  E-value: 2.00e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1311 PEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 1390
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1391 EDSAASVLLTQTHLQERAqqwgqTLQAVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 1470
Cdd:cd12116    81 EDAEPALVLTDDALPDRL-----PAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGYRREYRL---DqfpvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPF 1547
Cdd:cd12116   156 HSMRERLGLgpgD----RLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRML 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1548 MDyVAEHGLDmsSMELLitssdsCS----VTDyrvLQERFGSQFR-IINAYGVTEAAIDSSLydepLAKLPEAGNVPIGK 1622
Cdd:cd12116   232 LD-AGWQGRA--GLTAL------CGgealPPD---LAARLLSRVGsLWNLYGPTETTIWSTA----ARVTAAAGPIPIGR 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1623 AALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVE-GERLYRTGDLARWMPDGNVDFIGRI 1701
Cdd:cd12116   296 PLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpGSRLYRTGDLVRRRADGRLEYLGRA 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1702 DNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvLCAYFTAESELKLS--ELRSSLSQELPGYMIPSYFVQL 1779
Cdd:cd12116   376 DGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRL 454
                         490
                  ....*....|....*.
gi 386647928 1780 EQLPLTANGKIDRKAL 1795
Cdd:cd12116   455 DALPLTANGKLDRKAL 470
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
4901-5385 2.04e-144

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 460.61  E-value: 2.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTQTHLQERAqqwgqTLQAALCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd12116    81 EDAEPALVLTDDALPDRL-----PAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRL---DqfpvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPF 5137
Cdd:cd12116   156 HSMRERLGLgpgD----RLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRML 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5138 MDyVAEHGLDmsSMVLLitssdsCS----VTDyrvLQERFGSQFR-IINAYGVTEAAIDSSLydepLAKLPEAGNVPIGK 5212
Cdd:cd12116   232 LD-AGWQGRA--GLTAL------CGgealPPD---LAARLLSRVGsLWNLYGPTETTIWSTA----ARVTAAAGPIPIGR 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5213 AALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVE-GERLYRTGDLARWMPDGNVDFIGRI 5291
Cdd:cd12116   296 PLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpGSRLYRTGDLVRRRADGRLEYLGRA 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5292 DNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKvLCAHFTAESELKLS--ELRSSLSQELPGYMIPSYFVQL 5369
Cdd:cd12116   376 DGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRL 454
                         490
                  ....*....|....*.
gi 386647928 5370 EQLPLTANGKIDRKAL 5385
Cdd:cd12116   455 DALPLTANGKLDRKAL 470
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
262-747 2.91e-144

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 459.48  E-value: 2.91e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  262 IHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPID 341
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  342 PEYPEERIRYMLEDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTT 421
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTD----------------------------------PDDLAYVIYTSGSTGRPKGVAIE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  422 HRNIIrvvkntNYIDVTGQ----DKL---LQLSSYSFDGSTFDIFGALLNGAKLVLVpkETVLDVAKLAGLIEkqqisVM 494
Cdd:cd12115   127 HRNAA------AFLQWAAAafsaEELagvLASTSICFDLSVFELFGPLATGGKVVLA--DNVLALPDLPAAAE-----VT 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  495 FITT--AFFNVLVDMNPdCLRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATsydVHEVEEGAV-SIP 571
Cdd:cd12115   194 LINTvpSAAAELLRHDA-LPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYST---VAPVPPGASgEVS 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  572 IGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVG 651
Cdd:cd12115   270 IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLG 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  652 RIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPA--NEVRSTLSQELPAYMLPSYFV 729
Cdd:cd12115   350 RADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGlvEDLRRHLGTRLPAYMVPSRFV 429
                         490
                  ....*....|....*...
gi 386647928  730 QLEQMPLTTNGKVDRRAL 747
Cdd:cd12115   430 RLDALPLTPNGKIDRSAL 447
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
4443-4873 1.51e-143

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 457.57  E-value: 1.51e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4443 YPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFEL-IDGEPVQRIYPEVDFAVET 4521
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4522 VQASEQEAKA--------IVRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLY----SG 4589
Cdd:pfam00668   85 IDISDLSESEeeeaieafIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqqllKG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4590 EELPGLRIQ-YKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIA 4668
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4669 AESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAF 4748
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4749 EHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQN-------TENKEMHLPGLHLTPYPTEygMSKFDLSLDMMEDSEGLE 4821
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNylgqdsqEEEFQLSELDLSVSSVIEE--EAKYDLSLTASERGGGLT 402
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386647928  4822 CSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIASLGILTADEKAQIV 4873
Cdd:pfam00668  403 IKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
5937-6420 1.55e-143

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 458.55  E-value: 1.55e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5937 IHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPID 6016
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6017 PDYPEDRIRYMLEDSGAKLLLVqghlldrasfadklvnlnddgayhedgsnlepvNGPEHLTYVIYTSGTTGRPKGVMVE 6096
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLT---------------------------------SSPSDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6097 HRNVV-RLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDavSLKNAIQQYGINTMWLTAPL 6175
Cdd:cd05918   128 HRALStSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTPSV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6176 YNQLSQQDsgmFAGLKTLIVGGDVLSvphiNRVLREHA-GLSIVNGYGPTENTTFSTTHTIVGEQKeAVPIGKPINnSTA 6254
Cdd:cd05918   206 ARLLDPED---VPSLRTLVLGGEALT----QSDVDTWAdRVRLINAYGPAECTIAATVSPVVPSTD-PRNIGRPLG-ATC 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6255 YIVD--SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVE-------SSFLPGERCYRTGDLARWLPDGTLEYKGR 6325
Cdd:cd05918   277 WVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEdpawlkqEGSGRGRRLYRTGDLVRYNPDGSLEYVGR 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6326 IDEQVKIRGYRIELGEIEEQLLK---VASVKEATVIVREDESGQKQLCAYFVAERELT-------------------IGE 6383
Cdd:cd05918   357 KDTQVKIRGQRVELGEIEHHLRQslpGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefralVAE 436
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 6384 LRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05918   437 LRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
262-747 3.91e-143

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 457.39  E-value: 3.91e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  262 IHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPID 341
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  342 PEYPEERIRYMLEDSGTQVLLsqghlqervsfsgtwirlddeeayhedgsnlesVNGPEHLTYVIYTSGTTGKPKGNLTT 421
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVL---------------------------------TSSPSDAAYVIFTSGSTGKPKGVVIE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  422 HRNIIRVVKN-TNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAkLVLVPKETVLdVAKLAGLIEKQQISVMFITTAF 500
Cdd:cd05918   128 HRALSTSALAhGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGG-CLCIPSEEDR-LNDLAGFINRLRVTWAFLTPSV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  501 FNVLvdmNPDCLRHARAILFGGERVSVSHVRKALGHLgpgKIKHVYGPTESTVFATSYDVHEVEEGAVsipIGGPISNTA 580
Cdd:cd05918   206 ARLL---DPEDVPSLRTLVLGGEALTQSDVDTWADRV---RLINAYGPAECTIAATVSPVVPSTDPRN---IGRPLGATC 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  581 iYIVNAQN--KLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNP-------FAPGERMYRTGDLARWLPDGTIEYVG 651
Cdd:cd05918   277 -WVVDPDNhdRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVG 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  652 RIDDQVKIRGFRIELGEIEAHLLKLEAIEK---ATVVVRESANGEKQLCAYYVADRSLP-------------------AN 709
Cdd:cd05918   356 RKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefralVA 435
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 386647928  710 EVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05918   436 ELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
4890-5386 2.45e-142

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 453.55  E-value: 2.45e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4890 HALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 4969
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4970 DYPSDRIQFMLEDSAASVLLTQthlqeraqqwgqtlqaalclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGV 5049
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTN--------------------------------------PDDLAYVIYTSGSTGLPKGV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5050 MIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITI-FE 5128
Cdd:cd17645   123 MIEHHNLVNLCEWHRPYFGVTPAD-KSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsFL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5129 STPaLIIPFMDyvaehgLDMSSMVLLITSSDscsvtdyrVLQERFGSQFRIINAYGVTEAAIDSSLYDEPlaklPEAGNV 5208
Cdd:cd17645   202 PTG-AAEQFMQ------LDNQSLRVLLTGGD--------KLKKIERKGYKLVNNYGPTENTVVATSFEID----KPYANI 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5209 PIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFI 5288
Cdd:cd17645   263 PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFL 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5289 GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQ 5368
Cdd:cd17645   343 GRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVH 422
                         490
                  ....*....|....*...
gi 386647928 5369 LEQLPLTANGKIDRKALP 5386
Cdd:cd17645   423 LKALPLTANGKVDRKALP 440
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
2349-2828 2.24e-141

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 450.61  E-value: 2.24e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2349 QLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPE 2428
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2429 YPEDRISYMLEDSSAQVLLaqrrlqervsfagtvvtvddeqayagdgsnleSAVGPNDLAYIIYTSGTTGKPKGVMVEHH 2508
Cdd:cd17653    81 LPSARIQAILRTSGATLLL--------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMVPHR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2509 GLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIptketildyqwfeRYMSDNGITTA------TL 2582
Cdd:cd17653   129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL-------------ADPSDPFAHVArtvdalMS 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2583 PPTYAVYLNPDHMPDFKRLIAAGSASSLELLQQWKDKVKYFNAYGPTEDSICTTiwTPSTEDISQlksVPIGGPIVNHRI 2662
Cdd:cd17653   196 TPSILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISST--MTELLPGQP---VTIGKPIPNSTC 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2663 YIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRG 2742
Cdd:cd17653   271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2743 YRIELGEIEEQLLKVAS-VQEAIVIAHDDasgqkQLCAyFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNG 2821
Cdd:cd17653   351 FRINLEEIEEVVLQSQPeVTQAAAIVVNG-----RLVA-FVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANG 424

                  ....*..
gi 386647928 2822 KIDRKAL 2828
Cdd:cd17653   425 KVDRKAL 431
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1901-2330 4.73e-140

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 447.55  E-value: 4.73e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1901 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFEL-VNGEPVQRV--YKEVNFAV 1977
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVIleERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1978 EHYR-TSEAEAGEVVRGFVR-----TFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLY----NG 2047
Cdd:pfam00668   85 IDISdLSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqqllKG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2048 ESLATLRIQ-YKDYAVWQQSEEQLERVKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVA 2126
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2127 AESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAY 2206
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2207 EHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNT-----ENEELQLDGLKLAPYPSGNTIARFDLTLDVTETGSGLECN 2281
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYlgqdsQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTIK 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 386647928  2282 LEYATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQTQL 2330
Cdd:pfam00668  405 IDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
5491-5920 2.51e-139

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 445.62  E-value: 2.51e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5491 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFEL-VNGEPVQRV--YKEVNFAV 5567
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVIleERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5568 EHYR-TSEAEAGEVVRGFVR-----TFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMY----NG 5637
Cdd:pfam00668   85 IDISdLSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqqllKG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5638 ESLAPLRIQ-YKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIA 5716
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5717 AESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAY 5796
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5797 EHQSYPFEELVEKAQPARDLSRNPLFDTLFALQN-----KETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSEGLELS 5871
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNylgqdSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTIK 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 386647928  5872 MEYSTALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEKEHI 5920
Cdd:pfam00668  405 IDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
4901-5386 5.99e-139

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 444.12  E-value: 5.99e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTQthlqeraqqwgqtlqaalclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd17649    81 EDSGAGLLLTH-------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRL---DqfpvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPF 5137
Cdd:cd17649   124 QATAERYGLtpgD----RELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQL 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5138 MDYVAEHGLDMS-SMVLLITSSDSCSVtdyRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALN 5216
Cdd:cd17649   200 AEEADRTGDGRPpSLRLYIFGGEALSP---ELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGG 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5217 AKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQA 5295
Cdd:cd17649   277 RSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQV 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5296 KIRGYRIETGEIETQLLKAEGvREAVVVVREDAKGQKVLCAHFTAESELKLSE----LRSSLSQELPGYMIPSYFVQLEQ 5371
Cdd:cd17649   357 KIRGFRIELGEIEAALLEHPG-VREAAVVALDGAGGKQLVAYVVLRAAAAQPElraqLRTALRASLPDYMVPAHLVFLAR 435
                         490
                  ....*....|....*
gi 386647928 5372 LPLTANGKIDRKALP 5386
Cdd:cd17649   436 LPLTPNGKLDRKALP 450
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1311-1796 1.13e-138

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 443.35  E-value: 1.13e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1311 PEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 1390
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1391 EDSAASVLLTQthlqeraqqwgqtlqavlclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 1470
Cdd:cd17649    81 EDSGAGLLLTH-------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGYRREYRL---DqfpvRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPF 1547
Cdd:cd17649   124 QATAERYGLtpgD----RELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQL 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1548 MDYVAEHGLDMS-SMELLITSSDSCSVtdyRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALN 1626
Cdd:cd17649   200 AEEADRTGDGRPpSLRLYIFGGEALSP---ELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGG 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1627 AKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPF-VEGERLYRTGDLARWMPDGNVDFIGRIDNQA 1705
Cdd:cd17649   277 RSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQV 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1706 KIRGYRIETGEIETQLLKAEGvREAVVVVREDAKGQKVLCAYFTAESELKLSE----LRSSLSQELPGYMIPSYFVQLEQ 1781
Cdd:cd17649   357 KIRGFRIELGEIEAALLEHPG-VREAAVVALDGAGGKQLVAYVVLRAAAAQPElraqLRTALRASLPDYMVPAHLVFLAR 435
                         490
                  ....*....|....*
gi 386647928 1782 LPLTANGKIDRKALP 1796
Cdd:cd17649   436 LPLTPNGKLDRKALP 450
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
3859-4337 1.17e-137

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 439.82  E-value: 1.17e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY 3938
Cdd:cd17653     2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 PEDRIRYMLEDSGAQALLTQRhlrervsfagtfvavddeqayhadgsnlepvvGPNHLAYVIYTSGTTGKPKGVMVEHHG 4018
Cdd:cd17653    82 PSARIQAILRTSGATLLLTTD--------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4019 LCS-LKLMFANtLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSttilDYPLFESymnENGITATILPPTYAA 4097
Cdd:cd17653   130 VLNyVSQPPAR-LDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADP----SDPFAHV---ARTVDALMSTPSILS 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4098 YLNPDRMPSLKKLITGGSAASVEFVQQWKDKVLYFNAYGPTEASIVTSIwdeasDSLGDRKSVPIGRPLANHRIYVVDSH 4177
Cdd:cd17653   202 TLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTM-----TELLPGQPVTIGKPIPNSTCYILDAD 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4178 NRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELG 4257
Cdd:cd17653   277 LQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4258 EVETQLAKIDA-VQEAIVLAREDangqqQLVAyFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKA 4336
Cdd:cd17653   357 EIEEVVLQSQPeVTQAAAIVVNG-----RLVA-FVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKA 430

                  .
gi 386647928 4337 L 4337
Cdd:cd17653   431 L 431
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
3868-4338 4.82e-136

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 436.06  E-value: 4.82e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAG-VRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYM 3946
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3947 LEDSGAQALLTqrhlrervsfagtfvavddeqayhadgsnlepvvGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSL---- 4022
Cdd:cd17648    81 LEDTGARVVIT----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLrtsl 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4023 -KLMFantLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAYLNP 4101
Cdd:cd17648   127 sERYF---GRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4102 DRMPSLKKLItggsAASVEFVQQWKDKV------LYFNAYGPTEASiVTSIWDEASDslGDRKSVPIGRPLANHRIYVVD 4175
Cdd:cd17648   204 ARLPHLKRVD----AAGEEFTAPVFEKLrsrfagLIINAYGPTETT-VTNHKRFFPG--DQRFDKSLGRPVRNTKCYVLN 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4176 SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPF-EPGE-------RMYRTGDLVRWLPDGNLEYLGRIDHQV 4247
Cdd:cd17648   277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqTEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQV 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4248 KIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN-----GQQQLVAYFVAQRE-LTAAELRATMSQELPNYMIPSYFVQL 4321
Cdd:cd17648   357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLVRL 436
                         490
                  ....*....|....*..
gi 386647928 4322 AQMPLTPNGKIDRKALP 4338
Cdd:cd17648   437 EGIPVTINGKLDVRALP 453
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
8034-8455 1.49e-134

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 431.76  E-value: 1.49e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8034 YPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEM-ANGEPVQRVYSDVEFAVEY 8112
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8113 ---SKADREEAVEIAQRFVR-----PFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYA----G 8180
Cdd:pfam00668   85 idiSDLSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQqllkG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8181 EELPPLRIQ-YKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELA 8259
Cdd:pfam00668  165 EPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8260 ARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAF 8339
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8340 EHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTVA----AQFDLTLSVAEDDGAIRGS 8415
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSVieeeAKYDLSLTASERGGGLTIK 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 386647928  8416 FQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQL 8455
Cdd:pfam00668  405 IDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDL 444
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
3868-4337 1.57e-133

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 429.77  E-value: 1.57e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQRHLRERVSFAGTFVAVDDeQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLcslklmfA 4027
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDL-DALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAA-------L 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4028 NTL-------QMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAYL- 4099
Cdd:cd12114   153 NTIldinrrfAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLl 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4100 -----NPDRMPSLKKLITGGSAASVEFVQQWKD---KVLYFNAYGPTEASIvTSIWDEASDSLGDRKSVPIGRPLANHRI 4171
Cdd:cd12114   233 dvleaAQALLPSLRLVLLSGDWIPLDLPARLRAlapDARLISLGGATEASI-WSIYHPIDEVPPDWRSIPYGRPLANQRY 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4172 YVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPfePGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRG 4251
Cdd:cd12114   312 RVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4252 YRIELGEVETQLAKIDAVQEAIVLAREDAnGQQQLVAYFVAQRE---LTAAELRATMSQELPNYMIPSYFVQLAQMPLTP 4328
Cdd:cd12114   390 YRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTA 468

                  ....*....
gi 386647928 4329 NGKIDRKAL 4337
Cdd:cd12114   469 NGKVDRAAL 477
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
7451-7928 2.07e-133

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 427.50  E-value: 2.07e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:cd17653     2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLLTQRhlqecvsfdgkviaaddeqaygedgsnlepvvGPNHLAYVIYTSGTTGKPKGVMVEHHG 7610
Cdd:cd17653    82 PSARIQAILRTSGATLLLTTD--------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7611 LCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYI--PAKDtildyplFESYMNEngITAAILPPTYA 7688
Cdd:cd17653   130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLadPSDP-------FAHVART--VDALMSTPSIL 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7689 IYLSPDRLPSLKKLITGGSAASVEFVQQWKDKVRYFNAYGPTEASIVTSVWAASPDgldlRSVPIGRPIANHQIFIVDSQ 7768
Cdd:cd17653   201 STLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPG----QPVTIGKPIPNSTCYILDAD 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7769 NHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELG 7848
Cdd:cd17653   277 LQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7849 EIEEQLLKIAS-VQETIVIARGDangqqQLCAyFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNA 7927
Cdd:cd17653   357 EIEEVVLQSQPeVTQAAAIVVNG-----RLVA-FVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKA 430

                  .
gi 386647928 7928 L 7928
Cdd:cd17653   431 L 431
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
854-1264 1.59e-132

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 424.91  E-value: 1.59e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  854 PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYP--EVEFAVEH 931
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPaaEARPDLTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IRANEEEADAAVKQFIRA-FDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEF-----ARLYGGE-DLPA 1004
Cdd:cd19540    83 VDVTEDELAARLAEAARRgFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLatayaARRAGRApDWAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1005 LRIQYKDYAVWQQ----SEAQKEQL-KRQEAYWLEVFRGeLP-VLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIA 1078
Cdd:cd19540   163 LPVQYADYALWQRellgDEDDPDSLaARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1079 SENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAF 1158
Cdd:cd19540   242 REHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1159 ERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEFRLPGLQLTPYPVEEHTSKFDLSLDIMESGD------GFLC 1232
Cdd:cd19540   322 AHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDadgapaGLTG 401
                         410       420       430
                  ....*....|....*....|....*....|..
gi 386647928 1233 GIEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19540   402 ELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
PRK05691 PRK05691
peptide synthase; Validated
191-837 6.45e-132

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 471.19  E-value: 6.45e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  191 DEVRLHLTYNGNLYTESFIAQAVDHLNRLFSVVLFQPDLALGQADLLSEAEKHQLLDAFNKTGTDYPRDTTIHRLFEEQA 270
Cdd:PRK05691 3651 DDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQV 3730
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  271 ERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIR 350
Cdd:PRK05691 3731 AAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQ 3810
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  351 YMLEDSGTQVL------LSQGH-LQERVSFSGTWIRLDDEEAYHEDGS--NLESVNGPEHLTYVIYTSGTTGKPKGNLTT 421
Cdd:PRK05691 3811 RIIELSRTPVLvcsaacREQARaLLDELGCANRPRLLVWEEVQAGEVAshNPGIYSGPDNLAYVIYTSGSTGLPKGVMVE 3890
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  422 HRNIIR-VVKNTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAF 500
Cdd:PRK05691 3891 QRGMLNnQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSL 3970
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  501 FNVLVDMNPDCLRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTA 580
Cdd:PRK05691 3971 IQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNR 4050
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  581 IYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPF-APGERMYRTGDLARWLPDGTIEYVGRIDDQVKI 659
Cdd:PRK05691 4051 LYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKI 4130
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  660 RGFRIELGEIEAHLLKLEAIEKATVVVRESANGeKQLCAYYVADRSLPA-----NEVRSTLSQELPAYMLPSYFVQLEQM 734
Cdd:PRK05691 4131 RGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLVPHQTVLAqgallERIKQRLRAELPDYMVPLHWLWLDRL 4209
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  735 PLTTNGKVDRRALPAPEESMETGVEFVEPRTELEAGIVNIWKEILKIEKISVKDSFFELGGHSLRATTMVSRLHKELNIS 814
Cdd:PRK05691 4210 PLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRN 4289
                         650       660
                  ....*....|....*....|...
gi 386647928  815 LPLRDVFRYPTVEKLAEAISGMG 837
Cdd:PRK05691 4290 VPLRAMFECSTVEELAEYIEGLA 4312
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
274-747 1.02e-131

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 424.38  E-value: 1.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQGHLQERVSFSGTWIRLDDeEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN 433
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDL-DALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  434 -YIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDC- 511
Cdd:cd12114   160 rRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAq 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  512 --LRHARAILFGGERVSVS---HVRKALGH-----LGpgkikhvyGPTESTVFATSYDVHEVEEGAVSIPIGGPISNTAI 581
Cdd:cd12114   240 alLPSLRLVLLSGDWIPLDlpaRLRALAPDarlisLG--------GATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRY 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  582 YIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPfaPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRG 661
Cdd:cd12114   312 RVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  662 FRIELGEIEAHLLKLEAIEKATVVVRESAnGEKQLCAYYVADRSLP---ANEVRSTLSQELPAYMLPSYFVQLEQMPLTT 738
Cdd:cd12114   390 YRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTpiaPDALRAFLAQTLPAYMIPSRVIALEALPLTA 468

                  ....*....
gi 386647928  739 NGKVDRRAL 747
Cdd:cd12114   469 NGKVDRAAL 477
PRK05691 PRK05691
peptide synthase; Validated
7455-8455 2.14e-131

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 469.26  E-value: 2.14e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7455 QAERMPEKAAVVF------ENTQLTYRELNERANRLARTLRAEGVQADQPVgLMIERSLEMIVGAFAIMKAGGAYVPIDP 7528
Cdd:PRK05691   18 RAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7529 -----EYPEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSN-------LEPVVGPNHLAYVIYTSG 7596
Cdd:PRK05691   97 pesarRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDpalaeawQEPALQPDDIAFLQYTSG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7597 TTGKPKGVMVEHHGLCSLKLMFAETLRIT--EEDRVVQFASLSFDAS-CWEIFKALFFGATLYIPAKDTILDYPL--FES 7671
Cdd:PRK05691  177 STALPKGVQVSHGNLVANEQLIRHGFGIDlnPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYFLERPLrwLEA 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7672 YMNENGITAAilPPTYAIYLSPDRLP--SLKKL--------ITGGSAASVEFVQQWKDKV--------RYFNAYGPTEAS 7733
Cdd:PRK05691  257 ISEYGGTISG--GPDFAYRLCSERVSesALERLdlsrwrvaYSGSEPIRQDSLERFAEKFaacgfdpdSFFASYGLAEAT 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7734 IVTS-------VWAASPDGLDL---RSVP--------IGRPIANHQIFIVDSQN-HMLPVGVAGELCISGAGLARGYLNR 7794
Cdd:PRK05691  335 LFVSggrrgqgIPALELDAEALarnRAEPgtgsvlmsCGRSQPGHAVLIVDPQSlEVLGDNRVGEIWASGPSIAHGYWRN 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7795 PELTAEKFVDnpfLAGERMYRTGDLArWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASV-------------- 7860
Cdd:PRK05691  415 PEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVvrkgrvaafavnhq 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7861 -QETIVIARGDANGQQQLcayfvadreLTVSELRGTLSQELPG--YMIPSYFVQLE--QMPLTPNGKIDRNA--LPAPEG 7933
Cdd:PRK05691  491 gEEGIGIAAEISRSVQKI---------LPPQALIKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKLQRSAcrLRLADG 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7934 SMQTGADF-----VEPRTP------VEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVNKELNVNLPLRDIF 8002
Cdd:PRK05691  562 SLDSYALFpalqaVEAAQTaasgdeLQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLF 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8003 RFPTVEALAQVIDGLEQE---EHSAIPVIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQ 8079
Cdd:PRK05691  642 EAPTLAAFSAAVARQLAGggaAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQR 721
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8080 LIERHETLRTGFEMANGEPVQRVYSDVEFAVEY------SKADREE-AVEIAQRFVR-PFDLRKPPLLRVGLIEVEPERH 8151
Cdd:PRK05691  722 LVERHESLRTRFYERDGVALQRIDAQGEFALQRidlsdlPEAEREArAAQIREEEARqPFDLEKGPLLRVTLVRLDDEEH 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8152 ILMLDMHHIISDGASVGILQEEFSRLYAGE------ELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIE 8225
Cdd:PRK05691  802 QLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLE 881
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8226 LPTDYERTSTRSFEGAELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPII 8305
Cdd:PRK05691  882 LATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLV 961
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8306 GMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASrnpVFDTMFvlqNTEDRGIEAdAFS 8385
Cdd:PRK05691  962 GFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG---LFQVMF---NHQQRDLSA-LRR 1034
                        1050      1060      1070      1080      1090      1100      1110
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 8386 LTPFVFDQ----TVAAQFDLTLSVAED-DGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQL 8455
Cdd:PRK05691 1035 LPGLLAEElpwhSREAKFDLQLHSEEDrNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQL 1109
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
4901-5385 2.81e-130

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 420.52  E-value: 2.81e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTQtHLQERAQQWGQTLQAalcLDDEAAYAEDASNVANVnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd12114    81 ADAGARLVLTD-GPDAQLDVAVFDVLI---LDLDALAAPAPPPPVDV-APDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 5140
Cdd:cd12114   156 LDINRRFAVGP-DDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5141 VAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTEAAIDSSLYdePLAKLPEA-GNVPIGKAALNAKF 5219
Cdd:cd12114   235 LEAAQALLPSLRLVLLSGDWIPLDLPARLRALA-PDARLISLGGATEASIWSIYH--PIDEVPPDwRSIPYGRPLANQRY 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5220 YIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPfvEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRG 5299
Cdd:cd12114   312 RVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5300 YRIETGEIETQLLKAEGVREAVVVVREDaKGQKVLCAHFTAESE---LKLSELRSSLSQELPGYMIPSYFVQLEQLPLTA 5376
Cdd:cd12114   390 YRIELGEIEAALQAHPGVARAVVVVLGD-PGGKRLAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTA 468

                  ....*....
gi 386647928 5377 NGKIDRKAL 5385
Cdd:cd12114   469 NGKVDRAAL 477
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1311-1795 4.77e-130

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 419.75  E-value: 4.77e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1311 PEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 1390
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1391 EDSAASVLLTQTHlqeraqqWGQTLQAVLC---LDDEAAYAEDASNVANVnEPHDLAYVIYTSGTTGRPKGVMIEHRSLV 1467
Cdd:cd12114    81 ADAGARLVLTDGP-------DAQLDVAVFDvliLDLDALAAPAPPPPVDV-APDDLAYVIFTSGSTGTPKGVMISHRAAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1468 NTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPF 1547
Cdd:cd12114   153 NTILDINRRFAVGP-DDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEML 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1548 MDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTEAAIDSSLYdePLAKLPEA-GNVPIGKAALN 1626
Cdd:cd12114   232 LDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALA-PDARLISLGGATEASIWSIYH--PIDEVPPDwRSIPYGRPLAN 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1627 AKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPfvEGERLYRTGDLARWMPDGNVDFIGRIDNQAK 1706
Cdd:cd12114   309 QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1707 IRGYRIETGEIETQLLKAEGVREAVVVVREDaKGQKVLCAYFTAESE---LKLSELRSSLSQELPGYMIPSYFVQLEQLP 1783
Cdd:cd12114   387 VRGYRIELGEIEAALQAHPGVARAVVVVLGD-PGGKRLAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALP 465
                         490
                  ....*....|..
gi 386647928 1784 LTANGKIDRKAL 1795
Cdd:cd12114   466 LTANGKVDRAAL 477
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1300-1795 6.57e-130

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 417.87  E-value: 6.57e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1300 HALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 1379
Cdd:cd12115     2 HDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1380 DYPSDRIQFMLEDSAASVLLTQthlqeraqqwgqtlqavlclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGV 1459
Cdd:cd12115    82 AYPPERLRFILEDAQARLVLTD--------------------------------------PDDLAYVIYTSGSTGRPKGV 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 MIEHRSLVNTAAGYRREYRLDQFpVRLLQLASFSFDVFVGDIARTLYNGGTMVICpkDDRIDPARLHywiSEEKITIFES 1539
Cdd:cd12115   124 AIEHRNAAAFLQWAAAAFSAEEL-AGVLASTSICFDLSVFELFGPLATGGKVVLA--DNVLALPDLP---AAAEVTLINT 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1540 TPALiipfMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYDEPLAKLpeaGNVP 1619
Cdd:cd12115   198 VPSA----AAELLRHDALPASVRVVNLAGEPLPRDLVQRLYARLQVE-RVVNLYGPSEDTTYSTVAPVPPGAS---GEVS 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1620 IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIG 1699
Cdd:cd12115   270 IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLG 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1700 RIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAE--SELKLSELRSSLSQELPGYMIPSYFV 1777
Cdd:cd12115   350 RADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLGTRLPAYMVPSRFV 429
                         490
                  ....*....|....*...
gi 386647928 1778 QLEQLPLTANGKIDRKAL 1795
Cdd:cd12115   430 RLDALPLTPNGKIDRSAL 447
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
7460-7929 1.90e-129

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 416.80  E-value: 1.90e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEG-VQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYM 7538
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7539 LEDSGAQVLLTqrhlqecvsfdgkviaaddeqaygedgsnlepvvGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMF 7618
Cdd:cd17648    81 LEDTGARVVIT----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7619 AET--LRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAIYLSPDRL 7696
Cdd:cd17648   127 SERyfGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLARL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7697 PSLKKLItggsAASVEFVQQWKDKVR------YFNAYGPTEASIVTSVWAASPDGLDLRSvpIGRPIANHQIFIVDSQNH 7770
Cdd:cd17648   207 PHLKRVD----AAGEEFTAPVFEKLRsrfaglIINAYGPTETTVTNHKRFFPGDQRFDKS--LGRPVRNTKCYVLNDAMK 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7771 MLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGE--------RMYRTGDLARWLPDGNIEYLGRIDHQVKIRG 7842
Cdd:cd17648   281 RVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRG 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7843 YRIELGEIEEQLLKIASVQETIVIARGDAN-----GQQQLCAYFVADRE-LTVSELRGTLSQELPGYMIPSYFVQLEQMP 7916
Cdd:cd17648   361 QRIEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLVRLEGIP 440
                         490
                  ....*....|...
gi 386647928 7917 LTPNGKIDRNALP 7929
Cdd:cd17648   441 VTINGKLDVRALP 453
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
5949-6421 2.28e-129

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 416.80  E-value: 2.28e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAG-VQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYM 6027
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6028 LEDSGAKLLlvqghlldrasfadklvnlnddgayhedgsnlepVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNT 6107
Cdd:cd17648    81 LEDTGARVV----------------------------------ITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6108 N--YVELNEQTH-ILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAplyNQLSQQDS 6184
Cdd:cd17648   127 SerYFGRDNGDEaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTP---SVLQQYDL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6185 GMFAGLKTLIVGGDVLSVPHINRVLREHAGLsIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLL 6264
Cdd:cd17648   204 ARLPHLKRVDAAGEEFTAPVFEKLRSRFAGL-IINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRV 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6265 PVGVWGELIVGGDGVARGYLNRPELTAEKFVESSF-LPGE-------RCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYR 6336
Cdd:cd17648   283 PVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqTEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQR 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6337 IELGEIEEQLLKVASVKEATVIVREDES-----GQKQLCAYFVAERE-LTIGELRAALSQELPNYMIPSHFVPLERMPLT 6410
Cdd:cd17648   363 IEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
                         490
                  ....*....|.
gi 386647928 6411 PNGKIDRRALP 6421
Cdd:cd17648   443 INGKLDVRALP 453
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1311-1796 3.25e-129

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 416.42  E-value: 3.25e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1311 PEVAAVVYENDRLTYRELNERANRLARMLRAQG-VKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFM 1389
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1390 LEDSAASVLLTqthlqeraqqwgqtlqavlclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNT 1469
Cdd:cd17648    81 LEDTGARVVIT--------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1470 AAGYRREYRL-DQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFm 1548
Cdd:cd17648   123 RTSLSERYFGrDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1549 DYVAehgldMSSMELLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAIDSSLYDEPLaklPEAGNVPIGKAALNAK 1628
Cdd:cd17648   202 DLAR-----LPHLKRVDAAGEEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNHKRFFPG---DQRFDKSLGRPVRNTK 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1629 FYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGE--------RLYRTGDLARWMPDGNVDFIGR 1700
Cdd:cd17648   272 CYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGR 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1701 IDNQAKIRGYRIETGEIETQLLKAEGVRE-----AVVVVREDAKGQKVLCAYFTAESE-LKLSELRSSLSQELPGYMIPS 1774
Cdd:cd17648   352 NDFQVKIRGQRIEPGEVEAALASYPGVREcavvaKEDASQAQSRIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPA 431
                         490       500
                  ....*....|....*....|..
gi 386647928 1775 YFVQLEQLPLTANGKIDRKALP 1796
Cdd:cd17648   432 RLVRLEGIPVTINGKLDVRALP 453
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
2359-2828 1.20e-128

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 415.52  E-value: 1.20e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQRRLQERVSFAGTVVTVDDeQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLcslkqmfA 2518
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDL-DALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAA-------L 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NTL-------QINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPT----------KETILDYQ---------WFERYM 2572
Cdd:cd12114   153 NTIldinrrfAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDearrrdpahwAELIERHGvtlwnsvpaLLEMLL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2573 SDNGITTATLPPTYAVYLNPDHMPdfkrliaagsassLELLQQWKDKVK---YFNAYGPTEDSIcTTIWTPSTEDISQLK 2649
Cdd:cd12114   233 DVLEAAQALLPSLRLVLLSGDWIP-------------LDLPARLRALAPdarLISLGGATEASI-WSIYHPIDEVPPDWR 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2650 SVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPfePGERMYRTGDLAKWLPDGTIE 2729
Cdd:cd12114   299 SIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLE 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2730 YLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDAsGQKQLCAYFVADR---TMTVGELRGELSGELPGYMIP 2806
Cdd:cd12114   377 FLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNdgtPIAPDALRAFLAQTLPAYMIP 455
                         490       500
                  ....*....|....*....|..
gi 386647928 2807 AHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd12114   456 SRVIALEALPLTANGKVDRAAL 477
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
2359-2829 1.41e-128

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 414.49  E-value: 1.41e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALG-VKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYM 2437
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2438 LEDSSAQVLLAqrrlqervsfagtvvtvddeqayagdgsnlesavGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMF 2517
Cdd:cd17648    81 LEDTGARVVIT----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2518 ANT--LQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAVYLNPDHM 2595
Cdd:cd17648   127 SERyfGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLARL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2596 PDFKRLIAAGSASSLELLQQWKDKVK--YFNAYGPTEDSICTTIwtpSTEDISQLKSVPIGGPIVNHRIYIVDAHYQPVP 2673
Cdd:cd17648   207 PHLKRVDAAGEEFTAPVFEKLRSRFAglIINAYGPTETTVTNHK---RFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVP 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2674 VGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGE-------RMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRI 2745
Cdd:cd17648   284 VGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqTEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRI 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2746 ELGEIEEQLLKVASVQEAIVIAHDDAS-----GQKQLCAYFVADR-TMTVGELRGELSGELPGYMIPAHFVQLERMPLTP 2819
Cdd:cd17648   364 EPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPgHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTI 443
                         490
                  ....*....|
gi 386647928 2820 NGKIDRKALP 2829
Cdd:cd17648   444 NGKLDVRALP 453
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
4901-5386 2.03e-128

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 414.10  E-value: 2.03e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQG-VKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFM 4979
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4980 LEDSAASVLLTqthlqeraqqwgqtlqaalclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNT 5059
Cdd:cd17648    81 LEDTGARVVIT--------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5060 AAGYRREYRL-DQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIPFm 5138
Cdd:cd17648   123 RTSLSERYFGrDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5139 DYVAehgLDMSSMVLLITSSDSCSVtdYRVLQERFGSqfRIINAYGVTEAAIDSSLYDEPLaklPEAGNVPIGKAALNAK 5218
Cdd:cd17648   202 DLAR---LPHLKRVDAAGEEFTAPV--FEKLRSRFAG--LIINAYGPTETTVTNHKRFFPG---DQRFDKSLGRPVRNTK 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5219 FYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGE--------RLYRTGDLARWMPDGNVDFIGR 5290
Cdd:cd17648   272 CYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGR 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5291 IDNQAKIRGYRIETGEIETQLLKAEGVRE-----AVVVVREDAKGQKVLCAHFTAESE-LKLSELRSSLSQELPGYMIPS 5364
Cdd:cd17648   352 NDFQVKIRGQRIEPGEVEAALASYPGVREcavvaKEDASQAQSRIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPA 431
                         490       500
                  ....*....|....*....|..
gi 386647928 5365 YFVQLEQLPLTANGKIDRKALP 5386
Cdd:cd17648   432 RLVRLEGIPVTINGKLDVRALP 453
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
4890-5385 2.79e-128

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 413.25  E-value: 2.79e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4890 HALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 4969
Cdd:cd12115     2 HDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4970 DYPSDRIQFMLEDSAASVLLTQthlqeraqqwgqtlqaalclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGV 5049
Cdd:cd12115    82 AYPPERLRFILEDAQARLVLTD--------------------------------------PDDLAYVIYTSGSTGRPKGV 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5050 MIEHRSLVNTAAGYRREYRLDQFpVRLLQLASFSFDVFVGDIARTLYNGGTMVICpkDDRIDPARLHywiSEEKITIFES 5129
Cdd:cd12115   124 AIEHRNAAAFLQWAAAAFSAEEL-AGVLASTSICFDLSVFELFGPLATGGKVVLA--DNVLALPDLP---AAAEVTLINT 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5130 TPALiipfMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYDEPLAKLpeaGNVP 5209
Cdd:cd12115   198 VPSA----AAELLRHDALPASVRVVNLAGEPLPRDLVQRLYARLQVE-RVVNLYGPSEDTTYSTVAPVPPGAS---GEVS 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5210 IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIG 5289
Cdd:cd12115   270 IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLG 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5290 RIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAE--SELKLSELRSSLSQELPGYMIPSYFV 5367
Cdd:cd12115   350 RADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLGTRLPAYMVPSRFV 429
                         490
                  ....*....|....*...
gi 386647928 5368 QLEQLPLTANGKIDRKAL 5385
Cdd:cd12115   430 RLDALPLTPNGKIDRSAL 447
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
7460-7928 2.97e-128

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 414.36  E-value: 2.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLTQRHL-QECVSFDGKVIAADDEQAYGEDgsNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMF 7618
Cdd:cd12114    81 ADAGARLVLTDGPDaQLDVAVFDVLILDLDALAAPAP--PPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7619 AETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITA-----AILPPTYAIYLSP 7693
Cdd:cd12114   159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLwnsvpALLEMLLDVLEAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7694 -DRLPSLKKLITGGSAASVEFVQQWKD---KVRYFNAYGPTEASIVTSVWAASPDGLDLRSVPIGRPIANHQIFIVDSQN 7769
Cdd:cd12114   239 qALLPSLRLVLLSGDWIPLDLPARLRAlapDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPRG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7770 HMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPflAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGE 7849
Cdd:cd12114   319 RDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGE 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7850 IEEQLLKIASVQETIVIARGDAnGQQQLCAYFVADRELTV---SELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRN 7926
Cdd:cd12114   397 IEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPiapDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475

                  ..
gi 386647928 7927 AL 7928
Cdd:cd12114   476 AL 477
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
4444-4854 5.11e-128

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 411.82  E-value: 5.11e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4444 PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYP--EVDFAVET 4521
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPaaEARPDLTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4522 VQASEQEAKAIVRDFI-RPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYS----GEElPG-- 4594
Cdd:cd19540    83 VDVTEDELAARLAEAArRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAarraGRA-PDwa 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4595 -LRIQYKDYAVWQQ----SEAQKEQL-KRQEAYWLEAFRGeLP-VLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRI 4667
Cdd:cd19540   162 pLPVQYADYALWQRellgDEDDPDSLaARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4668 AAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGA 4747
Cdd:cd19540   241 AREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4748 FEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEMHLPGLHLTPYPTEYGMSKFDLSLDMME------DSEGLE 4821
Cdd:cd19540   321 FAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGLT 400
                         410       420       430
                  ....*....|....*....|....*....|...
gi 386647928 4822 CSLEFATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19540   401 GELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
264-747 1.09e-126

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 408.24  E-value: 1.09e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  264 RLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPE 343
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  344 YPEERIRYMLEDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvNGPEHLTYVIYTSGTTGKPKGNLTTHR 423
Cdd:cd17653    81 LPSARIQAILRTSGATLLLTT--------------------------------DSPDDLAYIIFTSGSTGIPKGVMVPHR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  424 NIIRVVKNTNY-IDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLV-PKETVLDVAKlagliekqQISVMFITTAFF 501
Cdd:cd17653   129 GVLNYVSQPPArLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAdPSDPFAHVAR--------TVDALMSTPSIL 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  502 NVLvdmNPDCLRHARAILFGGERVSVSHVRkalgHLGPGK-IKHVYGPTESTVFATsydVHEVEEGaVSIPIGGPISNTA 580
Cdd:cd17653   201 STL---SPQDFPNLKTIFLGGEAVPPSLLD----RWSPGRrLYNAYGPTECTISST---MTELLPG-QPVTIGKPIPNST 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  581 IYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIR 660
Cdd:cd17653   270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  661 GFRIELGEIEAHLLKLEA-IEKATVVVRESangekQLCAyYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTN 739
Cdd:cd17653   350 GFRINLEEIEEVVLQSQPeVTQAAAIVVNG-----RLVA-FVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTAN 423

                  ....*...
gi 386647928  740 GKVDRRAL 747
Cdd:cd17653   424 GKVDRKAL 431
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
274-748 1.70e-126

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 408.33  E-value: 1.70e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAG-VQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYM 352
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  353 LEDSGTQVLLSqghlqervsfsgtwirlddeeayhedgsnlesvnGPEHLTYVIYTSGTTGKPKGNLTTHR---NIIRVV 429
Cdd:cd17648    81 LEDTGARVVIT----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGsvvNLRTSL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  430 KNTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAffnVLVDMNP 509
Cdd:cd17648   127 SERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPS---VLQQYDL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  510 DCLRHARAILFGGERVSVSHVRKALGHLgPGKIKHVYGPTESTVFATsydVHEVEEGA-VSIPIGGPISNTAIYIVNAQN 588
Cdd:cd17648   204 ARLPHLKRVDAAGEEFTAPVFEKLRSRF-AGLIINAYGPTETTVTNH---KRFFPGDQrFDKSLGRPVRNTKCYVLNDAM 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  589 KLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFA-PGE-------RMYRTGDLARWLPDGTIEYVGRIDDQVKIR 660
Cdd:cd17648   280 KRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQtEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIR 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  661 GFRIELGEIEAHLLKLEAIEKATVVVRESAN-----GEKQLCAYYVADR-SLPANEVRSTLSQELPAYMLPSYFVQLEQM 734
Cdd:cd17648   360 GQRIEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPgHVPESDLLSFLRAKLPRYMVPARLVRLEGI 439
                         490
                  ....*....|....
gi 386647928  735 PLTTNGKVDRRALP 748
Cdd:cd17648   440 PVTINGKLDVRALP 453
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1902-2312 6.64e-126

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 406.04  E-value: 6.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1902 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRV--YKEVNFAVEH 1979
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1980 YRTSEAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLY----NGE--SLAT 2052
Cdd:cd19540    83 VDVTEDELAARLAEAARRgFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRapDWAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2053 LRIQYKDYAVWQQ----SEEQLE-RVKRQEAYWLDMFRGeLP-VLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVA 2126
Cdd:cd19540   163 LPVQYADYALWQRellgDEDDPDsLAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2127 AESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAY 2206
Cdd:cd19540   242 REHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2207 EHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEELQLDGLKLAPYPSGNTIARFDLTLDVTE------TGSGLEC 2280
Cdd:cd19540   322 AHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGLTG 401
                         410       420       430
                  ....*....|....*....|....*....|..
gi 386647928 2281 NLEYATSLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19540   402 ELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
5939-6420 8.65e-126

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 405.54  E-value: 8.65e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5939 QLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPD 6018
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6019 YPEDRIRYMLEDSGAKLLLvqghlldrasfadklvnlnddgayhedgsnlePVNGPEHLTYVIYTSGTTGRPKGVMVEHR 6098
Cdd:cd17653    81 LPSARIQAILRTSGATLLL--------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMVPHR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6099 NVVRLVKNTNYvELNEQTH--ILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKnaiqqygINTMWLTAPLY 6176
Cdd:cd17653   129 GVLNYVSQPPA-RLDVGPGsrVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVART-------VDALMSTPSIL 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6177 NQLSQQDsgmFAGLKTLIVGGDVLSVPHINRVLrehAGLSIVNGYGPTEnTTFSTTHTIVgEQKEAVPIGKPINNSTAYI 6256
Cdd:cd17653   201 STLSPQD---FPNLKTIFLGGEAVPPSLLDRWS---PGRRLYNAYGPTE-CTISSTMTEL-LPGQPVTIGKPIPNSTCYI 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6257 VDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYR 6336
Cdd:cd17653   273 LDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFR 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6337 IELGEIEEQLLKVAS-VKEATVIVREDesgqkQLCAyFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:cd17653   353 INLEEIEEVVLQSQPeVTQAAAIVVNG-----RLVA-FVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426

                  ....*
gi 386647928 6416 DRRAL 6420
Cdd:cd17653   427 DRKAL 431
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
5492-5902 1.51e-125

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 404.88  E-value: 1.51e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5492 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRV--YKEVNFAVEH 5569
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5570 YRTSEAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMY----NGE--SLAP 5642
Cdd:cd19540    83 VDVTEDELAARLAEAARRgFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRapDWAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5643 LRIQYKDYATWQQ----SEAQQEQ-MKRQEAYWLDMFRGeLP-VLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIA 5716
Cdd:cd19540   163 LPVQYADYALWQRellgDEDDPDSlAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5717 AESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAY 5796
Cdd:cd19540   242 REHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5797 EHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGELQLDGLRLTPYPAEHTVAKFDLSVDVTE------GSEGLEL 5870
Cdd:cd19540   322 AHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGLTG 401
                         410       420       430
                  ....*....|....*....|....*....|..
gi 386647928 5871 SMEYSTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19540   402 ELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
3394-3840 2.13e-125

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 405.18  E-value: 2.13e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3394 IENIYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGWRGEPLQIVYRYKPV 3473
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3474 EFAYEDLRHLAEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEA 3553
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3554 YLRNDLSERPAAPSYSHYIEW----LEKQDMEAAARYWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERM 3629
Cdd:pfam00668  161 LLKGEPLPLPPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3630 SRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEiaGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQE 3709
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3710 AALESGGYDYYPLYEIQAQSAQKQD-----LITHIMAFENFPMDEQIEQAGSYEDGKLAITDVDIaEQTNYDFTLVVMP- 3783
Cdd:pfam00668  319 DLLSAEPHQGYPFGDLVNDLRLPRDlsrhpLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSVIE-EEAKYDLSLTASEr 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  3784 GEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAEII 3840
Cdd:pfam00668  398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
5949-6420 5.15e-125

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 405.12  E-value: 5.15e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQGHLLDRASFADKLVNLNDDGAYHEDGSNLEPVNgPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTN 6108
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVA-PDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6109 -YVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGInTMWLTAPLYNQL----SQQD 6183
Cdd:cd12114   160 rRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGV-TLWNSVPALLEMlldvLEAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6184 SGMFAGLKTLIVGGD--VLSVPHINRVLREHAGLsIVNGyGPTENTTFSTTHTIvGEQKEA---VPIGKPINNSTAYIVD 6258
Cdd:cd12114   239 QALLPSLRLVLLSGDwiPLDLPARLRALAPDARL-ISLG-GATEASIWSIYHPI-DEVPPDwrsIPYGRPLANQRYRVLD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6259 SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSflPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIE 6338
Cdd:cd12114   316 PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIE 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6339 LGEIEEQLLKVASVKEATVIVReDESGQKQLCAYFVAERE---LTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:cd12114   394 LGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472

                  ....*
gi 386647928 6416 DRRAL 6420
Cdd:cd12114   473 DRAAL 477
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1300-1795 6.35e-124

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 402.31  E-value: 6.35e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1300 HALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 1379
Cdd:cd05918     2 HDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1380 DYPSDRIQFMLEDSAASVLLTQThlqeraqqwgqtlqavlclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGV 1459
Cdd:cd05918    82 SHPLQRLQEILQDTGAKVVLTSS-------------------------------------PSDAAYVIFTSGSTGKPKGV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 MIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDpaRLHYWISEEKITIFES 1539
Cdd:cd05918   125 VIEHRALSTSALAHGRALGLTS-ESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1540 TP---ALIIPfmdyvaehgLDMSSMELLITSSDSCSVTDyrvlQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKlpEAG 1616
Cdd:cd05918   202 TPsvaRLLDP---------EDVPSLRTLVLGGEALTQSD----VDTWADRVRLINAYGPAECTIAATVSPVVPST--DPR 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1617 NvpIGKaALNAKFYIVDA--HLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSP-------FVEGERLYRTGDLA 1687
Cdd:cd05918   267 N--IGR-PLGATCWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLV 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1688 RWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVV---VVREDAKGQKVLCAYFTAESELK--------- 1755
Cdd:cd05918   344 RYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslf 423
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 1756 ----------LSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05918   424 lepsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
7448-7930 1.78e-123

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 399.57  E-value: 1.78e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7448 IHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPID 7527
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7528 PEYPEDRIRYMLEDSGAQVLLTqrhlqecvsfdgkviaaddeqaygedgsnlepvvgpnhlAYVIYTSGTTGKPKGVMVE 7607
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7608 HHGLCSLKLMFAETLRITEEDRVVQFASLSFDAS-CWEIFKALFFGATLYIPAKdtiLDYPLFESYMNENGITAAILPPT 7686
Cdd:COG0318   122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPT 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7687 YAIYL------SPDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEASIVTSVWAAspDGLDLRSVPIGRPIA 7758
Cdd:COG0318   199 MLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEERfgVRIVEGYGLTETSPVVTVNPE--DPGERRPGSVGRPLP 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7759 NHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDnpflageRMYRTGDLARWLPDGNIEYLGRIDHQV 7838
Cdd:COG0318   277 GVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDMI 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7839 KIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMP 7916
Cdd:COG0318   350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrPGAELDAEELRAFLRERLARYKVPRRVEFVDELP 429
                         490
                  ....*....|....
gi 386647928 7917 LTPNGKIDRNALPA 7930
Cdd:COG0318   430 RTASGKIDRRALRE 443
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
4890-5385 7.24e-123

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 399.22  E-value: 7.24e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4890 HALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 4969
Cdd:cd05918     2 HDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4970 DYPSDRIQFMLEDSAASVLLTQThlqeraqqwgqtlqaalclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGV 5049
Cdd:cd05918    82 SHPLQRLQEILQDTGAKVVLTSS-------------------------------------PSDAAYVIFTSGSTGKPKGV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5050 MIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDpaRLHYWISEEKITIFES 5129
Cdd:cd05918   125 VIEHRALSTSALAHGRALGLTS-ESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5130 TP---ALIIPfmdyvaehgLDMSSMVLLITSSDSCSVTDyrvlQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKlpEAG 5206
Cdd:cd05918   202 TPsvaRLLDP---------EDVPSLRTLVLGGEALTQSD----VDTWADRVRLINAYGPAECTIAATVSPVVPST--DPR 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5207 NvpIGKaALNAKFYIVDA--HLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSP-------FVEGERLYRTGDLA 5277
Cdd:cd05918   267 N--IGR-PLGATCWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLV 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5278 RWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVV---VVREDAKGQKVLCAHFTAESELK--------- 5345
Cdd:cd05918   344 RYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslf 423
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 5346 ----------LSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05918   424 lepsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1302-1795 1.24e-122

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 396.68  E-value: 1.24e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1302 LFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 1381
Cdd:cd17653     2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1382 PSDRIQFMLEDSAASVLLTQthlqeraqqwgqtlqavlclddeaayaedasnvanvNEPHDLAYVIYTSGTTGRPKGVMI 1461
Cdd:cd17653    82 PSARIQAILRTSGATLLLTT------------------------------------DSPDDLAYIIFTSGSTGIPKGVMV 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1462 EHRSLVNTAAgyRREYRLDQFP-VRLLQLASFSFDVFVGDIARTLYNGGTMVIC-PKDDRIDPARlhywiseeKITIFES 1539
Cdd:cd17653   126 PHRGVLNYVS--QPPARLDVGPgSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAdPSDPFAHVAR--------TVDALMS 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1540 TPALI--IPFMDYvaehgldmSSMELLITSSDSCSvtdyRVLQERFGSQFRIINAYGVTEAAIdSSLYDEPLAKLPeagn 1617
Cdd:cd17653   196 TPSILstLSPQDF--------PNLKTIFLGGEAVP----PSLLDRWSPGRRLYNAYGPTECTI-SSTMTELLPGQP---- 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1618 VPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDF 1697
Cdd:cd17653   259 VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEF 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1698 IGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREdakgQKVLCAYFTAESeLKLSELRSSLSQELPGYMIPSYFV 1777
Cdd:cd17653   339 LGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVV----NGRLVAFVTPET-VDVDGLRSELAKHLPSYAVPDRII 413
                         490
                  ....*....|....*...
gi 386647928 1778 QLEQLPLTANGKIDRKAL 1795
Cdd:cd17653   414 ALDSFPLTANGKVDRKAL 431
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
3856-4339 3.69e-122

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 396.10  E-value: 3.69e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3856 IHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPID 3935
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3936 PEYPEDRIRYMLEDSGAQALLTqrhlrervsfagtfvavddeqayhadgsnlepvvgpnhlAYVIYTSGTTGKPKGVMVE 4015
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4016 HHGLCSLKLMFANTLQMTEQDRVVQFASLSFDAS-CWEIFKALFFGATLYIPTSttiLDYPLFESYMNENGITATILPPT 4094
Cdd:COG0318   122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPT 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4095 YAAYL------NPDRMPSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTSIwdeASDSLGDRKSVPIGRPL 4166
Cdd:COG0318   199 MLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEERfgVRIVEGYGLTETSPVVTV---NPEDPGERRPGSVGRPL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4167 ANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDnpfepgeRMYRTGDLVRWLPDGNLEYLGRIDHQ 4246
Cdd:COG0318   276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDM 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4247 VKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQM 4324
Cdd:COG0318   349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
                         490
                  ....*....|....*
gi 386647928 4325 PLTPNGKIDRKALPA 4339
Cdd:COG0318   429 PRTASGKIDRRALRE 443
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
2355-2828 2.00e-121

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 393.54  E-value: 2.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRI 2434
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 SYMLEDSSAQVLLAQrrlqervsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLK 2514
Cdd:cd05945    81 REILDAAKPALLIAD----------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2515 QMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAVY----- 2589
Cdd:cd05945   127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMcllsp 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2590 -LNPDHMPDFKRLIAAGSASSLELLQQWKD---KVKYFNAYGPTEDSI-CTTI-WTPstEDISQLKSVPIGGPIVNHRIY 2663
Cdd:cd05945   207 tFTPESLPSLRHFLFCGEVLPHKTARALQQrfpDARIYNTYGPTEATVaVTYIeVTP--EVLDGYDRLPIGYAKPGAKLV 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2664 IVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVdnpFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGY 2743
Cdd:cd05945   285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2744 RIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV----ADRTMTVgELRGELSGELPGYMIPAHFVQLERMPLTP 2819
Cdd:cd05945   362 RIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpkpgAEAGLTK-AIKAELAERLPPYMIPRRFVYLDELPLNA 440

                  ....*....
gi 386647928 2820 NGKIDRKAL 2828
Cdd:cd05945   441 NGKIDRKAL 449
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
4892-5385 3.89e-121

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 392.06  E-value: 3.89e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4892 LFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 4971
Cdd:cd17653     2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4972 PSDRIQFMLEDSAASVLLTQthlqeraqqwgqtlqaalclddeaayaedasnvanvNEPHDLAYVIYTSGTTGRPKGVMI 5051
Cdd:cd17653    82 PSARIQAILRTSGATLLLTT------------------------------------DSPDDLAYIIFTSGSTGIPKGVMV 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5052 EHRSLVNTAAgyRREYRLDQFP-VRLLQLASFSFDVFVGDIARTLYNGGTMVIC-PKDDRIDPARlhywiseeKITIFES 5129
Cdd:cd17653   126 PHRGVLNYVS--QPPARLDVGPgSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAdPSDPFAHVAR--------TVDALMS 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5130 TPALI--IPFMDYvaehgldmSSMVLLITSSDSCSvtdyRVLQERFGSQFRIINAYGVTEAAIdSSLYDEPLAKLPeagn 5207
Cdd:cd17653   196 TPSILstLSPQDF--------PNLKTIFLGGEAVP----PSLLDRWSPGRRLYNAYGPTECTI-SSTMTELLPGQP---- 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5208 VPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDF 5287
Cdd:cd17653   259 VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEF 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5288 IGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREdakgQKVLCAHFTAESeLKLSELRSSLSQELPGYMIPSYFV 5367
Cdd:cd17653   339 LGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVV----NGRLVAFVTPET-VDVDGLRSELAKHLPSYAVPDRII 413
                         490
                  ....*....|....*...
gi 386647928 5368 QLEQLPLTANGKIDRKAL 5385
Cdd:cd17653   414 ALDSFPLTANGKVDRKAL 431
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
270-747 1.96e-120

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 390.84  E-value: 1.96e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERI 349
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  350 RYMLEDSGTQVLLSQGhlqervsfsgtwirlDDeeayhedgsnlesvngpehLTYVIYTSGTTGKPKGNLTTHRNIIRVV 429
Cdd:cd05945    81 REILDAAKPALLIADG---------------DD-------------------NAYIIFTSGSTGRPKGVQISHDNLVSFT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  430 K-NTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLV--- 505
Cdd:cd05945   127 NwMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLlsp 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  506 DMNPDCLRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDV-HEVEEGAVSIPIGGPISNTAIYIV 584
Cdd:cd05945   207 TFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVtPEVLDGYDRLPIGYAKPGAKLVIL 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  585 NAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPfapGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRI 664
Cdd:cd05945   287 DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  665 ELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPA---NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGK 741
Cdd:cd05945   364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAgltKAIKAELAERLPPYMIPRRFVYLDELPLNANGK 443

                  ....*.
gi 386647928  742 VDRRAL 747
Cdd:cd05945   444 IDRKAL 449
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
2347-2839 3.72e-120

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 390.33  E-value: 3.72e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2347 IHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPID 2426
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2427 PEYPEDRISYMLEDSSAQVLLAqrrlqervsfagtvvtvddeqayagdgsnlesavgpndlAYIIYTSGTTGKPKGVMVE 2506
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2507 HHGLCSLKQMFANTLQINAQDRVVQFASLSFDAS-CWEVFQTLFFGATLYIPTKetiLDYQWFERYMSDNGITTATLPPT 2585
Cdd:COG0318   122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPT 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2586 YAVYL------NPDHMPDFKRLIAAGSASSLELLQQWKDK--VKYFNAYGPTEDSICTTIwtpSTEDISQLKSVPIGGPI 2657
Cdd:COG0318   199 MLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEERfgVRIVEGYGLTETSPVVTV---NPEDPGERRPGSVGRPL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2658 VNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfepgeRMYRTGDLAKWLPDGTIEYLGRIDHQ 2737
Cdd:COG0318   276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDM 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2738 VKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGELPGYMIPAHFVQLERM 2815
Cdd:COG0318   349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
                         490       500
                  ....*....|....*....|....
gi 386647928 2816 PLTPNGKIDRKALPAPQGNASAGA 2839
Cdd:COG0318   429 PRTASGKIDRRALRERYAAGALEA 452
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
854-1264 1.97e-119

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 387.39  E-value: 1.97e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  854 PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAV--EH 931
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPklEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IRANEEEADAAVKQFIR-AFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY----GGE--DLPA 1004
Cdd:cd19538    83 KEVDEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYrarcKGEapELAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1005 LRIQYKDYAVWQQSEAQKE-----QLKRQEAYWLEVFRGeLPV-LEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIA 1078
Cdd:cd19538   163 LPVQYADYALWQQELLGDEsdpdsLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1079 SENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAF 1158
Cdd:cd19538   242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1159 ERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEFRLPGLQLTPYPVEEHTSKFDLSLDIME-----SGDGFLCG 1233
Cdd:cd19538   322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREqyndgTPNGIEGF 401
                         410       420       430
                  ....*....|....*....|....*....|.
gi 386647928 1234 IEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19538   402 IEYRTDLFDHETIEALAQRYLLLLESAVENP 432
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
8035-8446 2.09e-119

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 387.16  E-value: 2.09e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8035 PVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRV--YSDVEFAVEY 8112
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 SKADREEAVEIAQRFV-RPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLY----AGEE--LPP 8185
Cdd:cd19540    83 VDVTEDELAARLAEAArRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRApdWAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8186 LRIQYKDYAAWQR----SEA-YAKRVKQQEGYWLQTLAGeLP-VIELPTDYERTSTRSFEGAELEFEADEALTQRLNELA 8259
Cdd:cd19540   163 LPVQYADYALWQRellgDEDdPDSLAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8260 ARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAF 8339
Cdd:cd19540   242 REHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8340 EHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDqTVAAQFDLTLSVAE------DDGAIR 8413
Cdd:cd19540   322 AHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVD-TGVAKFDLSFTLTErrdadgAPAGLT 400
                         410       420       430
                  ....*....|....*....|....*....|...
gi 386647928 8414 GSFQYAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19540   401 GELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
8035-8446 2.87e-119

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 386.62  E-value: 2.87e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8035 PVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY-- 8112
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLei 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 SKADREE-AVEIAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGE------ELPP 8185
Cdd:cd19538    83 KEVDEEElESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8186 LRIQYKDYAAWQRS-----EAYAKRVKQQEGYWLQTLAGeLPV-IELPTDYERTSTRSFEGAELEFEADEALTQRLNELA 8259
Cdd:cd19538   163 LPVQYADYALWQQEllgdeSDPDSLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8260 ARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAF 8339
Cdd:cd19538   242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8340 EHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSlTPFVFDQTVAAQFDLTLSVAED-----DGAIRG 8414
Cdd:cd19538   322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLE-AKLELRTVGSAKFDLTFELREQyndgtPNGIEG 400
                         410       420       430
                  ....*....|....*....|....*....|..
gi 386647928 8415 SFQYAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19538   401 FIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
AMP-binding pfam00501
AMP-binding enzyme;
1303-1708 4.16e-118

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 382.82  E-value: 4.16e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1303 FEKQAERTPE-VAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 1381
Cdd:pfam00501    1 LERQAARTPDkTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1382 PSDRIQFMLEDSAASVLLTQTHLQ----ERAQQWGQTLQAVLCLDDEAAYAEDASN-----------VANVNEPHDLAYV 1446
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleelLEALGKLEVVKLVLVLDRDPVLKEEPLPeeakpadvpppPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1447 IYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPV---RLLQLASFSFDV-FVGDIARTLYNGGTMVICPKDDRIDP 1522
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpddRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1523 ARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDS 1602
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA--LVNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1603 SLYDEPLAKLPEAGnvPIGKAALNAKFYIVD-AHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegERLY 1681
Cdd:pfam00501  319 TTPLPLDEDLRSLG--SVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWY 390
                          410       420
                   ....*....|....*....|....*..
gi 386647928  1682 RTGDLARWMPDGNVDFIGRIDNQAKIR 1708
Cdd:pfam00501  391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
266-660 6.06e-118

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 382.43  E-value: 6.06e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   266 FEEQAERRPDAVAV-TFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEY 344
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   345 PEERIRYMLEDSGTQVLLSQGHLQ--------ERVSFSGTWIRLDDEEAYHEDGSNLESV-----------NGPEHLTYV 405
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleellealGKLEVVKLVLVLDRDPVLKEEPLPEEAKpadvpppppppPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   406 IYTSGTTGKPKGNLTTHRNIIRVVKNTNYID-----VTGQDKLLQLSSYSFDGS-TFDIFGALLNGAKLVLVPKETVLDV 479
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfgLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   480 AKLAGLIEKQQISVMFITTAFFNVLVDM---NPDCLRHARAILFGGERVSVSHVRKALGHLGPGkIKHVYGPTESTVFAT 556
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAgapKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   557 sYDVHEVEEGAVSIPIGGPISNTAIYIVNAQ-NKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADnpfapgERMYRT 635
Cdd:pfam00501  320 -TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 386647928   636 GDLARWLPDGTIEYVGRIDDQVKIR 660
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
7452-7841 7.86e-118

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 382.05  E-value: 7.86e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7452 FEEQAERMPEKAAV-VFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7531 PEDRIRYMLEDSGAQVLLTQRH--LQECVSFDGK--------VIAADDEQAYGEDGSNLE---------PVVGPNHLAYV 7591
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDAlkLEELLEALGKlevvklvlVLDRDPVLKEEPLPEEAKpadvpppppPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7592 IYTSGTTGKPKGVMVEHHGL----CSLKLMFAETLRITEEDRVVQFASLSFDAS-CWEIFKALFFGATLYIPAKDTILDY 7666
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7667 PLFESYMNENGITAAILPPTYAIYL------SPDRLPSLKKLITGGSAASVEFVQQWKDKVR--YFNAYGPTEASIVTSV 7738
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRELFGgaLVNGYGLTETTGVVTT 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7739 WAasPDGLDLRSVP-IGRPIANHQIFIVD-SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDnpflagERMYRT 7816
Cdd:pfam00501  321 PL--PLDEDLRSLGsVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 386647928  7817 GDLARWLPDGNIEYLGRIDHQVKIR 7841
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
5941-6333 1.37e-117

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 381.28  E-value: 1.37e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5941 FEEQAERIPDHLAV-TFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDY 6019
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6020 PEDRIRYMLEDSGAKLLLVQGHL--------------------LDRASFADKLVNLNDDGAYHEDGSNLEPVNgPEHLTY 6079
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellealgklevvklvlvLDRDPVLKEEPLPEEAKPADVPPPPPPPPD-PDDLAY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6080 VIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVE-----LNEQTHILQTGAVVFDAS-TFEIWGALLNGGRLYVVRNETILD 6153
Cdd:pfam00501  160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfgLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALD 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6154 AVSLKNAIQQYGINTMWLTAPLYNQLSQQDSG---MFAGLKTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTENTTFS 6230
Cdd:pfam00501  240 PAALLELIERYKVTVLYGVPTLLNMLLEAGAPkraLLSSLRLVLSGGAPLPPELARR-FRELFGGALVNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6231 TTHTIVGEQKEAVP-IGKPINNSTAYIVD-SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVEssflpgERCYRT 6308
Cdd:pfam00501  319 TTPLPLDEDLRSLGsVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 386647928  6309 GDLARWLPDGTLEYKGRIDEQVKIR 6333
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
3864-4337 3.40e-117

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 381.59  E-value: 3.40e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRI 3943
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 RYMLEDSGAQALltqrhlrervsfagtFVAVDDeqayhadgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLK 4023
Cdd:cd05945    81 REILDAAKPALL---------------IADGDD-------------------NAYIIFTSGSTGRPKGVQISHDNLVSFT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4024 LMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAY----- 4098
Cdd:cd05945   127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMcllsp 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4099 -LNPDRMPSLKKLITGGSAASVEFVQQWKD---KVLYFNAYGPTEASI-VTSI-WDEasDSLGDRKSVPIGRPLANHRIY 4172
Cdd:cd05945   207 tFTPESLPSLRHFLFCGEVLPHKTARALQQrfpDARIYNTYGPTEATVaVTYIeVTP--EVLDGYDRLPIGYAKPGAKLV 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4173 VVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVdnpFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGY 4252
Cdd:cd05945   285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4253 RIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAA---ELRATMSQELPNYMIPSYFVQLAQMPLTPN 4329
Cdd:cd05945   362 RIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYMIPRRFVYLDELPLNAN 441

                  ....*...
gi 386647928 4330 GKIDRKAL 4337
Cdd:cd05945   442 GKIDRKAL 449
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
4444-4854 6.82e-116

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 376.99  E-value: 6.82e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4444 PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAV--ET 4521
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPklEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4522 VQASEQEAKAIVRDFIR-PFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGE------ELPG 4594
Cdd:cd19538    83 KEVDEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4595 LRIQYKDYAVWQQSEAQKE-----QLKRQEAYWLEAFRGeLPV-LEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIA 4668
Cdd:cd19538   163 LPVQYADYALWQQELLGDEsdpdsLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4669 AESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAF 4748
Cdd:cd19538   242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4749 EHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEMHLPGLHLTPYPTEYGMSKFDLSLDMMEDSE-----GLECS 4823
Cdd:cd19538   322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREQYNdgtpnGIEGF 401
                         410       420       430
                  ....*....|....*....|....*....|.
gi 386647928 4824 LEFATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19538   402 IEYRTDLFDHETIEALAQRYLLLLESAVENP 432
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
5945-6420 1.02e-115

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 377.36  E-value: 1.02e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGhlldrasfadklvnlnDDGAYhedgsnlepvngpehltyVIYTSGTTGRPKGVMVEHRNVVRLV 6104
Cdd:cd05945    81 REILDAAKPALLIADG----------------DDNAY------------------IIFTSGSTGRPKGVQISHDNLVSFT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6105 K-NTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTmWLTAPLYNQLSQQD 6183
Cdd:cd05945   127 NwMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITV-WVSTPSFAAMCLLS 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6184 ----SGMFAGLKTLIVGGDVLSVPHInRVLREHA-GLSIVNGYGPTENTTFSTTHTIVGEQKEA---VPIGKPINNSTAY 6255
Cdd:cd05945   206 ptftPESLPSLRHFLFCGEVLPHKTA-RALQQRFpDARIYNTYGPTEATVAVTYIEVTPEVLDGydrLPIGYAKPGAKLV 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6256 IVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVessFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGY 6335
Cdd:cd05945   285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6336 RIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFV----AERELTIgELRAALSQELPNYMIPSHFVPLERMPLTP 6411
Cdd:cd05945   362 RIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpkpgAEAGLTK-AIKAELAERLPPYMIPRRFVYLDELPLNA 440

                  ....*....
gi 386647928 6412 NGKIDRRAL 6420
Cdd:cd05945   441 NGKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
4893-5298 1.63e-115

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 375.50  E-value: 1.63e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4893 FEKQAECTPEAAAV-VYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 4971
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4972 PSDRIQFMLEDSAASVLLTQTHLQ----ERAQQWGQTLQAALCLDDEAAYAEDASN-----------VANVNEPHDLAYV 5036
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKleelLEALGKLEVVKLVLVLDRDPVLKEEPLPeeakpadvpppPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5037 IYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPV---RLLQLASFSFDV-FVGDIARTLYNGGTMVICPKDDRIDP 5112
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpddRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5113 ARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDS 5192
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA--LVNGYGLTETTGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5193 SLYDEPLAKLPEAGnvPIGKAALNAKFYIVD-AHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegERLY 5271
Cdd:pfam00501  319 TTPLPLDEDLRSLG--SVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWY 390
                          410       420
                   ....*....|....*....|....*..
gi 386647928  5272 RTGDLARWMPDGNVDFIGRIDNQAKIR 5298
Cdd:pfam00501  391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
6986-7432 1.81e-115

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 376.67  E-value: 1.81e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6986 IENIYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPRGEPLQIVYRDKRI 7065
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7066 GFVYEDLSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEA 7145
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7146 YVQGDRPEQKAAPAYSQYIEW----LENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERM 7221
Cdd:pfam00668  161 LLKGEPLPLPPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7222 NRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAeiPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQE 7301
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7302 AALESGRYDFYPLYEIQTQSAQKQE-----LINHLLVFENYPMDEQVEQAGGDDSGTLSITDVDvAEHTNYNFTVTVFP- 7375
Cdd:pfam00668  319 DLLSAEPHQGYPFGDLVNDLRLPRDlsrhpLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSVI-EEEAKYDLSLTASEr 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  7376 GDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVEII 7432
Cdd:pfam00668  398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
AMP-binding pfam00501
AMP-binding enzyme;
3860-4250 2.45e-115

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 374.73  E-value: 2.45e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3860 FEEQALRNPDAVAV-VFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY 3938
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3939 PEDRIRYMLEDSGAQALLTQRHL--------RERVSFAGTFVAVDDEQAYHADGSN-----------LEPVVGPNHLAYV 3999
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleelleaLGKLEVVKLVLVLDRDPVLKEEPLPeeakpadvpppPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4000 IYTSGTTGKPKGVMVEHHGL----CSLKLMFANTLQMTEQDRVVQFASLSFDAS-CWEIFKALFFGATLYIPTSTTILDY 4074
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4075 PLFESYMNENGITATILPPTYAAYL------NPDRMPSLKKLITGGSAASVEFVQQWKDK---VLYfNAYGPTEASIVTS 4145
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRELfggALV-NGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4146 IWDEASDSLGDRKSvpIGRPLANHRIYVVD-SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDnpfepgERMYR 4224
Cdd:pfam00501  320 TPLPLDEDLRSLGS--VGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYR 391
                          410       420
                   ....*....|....*....|....*.
gi 386647928  4225 TGDLVRWLPDGNLEYLGRIDHQVKIR 4250
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
2351-2741 2.97e-115

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 374.73  E-value: 2.97e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2351 FEEQAERIPDHPAV-VFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEY 2429
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2430 PEDRISYMLEDSSAQVLLAQ--------RRLQERVSFAGTVVTVDDEQAYAGDGSN-----------LESAVGPNDLAYI 2490
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDdalkleelLEALGKLEVVKLVLVLDRDPVLKEEPLPeeakpadvpppPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2491 IYTSGTTGKPKGVMVEHHGL----CSLKQMFANTLQINAQDRVVQFASLSFDAS-CWEVFQTLFFGATLYIPTKETILDY 2565
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2566 QWFERYMSDNGITTATLPPTYAVYL------NPDHMPDFKRLIAAGSASSLELLQQWKDKV--KYFNAYGPTEDSICTTI 2637
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRELFggALVNGYGLTETTGVVTT 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2638 WTPSTEDISQLKSvpIGGPIVNHRIYIVDAHY-QPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfepgERMYRT 2716
Cdd:pfam00501  321 PLPLDEDLRSLGS--VGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 386647928  2717 GDLAKWLPDGTIEYLGRIDHQVKIR 2741
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1902-2312 3.61e-115

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 375.06  E-value: 3.61e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1902 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVY--KEVNFAVEH 1979
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILeeDEATPKLEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1980 YRTSEAEAGEVVRGFVR-TFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGE------SLAT 2052
Cdd:cd19538    83 KEVDEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2053 LRIQYKDYAVWQQS-----EEQLERVKRQEAYWLDMFRGeLPV-LEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVA 2126
Cdd:cd19538   163 LPVQYADYALWQQEllgdeSDPDSLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2127 AESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAY 2206
Cdd:cd19538   242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2207 EHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEELQLDGLKLAPYPSGNTIARFDLTLDVTE-----TGSGLECN 2281
Cdd:cd19538   322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREqyndgTPNGIEGF 401
                         410       420       430
                  ....*....|....*....|....*....|.
gi 386647928 2282 LEYATSLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19538   402 IEYRTDLFDHETIEALAQRYLLLLESAVENP 432
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
5937-6431 1.27e-114

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 374.15  E-value: 1.27e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5937 IHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPID 6016
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6017 PDYPEDRIRYMLEDSGAKLLLVQghlldrasfadklvnlnddgayhedgsnlepvngpehltYVIYTSGTTGRPKGVMVE 6096
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVTA---------------------------------------LILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6097 HRNVVRLVKNTN-YVELNEQTHILQTGAVVFDAS-TFEIWGALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTMWLTAP 6174
Cdd:COG0318   122 HRNLLANAAAIAaALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPT 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6175 LYNQLSQQ---DSGMFAGLKTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINN 6251
Cdd:COG0318   199 MLARLLRHpefARYDLSSLRLVVSGGAPLPPELLER-FEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPG 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6252 STAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVessflpgERCYRTGDLARWLPDGTLEYKGRIDEQVK 6331
Cdd:COG0318   278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDMII 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6332 IRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAALSQELPNYMIPSHFVPLERMPL 6409
Cdd:COG0318   351 SGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRRVEFVDELPR 430
                         490       500
                  ....*....|....*....|..
gi 386647928 6410 TPNGKIDRRALPAPQGNAPVGA 6431
Cdd:COG0318   431 TASGKIDRRALRERYAAGALEA 452
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
7456-7928 2.48e-114

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 373.12  E-value: 2.48e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLltqrhlqecvsfdgkvIAADDEqaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCS-L 7614
Cdd:cd05945    81 REILDAAKPALL----------------IADGDD------------------NAYIIFTSGSTGRPKGVQISHDNLVSfT 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7615 KLMFAETLrITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGIT----------AAILP 7684
Cdd:cd05945   127 NWMLSDFP-LGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITvwvstpsfaaMCLLS 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7685 PTyaiyLSPDRLPSLKKLITGGSAASVEFVQQWKD---KVRYFNAYGPTEASIVTSVWAASPDGLD-LRSVPIGRPIANH 7760
Cdd:cd05945   206 PT----FTPESLPSLRHFLFCGEVLPHKTARALQQrfpDARIYNTYGPTEATVAVTYIEVTPEVLDgYDRLPIGYAKPGA 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7761 QIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPflaGERMYRTGDLARWLPDGNIEYLGRIDHQVKI 7840
Cdd:cd05945   282 KLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKL 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7841 RGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV----ADRELTVsELRGTLSQELPGYMIPSYFVQLEQMP 7916
Cdd:cd05945   359 NGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpkpgAEAGLTK-AIKAELAERLPPYMIPRRFVYLDELP 437
                         490
                  ....*....|..
gi 386647928 7917 LTPNGKIDRNAL 7928
Cdd:cd05945   438 LNANGKIDRKAL 449
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
5492-5902 4.20e-114

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 371.98  E-value: 4.20e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5492 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVY--KEVNFAVEH 5569
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILeeDEATPKLEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5570 YRTSEAEAGEVVRGFVR-TFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGE------SLAP 5642
Cdd:cd19538    83 KEVDEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELAP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5643 LRIQYKDYATWQQS-----EAQQEQMKRQEAYWLDMFRGeLPV-LELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIA 5716
Cdd:cd19538   163 LPVQYADYALWQQEllgdeSDPDSLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5717 AESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAY 5796
Cdd:cd19538   242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5797 EHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSE-----GLELS 5871
Cdd:cd19538   322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREQYNdgtpnGIEGF 401
                         410       420       430
                  ....*....|....*....|....*....|.
gi 386647928 5872 MEYSTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19538   402 IEYRTDLFDHETIEALAQRYLLLLESAVENP 432
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1307-1795 6.74e-113

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 369.27  E-value: 6.74e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 1386
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QFMLEDSAASVLLTqthlqeraqqwgqtlqavlclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSL 1466
Cdd:cd05945    81 REILDAAKPALLIA--------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1467 VNTAAGYRREYRLDQFPVrLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPAliip 1546
Cdd:cd05945   123 VSFTNWMLSDFPLGPGDV-FLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPS---- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1547 FMDYVAEHGLD----MSSMELLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGK 1622
Cdd:cd05945   198 FAAMCLLSPTFtpesLPSLRHFLFCGEVLPHKTARALQQRF-PDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGY 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1623 AALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVdspFVEGERLYRTGDLARWMPDGNVDFIGRID 1702
Cdd:cd05945   277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLD 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1703 NQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESE---LKLSELRSSLSQELPGYMIPSYFVQL 1779
Cdd:cd05945   354 FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGaeaGLTKAIKAELAERLPPYMIPRRFVYL 433
                         490
                  ....*....|....*.
gi 386647928 1780 EQLPLTANGKIDRKAL 1795
Cdd:cd05945   434 DELPLNANGKIDRKAL 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
4897-5385 1.26e-112

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 368.50  E-value: 1.26e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4897 AECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 4976
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4977 QFMLEDSAASVLLTqthlqeraqqwgqtlqaalclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSL 5056
Cdd:cd05945    81 REILDAAKPALLIA--------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5057 VNTAAGYRREYRLDQFPVrLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPAliip 5136
Cdd:cd05945   123 VSFTNWMLSDFPLGPGDV-FLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPS---- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5137 FMDYVAEHGLDMSSMVLLITSSDSC----SVTDYRVLQERFgSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGK 5212
Cdd:cd05945   198 FAAMCLLSPTFTPESLPSLRHFLFCgevlPHKTARALQQRF-PDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGY 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5213 AALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVdspFVEGERLYRTGDLARWMPDGNVDFIGRID 5292
Cdd:cd05945   277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLD 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5293 NQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESE---LKLSELRSSLSQELPGYMIPSYFVQL 5369
Cdd:cd05945   354 FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGaeaGLTKAIKAELAERLPPYMIPRRFVYL 433
                         490
                  ....*....|....*.
gi 386647928 5370 EQLPLTANGKIDRKAL 5385
Cdd:cd05945   434 DELPLNANGKIDRKAL 449
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
262-753 5.21e-112

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 366.83  E-value: 5.21e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  262 IHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPID 341
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  342 PEYPEERIRYMLEDSGTQVLLSQghlqervsfsgtwirlddeeayhedgsnlesvngpehltYVIYTSGTTGKPKGNLTT 421
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVTA---------------------------------------LILYTSGTTGRPKGVMLT 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  422 HRNIIRVVKNTN-YIDVTGQDKLLQLSSYSFD-GSTFDIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVMFITTA 499
Cdd:COG0318   122 HRNLLANAAAIAaALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPT 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  500 FFNVLV---DMNPDCLRHARAILFGGERVSVSHVRKALGHLGPgKIKHVYGPTESTVFATSYDVHEVEEGAVSIpiGGPI 576
Cdd:COG0318   199 MLARLLrhpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGV-RIVEGYGLTETSPVVTVNPEDPGERRPGSV--GRPL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  577 SNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADnpfapgeRMYRTGDLARWLPDGTIEYVGRIDDQ 656
Cdd:COG0318   276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDM 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  657 VKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQM 734
Cdd:COG0318   349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
                         490
                  ....*....|....*....
gi 386647928  735 PLTTNGKVDRRALPAPEES 753
Cdd:COG0318   429 PRTASGKIDRRALRERYAA 447
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
8017-8455 2.20e-109

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 385.36  E-value: 2.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8017 LEQEEHSAIPVIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANG 8096
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8097 EPVQRVYSDVEFAVEY--------SKADREEAVEIAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVG 8168
Cdd:COG1020    81 RPVQVIQPVVAAPLPVvvllvdleALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8169 ILQEEFSRLY------AGEELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAE 8242
Cdd:COG1020   161 LLLAELLRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8243 LEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDK 8322
Cdd:COG1020   241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8323 TFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTvAAQFDLT 8402
Cdd:COG1020   321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSG-TAKFDLT 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 8403 LSVAEDDGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQL 8455
Cdd:COG1020   400 LTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPL 452
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1299-1797 9.97e-108

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 354.50  E-value: 9.97e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1299 FHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 1378
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1379 PDYPSDRIQFMLEDSAASVLLTqthlqeraqqwgqtlqavlclddeaayaedasnvanvnephdlAYVIYTSGTTGRPKG 1458
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT-------------------------------------------ALILYTSGTTGRPKG 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1459 VMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDV-FVGDIARTLYNGGTMVICPkddRIDPARLHYWISEEKITIF 1537
Cdd:COG0318   118 VMLTHRNLLANAAAIAAALGLTPGD-VVLVALPLFHVFgLTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVL 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1538 ESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAIDSSLYDEPLAklpEAGN 1617
Cdd:COG0318   194 FGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPG---ERRP 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1618 VPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegeRLYRTGDLARWMPDGNVDF 1697
Cdd:COG0318   269 GSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-------GWLRTGDLGRLDEDGYLYI 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1698 IGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAE--SELKLSELRSSLSQELPGYMIPSY 1775
Cdd:COG0318   342 VGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRR 421
                         490       500
                  ....*....|....*....|..
gi 386647928 1776 FVQLEQLPLTANGKIDRKALPA 1797
Cdd:COG0318   422 VEFVDELPRTASGKIDRRALRE 443
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
4889-5387 1.72e-106

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 350.65  E-value: 1.72e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4889 FHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 4968
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4969 PDYPSDRIQFMLEDSAASVLLTqthlqeraqqwgqtlqaalclddeaayaedasnvanvnephdlAYVIYTSGTTGRPKG 5048
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT-------------------------------------------ALILYTSGTTGRPKG 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5049 VMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSFDV-FVGDIARTLYNGGTMVICPkddRIDPARLHYWISEEKITIF 5127
Cdd:COG0318   118 VMLTHRNLLANAAAIAAALGLTPGD-VVLVALPLFHVFgLTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVL 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5128 ESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAIDSSLYDEPLAklpEAGN 5207
Cdd:COG0318   194 FGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPG---ERRP 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5208 VPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegeRLYRTGDLARWMPDGNVDF 5287
Cdd:COG0318   269 GSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-------GWLRTGDLGRLDEDGYLYI 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5288 IGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAE--SELKLSELRSSLSQELPGYMIPSY 5365
Cdd:COG0318   342 VGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRR 421
                         490       500
                  ....*....|....*....|..
gi 386647928 5366 FVQLEQLPLTANGKIDRKALPA 5387
Cdd:COG0318   422 VEFVDELPRTASGKIDRRALRE 443
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
3646-4443 2.28e-106

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 377.48  E-value: 2.28e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3646 AAWGIILQKYNGTDDAVFGSvvsgrSAEIAGIEemiglFIntipVRVSCEAEQSFADVMKRVQEAALESGGYDYYPLYEI 3725
Cdd:TIGR03443   54 AAFAALVYRLTGDEDIVLGT-----SSNKSGRP-----FV----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDEL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3726 QAQSAQKQDLITHIMAFenfpmdeqieqagsyedgKLAITDVDIAEQTNY------DFTLVVMPGE-ELAVRFYYNASVY 3798
Cdd:TIGR03443  120 SEHIQAAKKLERTPPLF------------------RLAFQDAPDNQQTTYstgsttDLTVFLTPSSpELELSIYYNSLLF 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3799 EHSAMERLMGHLIHVLEQVTASPNAPVSMLELVTEAEKAeiiHVFNNTA----AEYQQeqTIHGLFEEQALRNPDAVAVV 3874
Cdd:TIGR03443  182 SSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKS---LLPDPTKdldwSGFRG--AIHDIFADNAEKHPDRTCVV 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3875 FEKSQL---------TYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRY 3945
Cdd:TIGR03443  257 ETPSFLdpssktrsfTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTI 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3946 MLEDSGAQALLTQR-----------------HLRERV---------SFAGTFV---AVD---DEQAYHADGSNLepVVGP 3993
Cdd:TIGR03443  337 YLSVAKPRALIVIEkagtldqlvrdyidkelELRTEIpalalqddgSLVGGSLeggETDvlaPYQALKDTPTGV--VVGP 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3994 NHLAYVIYTSGTTGKPKGVMVEHHglcSLKLMF---ANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTT 4070
Cdd:TIGR03443  415 DSNPTLSFTSGSEGIPKGVLGRHF---SLAYYFpwmAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADD 491
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4071 ILDYPLFESYMNENGITATILpptyaaylnpdrMPSLKKLITGGSAASVE------FV------------QQWKDKVLYF 4132
Cdd:TIGR03443  492 IGTPGRLAEWMAKYGATVTHL------------TPAMGQLLSAQATTPIPslhhafFVgdiltkrdclrlQTLAENVCIV 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4133 NAYGPTEASIVTS---IWDEASDS--LGDRKSV-PIGRPLANHRIYVVDSHNRMLPVGVA--GELCISGVGLARGYLNRP 4204
Cdd:TIGR03443  560 NMYGTTETQRAVSyfeIPSRSSDStfLKNLKDVmPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLP 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4205 ELTAEKFVDNPF-EPGE---------------------RMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQ 4262
Cdd:TIGR03443  640 ELNAEKFVNNWFvDPSHwidldkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTH 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4263 LAKIDAVQEAIVLAREDANGQQQLVAYFVAQ-----------------------------RELTaAELRATMSQELPNYM 4313
Cdd:TIGR03443  720 LSQHPLVRENVTLVRRDKDEEPTLVSYIVPQdksdeleefksevddeessdpvvkglikyRKLI-KDIREYLKKKLPSYA 798
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4314 IPSYFVQLAQMPLTPNGKIDRKALPAPEGSMHAGgeyVAPR----------TPTEAKLAHIWQDVL--GLEKVGVKDNFF 4381
Cdd:TIGR03443  799 IPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAA---VAKNrsasaadeefTETEREIRDLWLELLpnRPATISPDDSFF 875
                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928  4382 ELGGHSLRATALASKVRKELNMELPLRHIFQFPTVEQLAEAIGQLEQQEF---------DAIPVVEEREYY 4443
Cdd:TIGR03443  876 DLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKGEEladegdseiEEEETVLELDYA 946
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
6517-6969 3.23e-105

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 347.40  E-value: 3.23e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6517 VTGEIGLTPIQ--RWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENG-YAAWNRAIGEG 6593
Cdd:pfam00668    1 VQDEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGePVQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6594 ELYSLEVADFrDVKSAEQAVEAKANE-IQSSIDLEVGPLFKAGLFQCAD-GDHLLLVIHHGVVDGVSWRILLEDVALGYE 6671
Cdd:pfam00668   81 ELEIIDISDL-SESEEEEAIEAFIQRdLQSPFDLEKGPLFRAGLFRIAEnRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6672 QAAKGEEVRLPAKTDsFRTWSEQLAAYAQSPAMENERAYW-EQIAQT-AVAPLPKDKQS--DRSLQQDSESITIqwsRKE 6747
Cdd:pfam00668  160 QLLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWlEQLEGElPVLQLPKDYARpaDRSFKGDRLSFTL---DED 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6748 TEQLLKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESimtdIDITRTVGWFTSKYPVLLQMEPGRSLST 6827
Cdd:pfam00668  236 TEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS----PDIERMVGMFVNTLPLRIDPKGGKTFSE 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6828 RIKKVKEDLRRI-PNKGIGYGLCRYLSAQP--DGTVWGAEPEISF-NYLGQFDQdlsNNDIGLSPYSSGLEMSDRQARSF 6903
Cdd:pfam00668  312 LIKRVQEDLLSAePHQGYPFGDLVNDLRLPrdLSRHPLFDPMFSFqNYLGQDSQ---EEEFQLSELDLSVSSVIEEEAKY 388
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  6904 ILDINGMITDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAHCAAKEWTELTPSDVQLKGLT 6969
Cdd:pfam00668  389 DLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2925-3372 3.97e-104

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 343.93  E-value: 3.97e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2925 VSGDVSLTPIQH--WFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHKSENGYT-AWNRAIGEG 3001
Cdd:pfam00668    1 VQDEYPLSPAQKrmWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPvQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3002 ELYGLEVVDLKGIEESAQAVEAKANEIQSSIDLEAGPFVKAGLFQCAD-GDHLLIVIHHGVVDGVSWRILLEDLAIGYEQ 3080
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAEnRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3081 AVKGEELRFPAKTDaYRTWSEQLAAYAQSPVIERELAYW-KRVAQTEVQ-PLPKD--EQVDVSLQQDSESISIEwtrEET 3156
Cdd:pfam00668  161 LLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWlEQLEGELPVlQLPKDyaRPADRSFKGDRLSFTLD---EDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3157 EQLLKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGRESImtdiDITRTVGWFTSKYPVVLELEQGKDISYL 3236
Cdd:pfam00668  237 EELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP----DIERMVGMFVNTLPLRIDPKGGKTFSEL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3237 LKKTKEDLRGI-PNKGIGYGICRYLSAAKNDIAWGA--EPEVSF-NYLGQFDQDLQNSdigVSAHTGGKQSSDRQKRIFV 3312
Cdd:pfam00668  313 IKRVQEDLLSAePHQGYPFGDLVNDLRLPRDLSRHPlfDPMFSFqNYLGQDSQEEEFQ---LSELDLSVSSVIEEEAKYD 389
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3313 LDINGMIADGTLSLELSYNGKEYRRETMERLAASLQESLRVIIAHCVSKERAELTPSDVQ 3372
Cdd:pfam00668  390 LSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE 449
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
5678-6520 1.84e-100

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 359.38  E-value: 1.84e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5678 LPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGeglqriAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTpiagRTHSD 5757
Cdd:TIGR03443    9 PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT----SSNKS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5758 LQPIIgmfvntlaIRSYPDDKKTFRSFLDEVKETMLGAYEHQSYPFEELVEKAQPARDLSRNPlfdTLFALQNKETGELQ 5837
Cdd:TIGR03443   79 GRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTP---PLFRLAFQDAPDNQ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5838 LDGlrltpYPAEHTVakfDLSVDVTEGSEGLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAPEAPLASLEMITAEEK 5917
Cdd:TIGR03443  148 QTT-----YSTGSTT---DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQK 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5918 EHIqrvfnateakypSDKT-----------IHQLFEEQAERIPDHLAV----TFED-----KQLTYGELNERANRLARTL 5977
Cdd:TIGR03443  220 SLL------------PDPTkdldwsgfrgaIHDIFADNAEKHPDRTCVvetpSFLDpssktRSFTYKQINEASNILAHYL 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5978 RNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVqghlLDRASFADKLVN--- 6054
Cdd:TIGR03443  288 LKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIV----IEKAGTLDQLVRdyi 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6055 --------------LNDDGA----YHEDGSN--LEP-----------VNGPEHLTYVIYTSGTTGRPKGVMVEHRNVV-- 6101
Cdd:TIGR03443  364 dkelelrteipalaLQDDGSlvggSLEGGETdvLAPyqalkdtptgvVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAyy 443
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6102 --------RLVKNTNYVELNEQTHilqtgavvfDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTA 6173
Cdd:TIGR03443  444 fpwmakrfGLSENDKFTMLSGIAH---------DPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTP 514
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6174 PLYNQLSQQDSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTEN---------TTFSTTHTIVGEQKEAVP 6244
Cdd:TIGR03443  515 AMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETqravsyfeiPSRSSDSTFLKNLKDVMP 594
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6245 IGKPINNSTAYIVD--SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFL---------------------- 6300
Cdd:TIGR03443  595 AGKGMKNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVdpshwidldkennkperefwlg 674
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6301 PGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE---- 6376
Cdd:TIGR03443  675 PRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQdksd 754
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6377 -------------------------RELtIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPAP-------- 6423
Cdd:TIGR03443  755 eleefksevddeessdpvvkglikyRKL-IKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdtaqlaav 833
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6424 -QGNAPVGAEyvAPRTEQEKALAAVWQAVL--GAERVGVTDHFFELGGDSIKSIQVSSRLHQagyKLEIrDL-----FKY 6495
Cdd:TIGR03443  834 aKNRSASAAD--EEFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRK---KLNV-ELplgliFKS 907
                          970       980
                   ....*....|....*....|....*
gi 386647928  6496 PTLAQLSQHiqpVARMIDQGEVTGE 6520
Cdd:TIGR03443  908 PTIKGFAKE---VDRLKKGEELADE 929
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
8035-8446 4.25e-100

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 331.27  E-value: 4.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8035 PVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFE-MANGEPVQRVYSDVEFAVEY- 8112
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVrDDGGVPRQEILPPGPAPLEVr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 ----SKADREEAVEIAQRFV--RPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAG------ 8180
Cdd:cd19539    83 dlsdPDSDRERRLEELLREResRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAArrkgpa 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8181 EELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGeLPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELAA 8260
Cdd:cd19539   163 APLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8261 RHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFE 8340
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8341 HQDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTVAAQFDLTLSVAEDDGAIRGSFQYAA 8420
Cdd:cd19539   322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYAT 401
                         410       420
                  ....*....|....*....|....*.
gi 386647928 8421 KLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19539   402 SLFDEETIQGFLADYLQVLRQLLANP 427
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
2088-2933 5.23e-100

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 357.84  E-value: 5.23e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2088 LPVLEMPTDYPRPAVRRFEGSTLSFRLDAglnealKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTpiagRTHGD 2167
Cdd:TIGR03443    9 PTLSVLPHDYLRPANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT----SSNKS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2168 LQPLIgmfvntlaIRNYPAGGKTFRSFLEEVKETTLGAYEHQTYPFEELVEKLQVPRDLSRNPIFdamFVLQNTENEELQ 2247
Cdd:TIGR03443   79 GRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPL---FRLAFQDAPDNQ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2248 LDGlklapYPSGNTIarfDLTLDVTETGSGLECNLEYATSLYARETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQ 2327
Cdd:TIGR03443  148 QTT-----YSTGSTT---DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQK 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2328 TQLhhvfnataADYEAD-------KTIHQLFEEQAERIPDHPAVV----FEGQQ-----LTYRELNERANRLARTLQALG 2391
Cdd:TIGR03443  220 SLL--------PDPTKDldwsgfrGAIHDIFADNAEKHPDRTCVVetpsFLDPSsktrsFTYKQINEASNILAHYLLKTG 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2392 VKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDR--------------------------ISYMLEDSSAQV 2445
Cdd:TIGR03443  292 IKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtldqlvRDYIDKELELRT 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2446 LLAQRRLQERVSFAGTVV------TVDDEQAYAGDGSNLesAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFAN 2519
Cdd:TIGR03443  372 EIPALALQDDGSLVGGSLeggetdVLAPYQALKDTPTGV--VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAK 449
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2520 TLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAvylnpdhmpdfk 2599
Cdd:TIGR03443  450 RFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMG------------ 517
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2600 RLIAAGSAS---SLE---------------LLQQWKDKVKYFNAYGPTEDSICTTIWT-PSTED----ISQLKSV-PIGG 2655
Cdd:TIGR03443  518 QLLSAQATTpipSLHhaffvgdiltkrdclRLQTLAENVCIVNMYGTTETQRAVSYFEiPSRSSdstfLKNLKDVmPAGK 597
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2656 PIVNHRIYIVDAH--YQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPGE--------------------- 2711
Cdd:TIGR03443  598 GMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvDPSHwidldkennkperefwlgprd 677
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2712 RMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--------- 2782
Cdd:TIGR03443  678 RLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVpqdksdele 757
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2783 ---------ADRTMTVG----------ELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALPAP---------QGN 2834
Cdd:TIGR03443  758 efksevddeESSDPVVKglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdtaqlaavaKNR 837
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2835 ASAGADyvAPRSEEEKVLADVWQAVL--GAERVGATDHFFELGGDSIKSIQVSSRLHQagyKLEIrDL-----FKYPTVA 2907
Cdd:TIGR03443  838 SASAAD--EEFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRK---KLNV-ELplgliFKSPTIK 911
                          970       980
                   ....*....|....*....|....*....
gi 386647928  2908 QLSKHI---RPVARMADQGEVSGDVSLTP 2933
Cdd:TIGR03443  912 GFAKEVdrlKKGEELADEGDSEIEEEETV 940
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
7238-8034 2.56e-98

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 352.44  E-value: 2.56e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7238 AVWGVILQKYNATDDVVYGSvvsgrPAEIPGIEemiglFIntipVRVACQPEESFADVMGRMQEAALESGRYDFYPLYEI 7317
Cdd:TIGR03443   54 AAFAALVYRLTGDEDIVLGT-----SSNKSGRP-----FV----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDEL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7318 --QTQSAQKQELINHL--LVFENYPMDEQveqaggDDSGTLSITDvdvaehtnynFTVTVFPG-DEIVVRFDYNSFVFER 7392
Cdd:TIGR03443  120 seHIQAAKKLERTPPLfrLAFQDAPDNQQ------TTYSTGSTTD----------LTVFLTPSsPELELSIYYNSLLFSS 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7393 ADMERLKGHLLHMLEQIVADPQASVGGLELATAAEKVeiiHVFNNTA----AEYarEQTIHGLFEEQAERMPEKAAVV-- 7466
Cdd:TIGR03443  184 DRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKS---LLPDPTKdldwSGF--RGAIHDIFADNAEKHPDRTCVVet 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7467 --FENTQ-----LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDR-IRYM 7538
Cdd:TIGR03443  259 psFLDPSsktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqTIYL 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7539 ----------LEDSGA-------------QVLLT--QRHLQECVSFDGKVIAADDE------QAYGEDGSNLepVVGPNH 7587
Cdd:TIGR03443  339 svakpralivIEKAGTldqlvrdyidkelELRTEipALALQDDGSLVGGSLEGGETdvlapyQALKDTPTGV--VVGPDS 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7588 LAYVIYTSGTTGKPKGVMVEHHglcSLKLMF---AETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTIL 7664
Cdd:TIGR03443  417 NPTLSFTSGSEGIPKGVLGRHF---SLAYYFpwmAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIG 493
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7665 DYPLFESYMNENGITAAILPPTYAIYLSPD---RLPSLKKLItggsaasveFV------------QQWKDKVRYFNAYGP 7729
Cdd:TIGR03443  494 TPGRLAEWMAKYGATVTHLTPAMGQLLSAQattPIPSLHHAF---------FVgdiltkrdclrlQTLAENVCIVNMYGT 564
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7730 TEAS------IVTSVwAASPDGLD-LRSV-PIGRPIANHQIFIVD--SQNHMLPVGVAGELCISGAGLARGYLNRPELTA 7799
Cdd:TIGR03443  565 TETQravsyfEIPSR-SSDSTFLKnLKDVmPAGKGMKNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNA 643
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7800 EKFVDN--------------------PFLAG--ERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKI 7857
Cdd:TIGR03443  644 EKFVNNwfvdpshwidldkennkperEFWLGprDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQH 723
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7858 ASVQETIVIARGDANGQQQLCAYFVAD-----------------------------RELtVSELRGTLSQELPGYMIPSY 7908
Cdd:TIGR03443  724 PLVRENVTLVRRDKDEEPTLVSYIVPQdksdeleefksevddeessdpvvkglikyRKL-IKDIREYLKKKLPSYAIPTV 802
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7909 FVQLEQMPLTPNGKIDRNALPAP---------EGSMQTGADfvEPRTPVEAELARIWQEVLGIGP--ISVKDNFFELGGH 7977
Cdd:TIGR03443  803 IVPLKKLPLNPNGKVDKPALPFPdtaqlaavaKNRSASAAD--EEFTETEREIRDLWLELLPNRPatISPDDSFFDLGGH 880
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  7978 SLRATVLSSKVNKELNVNLPLRDIFRFPTVEALAQVID------GLEQEEHSAIPVIGER---EYY 8034
Cdd:TIGR03443  881 SILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDrlkkgeELADEGDSEIEEEETVlelDYA 946
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1902-2312 2.68e-98

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 326.26  E-value: 2.68e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1902 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN-GEPVQRVYKEVNFAVEH- 1979
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEVr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1980 -----YRTSEAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGES---- 2049
Cdd:cd19539    83 dlsdpDSDRERRLEELLRERESRgFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgpa 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2050 --LATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGeLPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAA 2127
Cdd:cd19539   163 apLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2128 ESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAYE 2207
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2208 HQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEELQLDGLKLAPYPSG-NTIARFDLTLDVTETGSGLECNLEYAT 2286
Cdd:cd19539   322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDiPDGAKFDLNLTVTEEGTGLRGSLGYAT 401
                         410       420
                  ....*....|....*....|....*.
gi 386647928 2287 SLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19539   402 SLFDEETIQGFLADYLQVLRQLLANP 427
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
67-853 9.65e-98

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 350.90  E-value: 9.65e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    67 YMILLTGVQSLLYKYTSSSSILVGmpvvTKPNENRRPVnqlvILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMT 146
Cdd:TIGR03443   49 FIILLAAFAALVYRLTGDEDIVLG----TSSNKSGRPF----VLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELS 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   147 ERLelQYADGVPVVNTLVALKQLHITDYRQSAVS-----DVLFEFELDKDEVRLHLTYNGNLYTESFIAQAVDHLNRLFS 221
Cdd:TIGR03443  121 EHI--QAAKKLERTPPLFRLAFQDAPDNQQTTYStgsttDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLS 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   222 VVLFQPDLALGQADLLSEAEKHQL------LDAFNKTGTdyprdttIHRLFEEQAERRPDAVAV----TFED-----RQL 286
Cdd:TIGR03443  199 AASSNPDEPIGKVSLITPSQKSLLpdptkdLDWSGFRGA-------IHDIFADNAEKHPDRTCVvetpSFLDpssktRSF 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   287 TYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEER-IRYM----------LED 355
Cdd:TIGR03443  272 TYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqTIYLsvakpralivIEK 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   356 SGTQ---------------------VLLSQGHLQERVSFSGTWIRLDDEEAYHEDGSNLesVNGPEHLTYVIYTSGTTGK 414
Cdd:TIGR03443  352 AGTLdqlvrdyidkelelrteipalALQDDGSLVGGSLEGGETDVLAPYQALKDTPTGV--VVGPDSNPTLSFTSGSEGI 429
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   415 PKGNLTTHRNIirvvknTNYIDVTGQ-------DKLLQLSSYSFDGSTFDIFGALLNGAKLvLVPkeTVLDV---AKLAG 484
Cdd:TIGR03443  430 PKGVLGRHFSL------AYYFPWMAKrfglsenDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVP--TADDIgtpGRLAE 500
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   485 LIEKQQISVMFITTAFFNVLV---DMNPDCLRHAraiLFGGERVSVSHVRKaLGHLGPG-KIKHVYGPTEsTVFATSY-- 558
Cdd:TIGR03443  501 WMAKYGATVTHLTPAMGQLLSaqaTTPIPSLHHA---FFVGDILTKRDCLR-LQTLAENvCIVNMYGTTE-TQRAVSYfe 575
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   559 ------DVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVA--GELCVAGDGLARGYLNRPDLTAEKFADNPFA--- 627
Cdd:TIGR03443  576 ipsrssDSTFLKNLKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVdps 655
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   628 -------------------PGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRE 688
Cdd:TIGR03443  656 hwidldkennkperefwlgPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRR 735
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   689 SANGEKQLCAYYVADRSLPA----------------------------NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNG 740
Cdd:TIGR03443  736 DKDEEPTLVSYIVPQDKSDEleefksevddeessdpvvkglikyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNG 815
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   741 KVDRRALPAPEESM-----ETGVEFVEPR--TELEAGIVNIWKEIL--KIEKISVKDSFFELGGHSLRATTMVSRLHKEL 811
Cdd:TIGR03443  816 KVDKPALPFPDTAQlaavaKNRSASAADEefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKL 895
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386647928   812 NISLPLRDVFRYPTVEKLAEAI------SGMGEQVYSSIPAAEAR---EYY 853
Cdd:TIGR03443  896 NVELPLGLIFKSPTIKGFAKEVdrlkkgEELADEGDSEIEEEETVlelDYA 946
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
854-1264 1.39e-97

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 324.33  E-value: 1.39e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  854 PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMV-GGEPMQRIYPEVEFAVEHI 932
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDdGGVPRQEILPPGPAPLEVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  933 ----------RANEEEADAAVKqfiRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGG--- 999
Cdd:cd19539    83 dlsdpdsdreRRLEELLRERES---RGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAArrk 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1000 ---EDLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGeLPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQR 1076
Cdd:cd19539   160 gpaAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1077 IASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLG 1156
Cdd:cd19539   239 LAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1157 AFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEFRLPGLQltPYPVEE---HTSKFDLSLDIMESGDGFLCG 1233
Cdd:cd19539   319 AQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGL--SYTEGSdipDGAKFDLNLTVTEEGTGLRGS 396
                         410       420       430
                  ....*....|....*....|....*....|.
gi 386647928 1234 IEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19539   397 LGYATSLFDEETIQGFLADYLQVLRQLLANP 427
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
5492-5902 5.93e-97

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 322.41  E-value: 5.93e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5492 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN-GEPVQRVYKEVNFAVEH- 5569
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEVr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5570 -----YRTSEAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGES---- 5639
Cdd:cd19539    83 dlsdpDSDRERRLEELLRERESRgFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgpa 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5640 --LAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGeLPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAA 5717
Cdd:cd19539   163 apLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5718 ESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAYE 5797
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5798 HQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGELQLDGLRLTPYPA-EHTVAKFDLSVDVTEGSEGLELSMEYST 5876
Cdd:cd19539   322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSdIPDGAKFDLNLTVTEEGTGLRGSLGYAT 401
                         410       420
                  ....*....|....*....|....*.
gi 386647928 5877 ALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19539   402 SLFDEETIQGFLADYLQVLRQLLANP 427
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
2345-2828 1.14e-95

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 321.46  E-value: 1.14e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2345 KTIHQLfEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVP 2424
Cdd:PRK04813    3 DIIETI-EEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2425 IDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFAgTVVTVDD-EQAYAGDGS-NLESAVGPNDLAYIIYTSGTTGKPKG 2502
Cdd:PRK04813   82 VDVSSPAERIEMIIEVAKPSLIIATEELPLEILGI-PVITLDElKDIFATGNPyDFDHAVKGDDNYYIIFTSGTTGKPKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2503 VMVEHHGLCSlkqmFAN-TLQINAQDRVVQF---ASLSFDASCWEVFQTLFFGATLYIPTKETILDY-QWFERY-MSDNG 2576
Cdd:PRK04813  161 VQISHDNLVS----FTNwMLEDFALPEGPQFlnqAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFkQLFETLpQLPIN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2577 ITTAT--------LPPTYavylNPDHMPDFKRLIAAG---SASSLELLQQWKDKVKYFNAYGPTEdsicTTIWTPS---T 2642
Cdd:PRK04813  237 VWVSTpsfadmclLDPSF----NEEHLPNLTHFLFCGeelPHKTAKKLLERFPSATIYNTYGPTE----ATVAVTSieiT 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2643 EDI-SQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfEPGERMYRTGDLAK 2721
Cdd:PRK04813  309 DEMlDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2722 wLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAY-------FVADRTMTvGELRG 2794
Cdd:PRK04813  386 -LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYvvpkeedFEREFELT-KAIKK 463
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 2795 ELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK04813  464 ELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
1040-1884 4.75e-95

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 342.43  E-value: 4.75e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1040 LPVLEMPTDYARPAVQSYAGNALRFELDAQKReglqriASENGATLYMVLLAAYTILLQKYTGQEDVVIGTpiagRTHGD 1119
Cdd:TIGR03443    9 PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT----SSNKS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1120 LHPLIgmfvntlaIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFEELVDKLKLARDLSRNP-LFDTMFtlqntenkeF 1198
Cdd:TIGR03443   79 GRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAF---------Q 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1199 RLPGLQLTPYPVEEHTskfDLSLDIMESGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNPAAKIASLGILTVEE 1278
Cdd:TIGR03443  142 DAPDNQQTTYSTGSTT---DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQ 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1279 KAQLvhvfnpaaPDAPEN-------EVFHALFEKQAERTPEVAAVV-----YENDR----LTYRELNERANRLARMLRAQ 1342
Cdd:TIGR03443  219 KSLL--------PDPTKDldwsgfrGAIHDIFADNAEKHPDRTCVVetpsfLDPSSktrsFTYKQINEASNILAHYLLKT 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1343 GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDR---------------------IQFMLEDSAASVLLTQ 1401
Cdd:TIGR03443  291 GIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtLDQLVRDYIDKELELR 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1402 THLQERAQQWGQTL-------QAVLCLDDEAAYAEDASNVanVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYR 1474
Cdd:TIGR03443  371 TEIPALALQDDGSLvggslegGETDVLAPYQALKDTPTGV--VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMA 448
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1475 REYRL---DQFPVrllqLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPAL--IIpfmd 1549
Cdd:TIGR03443  449 KRFGLsenDKFTM----LSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMgqLL---- 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1550 yVAEHGLDMSSMELLITSSDSCSVTDYRVLQErFGSQFRIINAYGVTEAAIDSSLYDEP--------LAKLPEAgnVPIG 1621
Cdd:TIGR03443  521 -SAQATTPIPSLHHAFFVGDILTKRDCLRLQT-LAENVCIVNMYGTTETQRAVSYFEIPsrssdstfLKNLKDV--MPAG 596
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1622 KAALNAKFYIVDAH--LNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGE--------------------- 1678
Cdd:TIGR03443  597 KGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkperefwlgpr 676
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1679 -RLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYF-----TAE- 1751
Cdd:TIGR03443  677 dRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIvpqdkSDEl 756
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1752 SELK----------------------LSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASMqtgMEYV 1809
Cdd:TIGR03443  757 EEFKsevddeessdpvvkglikyrklIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQ---LAAV 833
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1810 APR----------TPQEAKLASIWQEVL--GLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEM 1877
Cdd:TIGR03443  834 AKNrsasaadeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGF 913

                   ....*..
gi 386647928  1878 AQAIARM 1884
Cdd:TIGR03443  914 AKEVDRL 920
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
4444-4854 1.12e-94

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 315.86  E-value: 1.12e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4444 PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELID-GEPVQRIYP------EVD 4516
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPpgpaplEVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4517 FAVETVQASEQEAKAIVRDFI-RPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSG------ 4589
Cdd:cd19539    83 DLSDPDSDRERRLEELLREREsRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAArrkgpa 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4590 EELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGeLPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAA 4669
Cdd:cd19539   163 APLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4670 ESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFE 4749
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4750 HQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEMHLPGlhLTPYPTEYGMS---KFDLSLDMMEDSEGLECSLEF 4826
Cdd:cd19539   322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAG--GLSYTEGSDIPdgaKFDLNLTVTEEGTGLRGSLGY 399
                         410       420
                  ....*....|....*....|....*...
gi 386647928 4827 ATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19539   400 ATSLFDEETIQGFLADYLQVLRQLLANP 427
PRK12467 PRK12467
peptide synthase; Provisional
7992-8455 1.14e-93

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 344.45  E-value: 1.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7992 LNVNLPLRDIFRFPT--VEALAQVIDGLEQEEHS----AIP-VIGEREYYPVSSAQKRLFILHQLEGAQQSYNIPGFATI 8064
Cdd:PRK12467    1 MDNNVALRIARRFITlpLEKRRLYLEKMQEEGVSfanlPIPqVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8065 EGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY------SKADREEAVE--IAQRFVRPFDLRKP 8136
Cdd:PRK12467   81 RGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLddlaneQGRARESQIEayINEEVARPFDLANG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8137 PLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGE------ELPPLRIQYKDYAAWQRSEAYAKRVKQQE 8210
Cdd:PRK12467  161 PLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8211 GYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVG 8290
Cdd:PRK12467  241 AYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8291 TPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNPVFDTMFV 8370
Cdd:PRK12467  321 VPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8371 LQNTEDRGIEADAFSLTPFVFD----QTVAAQFDLTLSVAEDDGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:PRK12467  401 HQNTATGGRDREGAQLPGLTVEelswARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEP 480

                  ....*....
gi 386647928 8447 DIRLSQIQL 8455
Cdd:PRK12467  481 RRRLGELPL 489
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
4622-5474 3.40e-93

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 336.65  E-value: 3.40e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4622 WLEAFRGeLPVLEMPTDYARPAVQSYAGDTLDFRMNSEISeglkriAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTp 4701
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4702 iagRTHADLQSLIgmfvntlaIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEELVDKLQMARDLSRNP-LFDTMFsl 4780
Cdd:TIGR03443   74 ---SSNKSGRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAF-- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4781 qntenkeMHLPGLHLTPYPTEygmSKFDLSLDMMEDSEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDPAAKIAS 4860
Cdd:TIGR03443  141 -------QDAPDNQQTTYSTG---STTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGK 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4861 LGILTADEKAQIvhvfnpaaPDAPEN-------EAFHALFEKQAECTPEAAAVV-----YENDR----LTYRELNERANR 4924
Cdd:TIGR03443  211 VSLITPSQKSLL--------PDPTKDldwsgfrGAIHDIFADNAEKHPDRTCVVetpsfLDPSSktrsFTYKQINEASNI 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4925 LARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDR---------------------IQFMLEDS 4983
Cdd:TIGR03443  283 LAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtLDQLVRDY 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4984 AASVLLTQTHLQERAQQWGQTL-------QAALCLDDEAAYAEDASNVanVNEPHDLAYVIYTSGTTGRPKGVMIEHRSL 5056
Cdd:TIGR03443  363 IDKELELRTEIPALALQDDGSLvggslegGETDVLAPYQALKDTPTGV--VVGPDSNPTLSFTSGSEGIPKGVLGRHFSL 440
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5057 VNTAAGYRREYRL---DQFPVrllqLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPAL 5133
Cdd:TIGR03443  441 AYYFPWMAKRFGLsenDKFTM----LSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAM 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5134 ----------IIPfmdyvaehGLDMSSMVLLITSSDSCsvTDYRVLQErfgsQFRIINAYGVTEAAIDSSLYDEP----- 5198
Cdd:TIGR03443  517 gqllsaqattPIP--------SLHHAFFVGDILTKRDC--LRLQTLAE----NVCIVNMYGTTETQRAVSYFEIPsrssd 582
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5199 ---LAKLPEAgnVPIGKAALNAKFYIVDAH--LNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGE----- 5268
Cdd:TIGR03443  583 stfLKNLKDV--MPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidl 660
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5269 -----------------RLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQ 5331
Cdd:TIGR03443  661 dkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEE 740
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5332 KVLCAHF-----TAE-SELK----------------------LSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRK 5383
Cdd:TIGR03443  741 PTLVSYIvpqdkSDElEEFKsevddeessdpvvkglikyrklIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKP 820
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5384 ALPAPDASMqtgMEYVAPR----------TPQEAKLVSIWQEVL--GLEKVGVKDNFFELGGHSLRATLLVGKVHKEMNV 5451
Cdd:TIGR03443  821 ALPFPDTAQ---LAAVAKNrsasaadeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNV 897
                          970       980
                   ....*....|....*....|...
gi 386647928  5452 ELPLRDVFRCSTVEEMAQAIARM 5474
Cdd:TIGR03443  898 ELPLGLIFKSPTIKGFAKEVDRL 920
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
2345-2828 7.97e-92

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 310.54  E-value: 7.97e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2345 KTIHQLFEeQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVP 2424
Cdd:TIGR01734    1 KLIEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2425 IDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSfAGTVVTVDDEQAYAGDGSNL--ESAVGPNDLAYIIYTSGTTGKPKG 2502
Cdd:TIGR01734   80 VDTSIPSERIEMIIEAAGPELVIHTAELSIDAV-GTQIITLSALEQAETSGGPVsfDHAVKGDDNYYIIYTSGSTGNPKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2503 VMVEHHGLCSlkqmFAN-TLQINAQDRVVQF---ASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGIT 2578
Cdd:TIGR01734  159 VQISHDNLVS----FTNwMLADFPLSEGKQFlnqAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLN 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2579 TATLPPTYA------VYLNPDHMPDFKRLIAAGS----ASSLELLQQWKdKVKYFNAYGPTEDSICTTIWTPSTEDISQL 2648
Cdd:TIGR01734  235 VWVSTPSFVdmclldPNFNQENYPHLTHFLFCGEelpvKTAKALLERFP-KATIYNTYGPTEATVAVTSVKITQEILDQY 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2649 KSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVdnpFEPGERMYRTGDLAKwLPDGTI 2728
Cdd:TIGR01734  314 PRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQL 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2729 EYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQ-KQLCAY-------FVADRTMTvGELRGELSGEL 2800
Cdd:TIGR01734  390 FYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAivpetedFEKEFQLT-KAIKKELKKSL 468
                          490       500
                   ....*....|....*....|....*...
gi 386647928  2801 PGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:TIGR01734  469 PAYMIPRKFIYRDQLPLTANGKIDRKAL 496
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
3397-3821 1.09e-91

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 306.68  E-value: 1.09e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3397 IYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGWRGEPLQIVYRYKPVEFA 3476
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3477 YEDLRHLAEAEwsAYLDQLVNDDKTRGFDLEQDALMRVKVVR-TQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYL 3555
Cdd:cd19536    81 ELDLTPLEEQL--DPLRAYKEETKIRRFDLGRAPLVRAALVRkDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3556 RNDLSERPAAPSYSHYIEWLEKQ-DMEAAARYWTGFLAGYDSqTTLPQGKLHNKDGEYTEANILrsLGKSLTERMSRIAK 3634
Cdd:cd19536   159 EYKPLSLPPAQPYRDFVAHERASiQQAASERYWREYLAGATL-ATLPALSEAVGGGPEQDSELL--VSVPLPVRSRSLAK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3635 QHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEMIGLFINTIPVRVSCeAEQSFADVMKRVQEAALES 3714
Cdd:cd19536   236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELES 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3715 GGYDYYPLYEIQAQSAQkQDLITHIMAFENFPMDEQIEQAGSyeDGKLAITDVDIAEQTNYDFTLVVMP-GEELAVRFYY 3793
Cdd:cd19536   315 LSHEQVPLADIQRCSEG-EPLFDSIVNFRHFDLDFGLPEWGS--DEGMRRGLLFSEFKSNYDVNLSVLPkQDRLELKLAY 391
                         410       420
                  ....*....|....*....|....*...
gi 386647928 3794 NASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19536   392 NSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
5935-6420 6.01e-91

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 307.98  E-value: 6.01e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5935 KTIHQLfEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLrnAGVQPDQMVGLMV--ERSLEMVVGMIAILKAGGAY 6012
Cdd:PRK04813    3 DIIETI-EEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFI--DSLKLPDKSPIIVfgHMSPEMLATFLGAVKAGHAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6013 VPIDPDYPEDRIRYMLEDSGAKLLLVQGHLLDRASFAD--KLVNLNDDGAYHEDGSNLEPVNGPEHLtYVIYTSGTTGRP 6090
Cdd:PRK04813   80 IPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPviTLDELKDIFATGNPYDFDHAVKGDDNY-YIIFTSGTTGKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6091 KGVMVEHRNvvrLVKNTNY-VELNEqthiLQTGAVV-------FDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQ 6162
Cdd:PRK04813  159 KGVQISHDN---LVSFTNWmLEDFA----LPEGPQFlnqapysFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6163 QYGINTmWLTAPLYNQLSQQDSG----MFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTI--- 6235
Cdd:PRK04813  232 QLPINV-WVSTPSFADMCLLDPSfneeHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEItde 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6236 VGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSflpGERCYRTGDLARwL 6315
Cdd:PRK04813  311 MLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFD---GQPAYHTGDAGY-L 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6316 PDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVA-----ERELTIG-ELRAALS 6389
Cdd:PRK04813  387 EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPkeedfEREFELTkAIKKELK 466
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 6390 QELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK04813  467 ERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
7452-7928 3.96e-90

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 305.67  E-value: 3.96e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7452 FEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYP 7531
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7532 EDRIRYMLEDSGAQVLLTQRHLQECVSfDGKVIAADDEQAYGEDGSNLEP--VVGPNHLAYVIYTSGTTGKPKGVMVEHH 7609
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATEELPLEIL-GIPVITLDELKDIFATGNPYDFdhAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7610 GLCSlklmFAETL----RITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYP-LFESyMNENGITAAILP 7684
Cdd:PRK04813  167 NLVS----FTNWMledfALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKqLFET-LPQLPINVWVST 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7685 PTYA--IYLSPD----RLPSLKKLITGGSAASVEFVQQWKD---KVRYFNAYGPTEASI-VTSVwAASPDGLD-LRSVPI 7753
Cdd:PRK04813  242 PSFAdmCLLDPSfneeHLPNLTHFLFCGEELPHKTAKKLLErfpSATIYNTYGPTEATVaVTSI-EITDEMLDqYKRLPI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7754 GRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDnpfLAGERMYRTGDLARwLPDGNIEYLGR 7833
Cdd:PRK04813  321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDGLLFYQGR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7834 IDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAY-------FVADRELTvSELRGTLSQELPGYMIP 7906
Cdd:PRK04813  397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYvvpkeedFEREFELT-KAIKKELKERLMEYMIP 475
                         490       500
                  ....*....|....*....|..
gi 386647928 7907 SYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK04813  476 RKFIYRDSLPLTPNGKIDRKAL 497
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
3860-4337 7.17e-90

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 304.90  E-value: 7.17e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3860 FEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGvrPDQLVGLMV--ERSLEMVVGIMAIMKAGGAYIPIDPE 3937
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLK--LPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIPVDVS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3938 YPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADGS-NLEPVVGPNHLAYVIYTSGTTGKPKGVMVEH 4016
Cdd:PRK04813   86 SPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPyDFDHAVKGDDNYYIIFTSGTTGKPKGVQISH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4017 HGLCSlklmFANTL----QMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYP-LFESyMNENGITATIL 4091
Cdd:PRK04813  166 DNLVS----FTNWMledfALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKqLFET-LPQLPINVWVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4092 PPTYA--AYLNPD----RMPSLKKLITGGSAASVEFVQQWKD---KVLYFNAYGPTEASI-VTSIwdEASDSLGDR-KSV 4160
Cdd:PRK04813  241 TPSFAdmCLLDPSfneeHLPNLTHFLFCGEELPHKTAKKLLErfpSATIYNTYGPTEATVaVTSI--EITDEMLDQyKRL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4161 PIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDnpfEPGERMYRTGDLVRwLPDGNLEYL 4240
Cdd:PRK04813  319 PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDGLLFYQ 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4241 GRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAY-------FVAQRELTAAeLRATMSQELPNYM 4313
Cdd:PRK04813  395 GRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYvvpkeedFEREFELTKA-IKKELKERLMEYM 473
                         490       500
                  ....*....|....*....|....
gi 386647928 4314 IPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK04813  474 IPRKFIYRDSLPLTPNGKIDRKAL 497
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
3861-4337 1.63e-86

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 295.13  E-value: 1.63e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3861 EEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGV---RPDQLVGLMverSLEMVVGIMAIMKAGGAYIPIDPE 3937
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILpkkSPIIVYGHM---EPHMLVAFLGSIKSGHAYIPVDTS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3938 YPEDRIRYMLEDSGAQALLTQRHLRerVSFAGTFV----AVDDEQAYHADGSNLEPVVGpNHLAYVIYTSGTTGKPKGVM 4013
Cdd:TIGR01734   84 IPSERIEMIIEAAGPELVIHTAELS--IDAVGTQIitlsALEQAETSGGPVSFDHAVKG-DDNYYIIYTSGSTGNPKGVQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4014 VEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLyIPTSTTILDYP--LFESyMNENGITATIL 4091
Cdd:TIGR01734  161 ISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTL-HCLDKDITNNFklLFEE-LPKTGLNVWVS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4092 PPTYA------AYLNPDRMPSLKKLITGG-----SAASvEFVQQWKDKVLYfNAYGPTEASI-VTSIwdEASDSLGDR-K 4158
Cdd:TIGR01734  239 TPSFVdmclldPNFNQENYPHLTHFLFCGeelpvKTAK-ALLERFPKATIY-NTYGPTEATVaVTSV--KITQEILDQyP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4159 SVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVdnpFEPGERMYRTGDLVRwLPDGNLE 4238
Cdd:TIGR01734  315 RLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLF 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4239 YLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQ-QQLVAYFVAQRELTAAE------LRATMSQELPN 4311
Cdd:TIGR01734  391 YQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPETEDFEKEfqltkaIKKELKKSLPA 470
                          490       500
                   ....*....|....*....|....*.
gi 386647928  4312 YMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:TIGR01734  471 YMIPRKFIYRDQLPLTANGKIDRKAL 496
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
7453-7928 2.02e-86

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 294.74  E-value: 2.02e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7453 EEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPE 7532
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7533 DRIRYMLEDSGAQVLLTQRHLqecvSFD---GKVIAADDEQAYGEDGSNLE---PVVGpNHLAYVIYTSGTTGKPKGVMV 7606
Cdd:TIGR01734   87 ERIEMIIEAAGPELVIHTAEL----SIDavgTQIITLSALEQAETSGGPVSfdhAVKG-DDNYYIIYTSGSTGNPKGVQI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7607 EHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPT 7686
Cdd:TIGR01734  162 SHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7687 YA------IYLSPDRLPSLKKLITGGSAASVEFVQQWKD---KVRYFNAYGPTEASI-VTSVwAASPDGLD-LRSVPIGR 7755
Cdd:TIGR01734  242 FVdmclldPNFNQENYPHLTHFLFCGEELPVKTAKALLErfpKATIYNTYGPTEATVaVTSV-KITQEILDqYPRLPIGF 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7756 PIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVdnpFLAGERMYRTGDLARwLPDGNIEYLGRID 7835
Cdd:TIGR01734  321 AKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLFYQGRLD 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7836 HQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQ-QQLCAY-------FVADRELTvSELRGTLSQELPGYMIPS 7907
Cdd:TIGR01734  397 FQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAivpetedFEKEFQLT-KAIKKELKKSLPAYMIPR 475
                          490       500
                   ....*....|....*....|.
gi 386647928  7908 YFVQLEQMPLTPNGKIDRNAL 7928
Cdd:TIGR01734  476 KFIYRDQLPLTANGKIDRKAL 496
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
5935-6420 3.77e-84

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 288.19  E-value: 3.77e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5935 KTIHQLFEeQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVP 6014
Cdd:TIGR01734    1 KLIEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6015 IDPDYPEDRIRYMLEDSGAKLLL-VQGHLLDraSFADKLVNLNDDGAYHEDGSNLE---PVNGPEHLtYVIYTSGTTGRP 6090
Cdd:TIGR01734   80 VDTSIPSERIEMIIEAAGPELVIhTAELSID--AVGTQIITLSALEQAETSGGPVSfdhAVKGDDNY-YIIYTSGSTGNP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6091 KGVMVEHRNvvrLVKNTNYV----ELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGI 6166
Cdd:TIGR01734  157 KGVQISHDN---LVSFTNWMladfPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6167 NTmWLTAPLYNQLSQQDSGM----FAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGE---Q 6239
Cdd:TIGR01734  234 NV-WVSTPSFVDMCLLDPNFnqenYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEildQ 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6240 KEAVPIG--KPinNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSflpGERCYRTGDLARwLPD 6317
Cdd:TIGR01734  313 YPRLPIGfaKP--DMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSHE---GQPAYRTGDAGT-ITD 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6318 GTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQ-KQLCAY-------FVAERELTiGELRAALS 6389
Cdd:TIGR01734  387 GQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAivpetedFEKEFQLT-KAIKKELK 465
                          490       500       510
                   ....*....|....*....|....*....|.
gi 386647928  6390 QELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:TIGR01734  466 KSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
262-747 5.68e-84

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 287.56  E-value: 5.68e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  262 IHRLfEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLrnAGVQADQLVGLMV--ERSLEMIVGIMGILKAGGAYVP 339
Cdd:PRK04813    5 IETI-EEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFI--DSLKLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  340 IDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTwIRLDD-EEAYHEDGSNLES--VNGPEHLtYVIYTSGTTGKPK 416
Cdd:PRK04813   82 VDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPV-ITLDElKDIFATGNPYDFDhaVKGDDNY-YIIFTSGTTGKPK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  417 GNLTTHRNIirvVKNTNYI----DVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQIS 492
Cdd:PRK04813  160 GVQISHDNL---VSFTNWMledfALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPIN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  493 VMFITTAFfnvlVDM-----------NPDcLRHaraILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDV- 560
Cdd:PRK04813  237 VWVSTPSF----ADMclldpsfneehLPN-LTH---FLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEIt 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  561 HEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPfapGERMYRTGDLAR 640
Cdd:PRK04813  309 DEMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFD---GQPAYHTGDAGY 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  641 wLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYV-------ADRSLPAnEVRS 713
Cdd:PRK04813  386 -LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVpkeedfeREFELTK-AIKK 463
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928  714 TLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK04813  464 ELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1303-1795 1.10e-83

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 286.79  E-value: 1.10e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1303 FEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 1382
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLEDSAASVLLTQTHLQEraqqwGQTLQAVLCLDD-EAAYAEDAS-NVANVNEPHDLAYVIYTSGTTGRPKGVM 1460
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATEELPL-----EILGIPVITLDElKDIFATGNPyDFDHAVKGDDNYYIIFTSGTTGKPKGVQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1461 IEHRSLVNTAAGYRREYRLDQFPVRLLQlASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFEST 1540
Cdd:PRK04813  163 ISHDNLVSFTNWMLEDFALPEGPQFLNQ-APYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVST 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1541 PALI-IPFMD--YVAEHgldMSSMELLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEA--AIDS-SLYDEPLAKLPE 1614
Cdd:PRK04813  242 PSFAdMCLLDpsFNEEH---LPNLTHFLFCGEELPHKTAKKLLERFPSA-TIYNTYGPTEAtvAVTSiEITDEMLDQYKR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1615 agnVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfVEGERLYRTGDLARwMPDGN 1694
Cdd:PRK04813  318 ---LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDGL 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1695 VDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREdaKGQKV--LCAYFTA-----ESELKL-SELRSSLSQE 1766
Cdd:PRK04813  391 LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYN--KDHKVqyLIAYVVPkeedfEREFELtKAIKKELKER 468
                         490       500
                  ....*....|....*....|....*....
gi 386647928 1767 LPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK04813  469 LMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
4893-5385 5.07e-83

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 284.87  E-value: 5.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4893 FEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 4972
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLEDSAASVLLTQTHLQERAQQwGQTLQAAlclDDEAAYAEDAS-NVANVNEPHDLAYVIYTSGTTGRPKGVMI 5051
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATEELPLEILG-IPVITLD---ELKDIFATGNPyDFDHAVKGDDNYYIIFTSGTTGKPKGVQI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5052 EHRSLVNTAAGYRREYRLDQFPVRLLQlASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTP 5131
Cdd:PRK04813  164 SHDNLVSFTNWMLEDFALPEGPQFLNQ-APYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 ALI-IPFMD--YVAEHgldMSSMVLLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEA--AIDS-SLYDEPLAKLPEa 5205
Cdd:PRK04813  243 SFAdMCLLDpsFNEEH---LPNLTHFLFCGEELPHKTAKKLLERFPSA-TIYNTYGPTEAtvAVTSiEITDEMLDQYKR- 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5206 gnVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfVEGERLYRTGDLARwMPDGNV 5285
Cdd:PRK04813  318 --LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDGLL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5286 DFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREdaKGQKV--LCAHFTA-----ESELKL-SELRSSLSQEL 5357
Cdd:PRK04813  392 FYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYN--KDHKVqyLIAYVVPkeedfEREFELtKAIKKELKERL 469
                         490       500
                  ....*....|....*....|....*...
gi 386647928 5358 PGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK04813  470 MEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
6989-7413 7.95e-83

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 281.26  E-value: 7.95e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6989 IYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPRGEPLQIVYRDKRIGFV 7068
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7069 YEDLSHLpaDERQASVERLEQEDIARGFDLEQDALVRVAVIR-TQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYV 7147
Cdd:cd19536    81 ELDLTPL--EEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRkDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7148 QGDRPEQKAAPAYSQYIEWLENQ-DSAAASAYWSNYLAGYEGQTaLPQEKAQKRSEGYVAEHVVceLDKELSERMNRAAK 7226
Cdd:cd19536   159 EYKPLSLPPAQPYRDFVAHERASiQQAASERYWREYLAGATLAT-LPALSEAVGGGPEQDSELL--VSVPLPVRSRSLAK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7227 QCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVACqPEESFADVMGRMQEAALES 7306
Cdd:cd19536   236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELES 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7307 GRYDFYPLYEIQTQSAQkQELINHLLVFENYPMDEQVEQAGGDDSgtLSITDVDVAEHTNYNFTVTVFP-GDEIVVRFDY 7385
Cdd:cd19536   315 LSHEQVPLADIQRCSEG-EPLFDSIVNFRHFDLDFGLPEWGSDEG--MRRGLLFSEFKSNYDVNLSVLPkQDRLELKLAY 391
                         410       420
                  ....*....|....*....|....*...
gi 386647928 7386 NSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19536   392 NSQVLDEEQAQRLAAYYKSAIAELATAP 419
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
5491-5902 1.01e-81

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 278.52  E-value: 1.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5491 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFA---- 5566
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFriei 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5567 --VEHYRTSEAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNG-----E 5638
Cdd:cd19066    82 idLRNLADPEARLLELIDQIQQTiYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqkP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5639 SLAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAAE 5718
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5719 SGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAYEH 5798
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5799 QSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGELQLDGLRL-TPYPAEHTVAKFDLSVDVTEGSEG-LELSMEYST 5876
Cdd:cd19066   322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFtTPVYTSSEGTVFDLDLEASEDPDGdLLLRLEYSR 401
                         410       420
                  ....*....|....*....|....*.
gi 386647928 5877 ALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19066   402 GVYDERTIDRFAERYMTALRQLIENP 427
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1901-2312 1.67e-81

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 277.75  E-value: 1.67e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1901 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFA---- 1976
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFriei 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1977 --VEHYRTSEAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNG-----E 2048
Cdd:cd19066    82 idLRNLADPEARLLELIDQIQQTiYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqkP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2049 SLATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAE 2128
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2129 SGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAYEH 2208
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2209 QTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTENEELQLDGLKL-APYPSGNTIARFDLTLDVTETGSG-LECNLEYAT 2286
Cdd:cd19066   322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFtTPVYTSSEGTVFDLDLEASEDPDGdLLLRLEYSR 401
                         410       420
                  ....*....|....*....|....*.
gi 386647928 2287 SLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19066   402 GVYDERTIDRFAERYMTALRQLIENP 427
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
1298-1795 5.02e-81

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 278.95  E-value: 5.02e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1298 VFHALFEkQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPL 1377
Cdd:TIGR01734    2 LIEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1378 DPDYPSDRIQFMLEDSAASVLLTQTHLQerAQQWGQTLQAVLCLDDEAAYAEDASNVANVNEpHDLAYVIYTSGTTGRPK 1457
Cdd:TIGR01734   81 DTSIPSERIEMIIEAAGPELVIHTAELS--IDAVGTQIITLSALEQAETSGGPVSFDHAVKG-DDNYYIIYTSGSTGNPK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1458 GVMIEHRSLVNTAagyrrEYRLDQFPV----RLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEK 1533
Cdd:TIGR01734  158 GVQISHDNLVSFT-----NWMLADFPLsegkQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTG 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1534 ITIFESTPALI-IPFMD-YVAEHglDMSSMELLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEA--AIDS-SLYDEP 1608
Cdd:TIGR01734  233 LNVWVSTPSFVdMCLLDpNFNQE--NYPHLTHFLFCGEELPVKTAKALLERFPKA-TIYNTYGPTEAtvAVTSvKITQEI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1609 LAKLPeagNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVdspFVEGERLYRTGDLAR 1688
Cdd:TIGR01734  310 LDQYP---RLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1689 wMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDaKGQKV--LCAYFTA-----ESELKLS-ELR 1760
Cdd:TIGR01734  384 -ITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYN-KDHKVeyLIAAIVPetedfEKEFQLTkAIK 461
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 386647928  1761 SSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:TIGR01734  462 KELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
7587-7924 6.15e-81

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 272.62  E-value: 6.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7587 HLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDtilDY 7666
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7667 PLFESYMNENGITAAILPPTYAIYL------SPDRLPSLKKLITGGSAASVEFVQQWKD--KVRYFNAYGPTEASIVTSV 7738
Cdd:cd04433    78 EAALELIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEEapGIKLVNGYGLTETGGTVAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7739 WaaSPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNpflagerMYRTGD 7818
Cdd:cd04433   158 G--PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------WYRTGD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7819 LARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVS--ELRGTL 7896
Cdd:cd04433   229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeELRAHV 308
                         330       340
                  ....*....|....*....|....*...
gi 386647928 7897 SQELPGYMIPSYFVQLEQMPLTPNGKID 7924
Cdd:cd04433   309 RERLAPYKVPRRVVFVDALPRTASGKID 336
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
4443-4854 1.35e-80

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 275.06  E-value: 1.35e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4443 YPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPE-VDFAVET 4521
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKtVRFRIEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4522 VQAS---EQEAKA---IVRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSG-----E 4590
Cdd:cd19066    82 IDLRnlaDPEARLlelIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqkP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4591 ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAE 4670
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4671 SGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEH 4750
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4751 QTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEMHLPGLHL-TPYPTEYGMSKFDLSLDMMEDSEG-LECSLEFAT 4828
Cdd:cd19066   322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFtTPVYTSSEGTVFDLDLEASEDPDGdLLLRLEYSR 401
                         410       420
                  ....*....|....*....|....*.
gi 386647928 4829 ALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19066   402 GVYDERTIDRFAERYMTALRQLIENP 427
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
4897-5385 7.14e-80

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 275.87  E-value: 7.14e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4897 AECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 4976
Cdd:TIGR01734   10 AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4977 QFMLEDSAASVLLTQTHLQerAQQWGQTLQAALCLDDEAAYAEDASNVANVNEpHDLAYVIYTSGTTGRPKGVMIEHRSL 5056
Cdd:TIGR01734   90 EMIIEAAGPELVIHTAELS--IDAVGTQIITLSALEQAETSGGPVSFDHAVKG-DDNYYIIYTSGSTGNPKGVQISHDNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5057 VNTAagyrrEYRLDQFPV----RLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPA 5132
Cdd:TIGR01734  167 VSFT-----NWMLADFPLsegkQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5133 LI-IPFMD-YVAEHglDMSSMVLLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTEA--AIDS-SLYDEPLAKLPeagN 5207
Cdd:TIGR01734  242 FVdMCLLDpNFNQE--NYPHLTHFLFCGEELPVKTAKALLERFPKA-TIYNTYGPTEAtvAVTSvKITQEILDQYP---R 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5208 VPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVdspFVEGERLYRTGDLARwMPDGNVDF 5287
Cdd:TIGR01734  316 LPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLFY 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5288 IGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDaKGQKV--LCAHFTA-----ESELKLS-ELRSSLSQELPG 5359
Cdd:TIGR01734  392 QGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYN-KDHKVeyLIAAIVPetedfEKEFQLTkAIKKELKKSLPA 470
                          490       500
                   ....*....|....*....|....*.
gi 386647928  5360 YMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:TIGR01734  471 YMIPRKFIYRDQLPLTANGKIDRKAL 496
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
853-1264 3.17e-79

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 271.20  E-value: 3.17e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  853 YPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFA-VEH 931
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFrIEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IR-ANEEEADAAVKQFI-----RAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGG-----E 1000
Cdd:cd19066    82 IDlRNLADPEARLLELIdqiqqTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqkP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1001 DLPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASE 1080
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1081 NGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFER 1160
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1161 QDYPFEELVDKLKLARDLSRNPLFDTMFTLQNT-----ENKEFRLPGLQLTPypveEHTSKFDLSLDIMESGDGFLCG-I 1234
Cdd:cd19066   322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNqqqlgKTGGFIFTTPVYTS----SEGTVFDLDLEASEDPDGDLLLrL 397
                         410       420       430
                  ....*....|....*....|....*....|
gi 386647928 1235 EYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19066   398 EYSRGVYDERTIDRFAERYMTALRQLIENP 427
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
3995-4333 3.35e-79

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 267.61  E-value: 3.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3995 HLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSttiLDY 4074
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4075 PLFESYMNENGITATILPPTYAAYL------NPDRMPSLKKLITGGSAASVEFVQQWKD--KVLYFNAYGPTEASIVTSI 4146
Cdd:cd04433    78 EAALELIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEEapGIKLVNGYGLTETGGTVAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4147 WdeaSDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNpfepgerMYRTG 4226
Cdd:cd04433   158 G---PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------WYRTG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4227 DLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVA--QRELTAAELRAT 4304
Cdd:cd04433   228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLrpGADLDAEELRAH 307
                         330       340
                  ....*....|....*....|....*....
gi 386647928 4305 MSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:cd04433   308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
8034-8446 1.64e-77

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 266.20  E-value: 1.64e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8034 YPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEYS 8113
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8114 K-----ADREEAV--EIAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAG-----E 8181
Cdd:cd19066    82 IdlrnlADPEARLleLIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqkP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8182 ELPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELAAR 8261
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8262 HESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEH 8341
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8342 QDYPFEELVERLNVKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTVAAQFDLTLSVAED-DGAIRGSFQYAA 8420
Cdd:cd19066   322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDpDGDLLLRLEYSR 401
                         410       420
                  ....*....|....*....|....*.
gi 386647928 8421 KLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19066   402 GVYDERTIDRFAERYMTALRQLIENP 427
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
4445-4676 2.46e-77

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 258.43  E-value: 2.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4445 VSSAQKRLYILqqlEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAVETVQA 4524
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4525 S-------EQEAKAIVRDFI-RPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGEE----- 4591
Cdd:COG4908    78 SalpeperEAELEELVAEEAsRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLegepp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4592 -LPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAE 4670
Cdd:COG4908   158 pLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                  ....*.
gi 386647928 4671 SGATLY 4676
Cdd:COG4908   238 HGATVN 243
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1902-2312 3.47e-77

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 265.09  E-value: 3.47e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1902 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGF--ELVNGEPVQRVYKEVNFAVEH 1979
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1980 YRTSEAEagEVVRGF----VRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGESLATLRI 2055
Cdd:cd19532    83 VQISDEA--EVEEEFerlkNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2056 QYKDYAVWQQSEEQLERVKRQEAYWLDMFRGE---LPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAESGAT 2132
Cdd:cd19532   161 QYLDFAARQRQDYESGALDEDLAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2133 LYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAYEHQTYP 2212
Cdd:cd19532   241 PFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2213 FEELVEKLQVPRDLSRNPIFDAMF-----VLQNTENEELQLDGLKLAPypsGNTIarFDLTLDVTETGSGlECNLEYAT- 2286
Cdd:cd19532   321 FDVLLDELGVPRSATHSPLFQVFInyrqgVAESRPFGDCELEGEEFED---ARTP--YDLSLDIIDNPDG-DCLLTLKVq 394
                         410       420
                  ....*....|....*....|....*..
gi 386647928 2287 -SLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19532   395 sSLYSEEDAELLLDSYVNLLEAFARDP 421
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
8036-8267 1.02e-75

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 253.81  E-value: 1.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8036 VSSAQKRLFILhqlEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY--- 8112
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVvdl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 ---SKADREEAVE--IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGEE----- 8182
Cdd:COG4908    78 salPEPEREAELEelVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLegepp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8183 -LPPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELAAR 8261
Cdd:COG4908   158 pLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                  ....*.
gi 386647928 8262 HESTLY 8267
Cdd:COG4908   238 HGATVN 243
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
854-1264 1.09e-75

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 260.85  E-value: 1.09e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  854 PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGI--EMVGGEPMQRIYPEVEFAVEH 931
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IR-ANEEEADAAVKQF-IRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGEDLPALRIQY 1009
Cdd:cd19532    83 VQiSDEAEVEEEFERLkNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1010 KDYAVWQQSEAQKEQLKRQEAYWLEVFRGE---LPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASENGATLY 1086
Cdd:cd19532   163 LDFAARQRQDYESGALDEDLAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVTPF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1087 MVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFE 1166
Cdd:cd19532   243 HFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1167 ELVDKLKLARDLSRNPLFDTMFTLQNTENKEFRLPGLQLTpyPVEEHTSK--FDLSLDIMESGDGfLCGIEYAT--ALYK 1242
Cdd:cd19532   323 VLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELE--GEEFEDARtpYDLSLDIIDNPDG-DCLLTLKVqsSLYS 399
                         410       420
                  ....*....|....*....|..
gi 386647928 1243 RETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19532   400 EEDAELLLDSYVNLLEAFARDP 421
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
855-1086 1.96e-75

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 253.04  E-value: 1.96e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  855 LSSAQKRLYILhqlEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVEHI-- 932
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVdl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  933 -----RANEEEADAAVKQFIRA-FDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGED----- 1001
Cdd:COG4908    78 salpePEREAELEELVAEEASRpFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLegepp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1002 -LPALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIASE 1080
Cdd:COG4908   158 pLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                  ....*.
gi 386647928 1081 NGATLY 1086
Cdd:COG4908   238 HGATVN 243
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
5492-5902 2.72e-75

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 259.70  E-value: 2.72e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5492 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGF--ELVNGEPVQRVYKEVNFAVEH 5569
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5570 YRTSEAEagEVVRGF----VRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGESLAPLRI 5645
Cdd:cd19532    83 VQISDEA--EVEEEFerlkNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5646 QYKDYATWQQSEAQQEQMKRQEAYWLDMFRGE---LPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAAESGAT 5722
Cdd:cd19532   161 QYLDFAARQRQDYESGALDEDLAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5723 LYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAYEHQSYP 5802
Cdd:cd19532   241 PFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5803 FEELVEKAQPARDLSRNPLFDTLF-----ALQNKETGELQLDGLRL----TPYpaehtvakfDLSVDVTEGSEG---LEL 5870
Cdd:cd19532   321 FDVLLDELGVPRSATHSPLFQVFInyrqgVAESRPFGDCELEGEEFedarTPY---------DLSLDIIDNPDGdclLTL 391
                         410       420       430
                  ....*....|....*....|....*....|..
gi 386647928 5871 SMeySTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19532   392 KV--QSSLYSEEDAELLLDSYVNLLEAFARDP 421
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
8034-8446 4.01e-75

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 259.06  E-value: 4.01e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8034 YPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFE-MANGEPVQRVYSDVEFAVEY 8112
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 ------SKADREEAVEIAQRFVR--PFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGE--- 8181
Cdd:cd19543    82 ldlshlSEAEQEAELEALAEEDRerGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALgeg 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8182 ---ELPPLRiQYKDYAAW---QRSEAyAKRvkqqegYWLQTLAG--ELPVieLPTDYERTSTRSFEGAELEFEADEALTQ 8253
Cdd:cd19543   162 qppSLPPVR-PYRDYIAWlqrQDKEA-AEA------YWREYLAGfeEPTP--LPKELPADADGSYEPGEVSFELSAELTA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8254 RLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRtHAD---VEPIIGMFVNTLAIRNYPAGDKTFLSYLEE 8330
Cdd:cd19543   232 RLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAElpgIETMVGLFINTLPVRVRLDPDQTVLELLKD 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8331 VKETTLGAFEHQDYPFEELverlnVKRDASRNPVFDTMFVLQN-----TEDRGIEADAFSLTPF-VFDQTvaaQFDLTLS 8404
Cdd:cd19543   311 LQAQQLELREHEYVPLYEI-----QAWSEGKQALFDHLLVFENypvdeSLEEEQDEDGLRITDVsAEEQT---NYPLTVV 382
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 386647928 8405 VAEDDGaIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19543   383 AIPGEE-LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4443-4854 3.64e-74

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 256.47  E-value: 3.64e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4443 YPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAVETV 4522
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4523 QASEQEAKAIVrDFIR-----PFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLY-----SGEEL 4592
Cdd:cd20484    82 DISSLKESEII-AYLRekakePFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqallqGKQPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4593 PGLRI-QYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAES 4671
Cdd:cd20484   161 LASSPaSYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4672 GATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEHQ 4751
Cdd:cd20484   241 SINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4752 TYPFEELVDKLQMARDLSRNPLFDTMFSLQNTenkeMHLPGLH--LTPYPTEYGMS---------KFDLSLDMMEDSEGL 4820
Cdd:cd20484   321 AYPFPAMVRDLNIPRSQANSPVFQVAFFYQNF----LQSTSLQqfLAEYQDVLSIEfvegihqegEYELVLEVYEQEDRF 396
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 4821 ECSLEFATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd20484   397 TLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4444-4854 2.53e-73

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 253.92  E-value: 2.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4444 PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGF--ELIDGEPVQRIYPEVDFAVET 4521
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4522 VQ-ASEQEAKAIVRDF-IRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGEELPGLRIQY 4599
Cdd:cd19532    83 VQiSDEAEVEEEFERLkNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4600 KDYAVWQQSEAQKEQLKRQEAYWLEAFRGE---LPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRIAAESGATLY 4676
Cdd:cd19532   163 LDFAARQRQDYESGALDEDLAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVTPF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4677 MVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFE 4756
Cdd:cd19532   243 HFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4757 ELVDKLQMARDLSRNPLFDTMFSLQNTENKEMHLPGLHLTPYPTEYGMSKFDLSLDMMEDSEGlECSLEFAT--ALYKRE 4834
Cdd:cd19532   323 VLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEGEEFEDARTPYDLSLDIIDNPDG-DCLLTLKVqsSLYSEE 401
                         410       420
                  ....*....|....*....|
gi 386647928 4835 TIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19532   402 DAELLLDSYVNLLEAFARDP 421
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
5939-6420 5.99e-73

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 254.41  E-value: 5.99e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5939 QLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPD 6018
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6019 YPEDRIRYMLEDSGAKlLLVQGHlldraSFADKLvnlnDDGAYHEdgsnLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHR 6098
Cdd:cd05936    83 YTPRELEHILNDSGAK-ALIVAV-----SFTDLL----AAGAPLG----ERVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6099 NvvrLVKNtnyvelneqthILQTGAVVFDAST-----------FEIWG-------ALLNGGRLYVVRNetiLDAVSLKNA 6160
Cdd:cd05936   149 N---LVAN-----------ALQIKAWLEDLLEgddvvlaalplFHVFGltvalllPLALGATIVLIPR---FRPIGVLKE 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6161 IQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTL---IVGGDVLSVPHINRVlREHAGLSIVNGYGPTENTTFSTTHTIVG 6237
Cdd:cd05936   212 IRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLrlcISGGAPLPVEVAERF-EELTGVPIVEGYGLTETSPVVAVNPLDG 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6238 EQKEAvPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPD 6317
Cdd:cd05936   291 PRKPG-SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDED 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6318 GTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQkQLCAYFVAERE--LTIGELRAALSQELPN 6394
Cdd:cd05936   363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSGE-AVKAFVVLKEGasLTEEEIIAFCREQLAG 441
                         490       500
                  ....*....|....*....|....*.
gi 386647928 6395 YMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05936   442 YKVPRQVEFRDELPKSAVGKILRREL 467
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
5491-5902 7.79e-73

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 252.62  E-value: 7.79e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5491 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHY 5570
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5571 RTSEAEAGEVVrGFVRT-----FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMY----NGES-- 5639
Cdd:cd20484    82 DISSLKESEII-AYLREkakepFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqallQGKQpt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5640 LAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAAES 5719
Cdd:cd20484   161 LASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5720 GATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAYEHQ 5799
Cdd:cd20484   241 SINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5800 SYPFEELVEKAQPARDLSRNPLFDTLFALQNKetgeLQLDGLR--LTPYPAE---------HTVAKFDLSVDVTEGSEGL 5868
Cdd:cd20484   321 AYPFPAMVRDLNIPRSQANSPVFQVAFFYQNF----LQSTSLQqfLAEYQDVlsiefvegiHQEGEYELVLEVYEQEDRF 396
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 5869 ELSMEYSTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd20484   397 TLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1903-2134 1.27e-72

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 244.95  E-value: 1.27e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1903 VSSAQKRLYILhqlEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYRT 1982
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1983 S-------EAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGES----- 2049
Cdd:COG4908    78 SalpeperEAELEELVAEEASRpFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLegepp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2050 -LATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAE 2128
Cdd:COG4908   158 pLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                  ....*.
gi 386647928 2129 SGATLY 2134
Cdd:COG4908   238 HGATVN 243
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
8034-8446 3.93e-72

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 250.70  E-value: 3.93e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8034 YPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEYS 8113
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8114 KADREEAVEIAQrFVR-----PFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGAS----VGILQEEFSRLYAGEEL- 8183
Cdd:cd20484    82 DISSLKESEIIA-YLRekakePFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSsltlIHSLLDAYQALLQGKQPt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8184 --PPLRIqYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELAAR 8261
Cdd:cd20484   161 laSSPAS-YYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8262 HESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEH 8341
Cdd:cd20484   240 QSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8342 QDYPFEELVERLNVKRDASRNPVFDTMF----VLQNTEDRGIEA---DAFSLTpFVFDQTVAAQFDLTLSVAEDDGAIRG 8414
Cdd:cd20484   320 AAYPFPAMVRDLNIPRSQANSPVFQVAFfyqnFLQSTSLQQFLAeyqDVLSIE-FVEGIHQEGEYELVLEVYEQEDRFTL 398
                         410       420       430
                  ....*....|....*....|....*....|..
gi 386647928 8415 SFQYAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd20484   399 NIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1901-2312 3.96e-72

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 250.70  E-value: 3.96e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1901 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHY 1980
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1981 RTSEAEAGEVVrGFVRT-----FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMST----DVLTEEFGRLYNGES-- 2049
Cdd:cd20484    82 DISSLKESEII-AYLREkakepFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSltliHSLLDAYQALLQGKQpt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2050 LATLRIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAAES 2129
Cdd:cd20484   161 LASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2130 GATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAYEHQ 2209
Cdd:cd20484   241 SINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2210 TYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTeneeLQLDGLK--LAPYPSGNTIA---------RFDLTLDVTETGSGL 2278
Cdd:cd20484   321 AYPFPAMVRDLNIPRSQANSPVFQVAFFYQNF----LQSTSLQqfLAEYQDVLSIEfvegihqegEYELVLEVYEQEDRF 396
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 2279 ECNLEYATSLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd20484   397 TLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
6992-7413 4.62e-72

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 250.35  E-value: 4.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGpRGEPLQIVYRDKRIGFVYED 7071
Cdd:cd19531     4 LSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEV-DGEPVQVILPPLPLPLPVVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7072 LSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDR 7151
Cdd:cd19531    83 LSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7152 PEQKAAPAysQYI-------EWLENQDSAAASAYWSNYLAGYEGQTALPQEK---AQKRSEGyvaEHVVCELDKELSERM 7221
Cdd:cd19531   163 SPLPPLPI--QYAdyavwqrEWLQGEVLERQLAYWREQLAGAPPVLELPTDRprpAVQSFRG---ARVRFTLPAELTAAL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7222 NRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAeiPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQE 7301
Cdd:cd19531   238 RALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNR--AELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7302 AALEsgrydfyplyeiqtqsAQK-QEL--------------INH------LLVFENYPMDEQveqaggdDSGTLSITDVD 7360
Cdd:cd19531   316 TALE----------------AYAhQDLpfeklvealqperdLSRsplfqvMFVLQNAPAAAL-------ELPGLTVEPLE 372
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 7361 VAEHT-NYNFTVTVFP-GDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19531   373 VDSGTaKFDLTLSLTEtDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
3398-3821 5.93e-72

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 249.96  E-value: 5.93e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3398 YALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYKPVEFAY 3477
Cdd:cd19531     2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEV-DGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3478 EDLRHLAEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESfHVLW-SFHHILMDGWCLPLIAKELFDTYEAYLR 3556
Cdd:cd19531    81 VDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDE-HVLLlTMHHIVSDGWSMGVLLRELAALYAAFLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3557 NDLSERPAAP-SYSHYI----EWLEKQDMEAAARYWTGFLAGYDSQTTLP-----------QGKLHNkdgeyteanilRS 3620
Cdd:cd19531   160 GRPSPLPPLPiQYADYAvwqrEWLQGEVLERQLAYWREQLAGAPPVLELPtdrprpavqsfRGARVR-----------FT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3621 LGKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRS-AEiagIEEMIGLFINTIPVRVSCEAEQS 3699
Cdd:cd19531   229 LPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNrAE---LEGLIGFFVNTLVLRTDLSGDPT 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3700 FADVMKRVQEAALEsgGYDYyplyeiqaqsaqkQDL--------------ITH-----IM-AFENFPMDEQieqagsyED 3759
Cdd:cd19531   306 FRELLARVRETALE--AYAH-------------QDLpfeklvealqperdLSRsplfqVMfVLQNAPAAAL-------EL 363
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 3760 GKLAITDVDIAEQT-NYDFTLVVMP-GEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19531   364 PGLTVEPLEVDSGTaKFDLTLSLTEtDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
853-1264 7.32e-72

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 249.81  E-value: 7.32e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  853 YPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVG-GEPMQRIYPEVEFAVEH 931
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGlGEPLQVVLKDRKLPWRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IR---ANEEEADAAVKQF-----IRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY--GGE- 1000
Cdd:cd19543    82 LDlshLSEAEQEAELEALaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYaaLGEg 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1001 ---DLPALRiQYKDYAVWqqseaqkeqLKRQ-----EAYWLEVFRG--ELPVLemPTDYARPAVQSYAGNALRFELDAQK 1070
Cdd:cd19543   162 qppSLPPVR-PYRDYIAW---------LQRQdkeaaEAYWREYLAGfeEPTPL--PKELPADADGSYEPGEVSFELSAEL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1071 REGLQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRtHGDLhP----LIGMFVNTLAIRNYPAADKTFLSY 1146
Cdd:cd19543   230 TARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAEL-PgietMVGLFINTLPVRVRLDPDQTVLEL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1147 LEDVKETTLGAFERQDYPFEELvdklkLARDLSRNPLFDTMFTLQN-----TENKEFRLPGLQLTPYPVEEHTSkFDLSL 1221
Cdd:cd19543   308 LKDLQAQQLELREHEYVPLYEI-----QAWSEGKQALFDHLLVFENypvdeSLEEEQDEDGLRITDVSAEEQTN-YPLTV 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 386647928 1222 DIMEsGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19543   382 VAIP-GEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4444-4853 9.12e-72

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 249.87  E-value: 9.12e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4444 PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAVETVQ 4523
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4524 AS-----EQEAKAIVRDFIR-PFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLY-------SGE 4590
Cdd:cd20483    83 LSeaadpEAALDQLVRNLRRqELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalragrDLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4591 ELPGLRIQYKDYAVWQQSEAQKEQLKRQEAYWLEAFRGE------LPVlempTDYARPAVQSYAGDTLDFRMNSEISEGL 4664
Cdd:cd20483   163 TVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIpdasklLPF----AKAERPPVKDYERSTVEATLDKELLARM 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4665 KRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETT 4744
Cdd:cd20483   239 KRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4745 LGAFEHQTYPFEELVDKLQMARDLSRNPLFdtmfslQNTENKEMHLPGLH-------LTPYPTEYGMSKFDLSLDMMEDS 4817
Cdd:cd20483   319 LEAYEHSAVPFDYIVDALDVPRSTSHFPIG------QIAVNYQVHGKFPEydtgdfkFTDYDHYDIPTACDIALEAEEDP 392
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 386647928 4818 E-GLECSLEFATALYKRETIERMAKHFEQLLTAIVND 4853
Cdd:cd20483   393 DgGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
2486-2824 9.62e-72

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 246.04  E-value: 9.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2486 DLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDY 2565
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2566 -QWFERYmsdnGITTATLPPTYAVYL---NPDHMPDF---KRLIAAGSASSLELLQQWKD--KVKYFNAYGPTEDSICTT 2636
Cdd:cd04433    81 lELIERE----KVTILLGVPTLLARLlkaPESAGYDLsslRALVSGGAPLPPELLERFEEapGIKLVNGYGLTETGGTVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2637 IWTPsteDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRT 2716
Cdd:cd04433   157 TGPP---DDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------WYRT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2717 GDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVA--DRTMTVGELRG 2794
Cdd:cd04433   227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLrpGADLDAEELRA 306
                         330       340       350
                  ....*....|....*....|....*....|
gi 386647928 2795 ELSGELPGYMIPAHFVQLERMPLTPNGKID 2824
Cdd:cd04433   307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
7460-7931 2.22e-71

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 251.67  E-value: 2.22e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVV-------FENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPE 7532
Cdd:cd17647     2 PERTCVVetpslnsSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7533 DRIRYMLEDSGAQVLLtqrhlqecvsfdgkVIAADDeqaygedgsnlePVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLC 7612
Cdd:cd17647    82 ARQNIYLGVAKPRGLI--------------VIRAAG------------VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7613 SLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILPPTYAIYLS 7692
Cdd:cd17647   136 YYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLT 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7693 PDR---LPSLKK------LITGGSAASVefvQQWKDKVRYFNAYGPTEASIVTSVW-----AASPDGLD-LRSV-PIGRP 7756
Cdd:cd17647   216 AQAttpFPKLHHaffvgdILTKRDCLRL---QTLAENVRIVNMYGTTETQRAVSYFevpsrSSDPTFLKnLKDVmPAGRG 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7757 IANHQIFIVD--SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDN--------------------PFLAG--ER 7812
Cdd:cd17647   293 MLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGprDR 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7813 MYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVAD-------- 7884
Cdd:cd17647   373 LYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRfdkpddes 452
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 7885 ----------------------RELTvSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAP 7931
Cdd:cd17647   453 faqedvpkevstdpivkgligyRKLI-KDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
3881-4340 3.07e-71

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 251.28  E-value: 3.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3881 TYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRH 3960
Cdd:cd17647    22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVIRA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3961 lrervsfAGTfvavddeqayhadgsnlepVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQ 4040
Cdd:cd17647   102 -------AGV-------------------VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4041 FASLSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILPPTYAAYLNPDR---MPSLKK------LI 4111
Cdd:cd17647   156 LSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQAttpFPKLHHaffvgdIL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4112 TGGSAASVefvQQWKDKVLYFNAYGPTEASIVTSIWDEASDS-----LGDRKSV-PIGRPLANHRIYVVDSHNR--MLPV 4183
Cdd:cd17647   236 TKRDCLRL---QTLAENVRIVNMYGTTETQRAVSYFEVPSRSsdptfLKNLKDVmPAGRGMLNVQLLVVNRNDRtqICGI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4184 GVAGELCISGVGLARGYLNRPELTAEKFVDNPF-EPG---------------------ERMYRTGDLVRWLPDGNLEYLG 4241
Cdd:cd17647   313 GEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvEPDhwnyldkdnnepwrqfwlgprDRLYRTGDLGRYLPNGDCECCG 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4242 RIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ---------------------------- 4293
Cdd:cd17647   393 RADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRfdkpddesfaqedvpkevstdpivkgli 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 4294 --RELTaAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAP 4340
Cdd:cd17647   473 gyRKLI-KDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
2349-2828 1.11e-70

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 247.86  E-value: 1.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2349 QLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPE 2428
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2429 YPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVtvddeqayagdgsnLESAVGPNDLAYIIYTSGTTGKPKGVMVEHh 2508
Cdd:cd05936    83 YTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLG--------------ERVALTPEDVAVLQYTSGTTGVPKGAMLTH- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2509 glcslKQMFANTLQINA--------QDRVVQ----FASLSFDASCwevFQTLFFGATLYI---PTKETILDyqwferYMS 2573
Cdd:cd05936   148 -----RNLVANALQIKAwledllegDDVVLAalplFHVFGLTVAL---LLPLALGATIVLiprFRPIGVLK------EIR 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2574 DNGITTATLPPTYAVYLNpdHMPDFK-------RLIAAGSAS-SLELLQQWKDK--VKYFNAYGPTEDSICTTIWTPSTE 2643
Cdd:cd05936   214 KHRVTIFPGVPTMYIALL--NAPEFKkrdfsslRLCISGGAPlPVEVAERFEELtgVPIVEGYGLTETSPVVAVNPLDGP 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2644 DisqlKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermyRTGDLAKWL 2723
Cdd:cd05936   292 R----KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMD 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2724 PDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA-HDDASGQkQLCAYFVADRTMTVG--ELRGELSGEL 2800
Cdd:cd05936   361 EDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGvPDPYSGE-AVKAFVVLKEGASLTeeEIIAFCREQL 439
                         490       500
                  ....*....|....*....|....*...
gi 386647928 2801 PGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05936   440 AGYKVPRQVEFRDELPKSAVGKILRREL 467
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
3859-4337 1.34e-70

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 247.48  E-value: 1.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY 3938
Cdd:cd05936     4 LLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 PEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVavddeqayhadgsnLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 4018
Cdd:cd05936    84 TPRELEHILNDSGAKALIVAVSFTDLLAAGAPLG--------------ERVALTPEDVAVLQYTSGTTGVPKGAMLTHRN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4019 LcslklmFANTLQM--------TEQDRVVQ----FASLSFDASCweiFKALFFGATLYIPTSTTILDypLFESyMNENGI 4086
Cdd:cd05936   150 L------VANALQIkawledllEGDDVVLAalplFHVFGLTVAL---LLPLALGATIVLIPRFRPIG--VLKE-IRKHRV 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4087 TATI-LPPTYAAYLN-PDR----MPSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTSiwdeASDSLGDRK 4158
Cdd:cd05936   218 TIFPgVPTMYIALLNaPEFkkrdFSSLRLCISGGAPLPVEVAERFEELtgVPIVEGYGLTETSPVVA----VNPLDGPRK 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4159 SVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermyRTGDLVRWLPDGNLE 4238
Cdd:cd05936   294 PGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFF 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4239 YLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRE--LTAAELRATMSQELPNYMIPS 4316
Cdd:cd05936   367 IVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGasLTEEEIIAFCREQLAGYKVPR 446
                         490       500
                  ....*....|....*....|.
gi 386647928 4317 YFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05936   447 QVEFRDELPKSAVGKILRREL 467
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
6076-6416 1.42e-70

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 242.58  E-value: 1.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTN-YVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNEtilDA 6154
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAaSGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6155 VSLKNAIQQYGINTMWLTAPLYNQLSQQDSGM---FAGLKTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTENTTFST 6231
Cdd:cd04433    78 EAALELIEREKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGTVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6232 THTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFvessflpGERCYRTGDL 6311
Cdd:cd04433   157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6312 ARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERE--LTIGELRAALS 6389
Cdd:cd04433   230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGadLDAEELRAHVR 309
                         330       340
                  ....*....|....*....|....*..
gi 386647928 6390 QELPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:cd04433   310 ERLAPYKVPRRVVFVDALPRTASGKID 336
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
853-1264 1.69e-70

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 246.07  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  853 YPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPE--VEFAVE 930
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSkpLSFQEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  931 HIRANEEEAdaaVKQFIRA-----FDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY-----GGE 1000
Cdd:cd20484    82 DISSLKESE---IIAYLREkakepFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqallqGKQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1001 DLPALRI-QYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREGLQRIAS 1079
Cdd:cd20484   159 PTLASSPaSYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFAR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1080 ENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFE 1159
Cdd:cd20484   239 SQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1160 RQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTenkeFRLPGLQ--LTPYP-------VEE--HTSKFDLSLDIMESGD 1228
Cdd:cd20484   319 HAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNF----LQSTSLQqfLAEYQdvlsiefVEGihQEGEYELVLEVYEQED 394
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 386647928 1229 GFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd20484   395 RFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1902-2311 1.69e-70

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 246.02  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1902 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYR 1981
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1982 TSEAEAGEV-----VRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYN----GESLA 2051
Cdd:cd20483    83 LSEAADPEAaldqlVRNLRRQeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDalraGRDLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2052 TL---RIQYKDYAVWQQSEEQLERVKRQEAYWLDMFRGeLPvlEMPTDYP-----RPAVRRFEGSTLSFRLDAGLNEALK 2123
Cdd:cd20483   163 TVpppPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEG-IP--DASKLLPfakaeRPPVKDYERSTVEATLDKELLARMK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2124 RVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTL 2203
Cdd:cd20483   240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2204 GAYEHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQ-NTENEELQLDGLKLAPYPSGNTIARFDLTLDVTETGS-GLECN 2281
Cdd:cd20483   320 EAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvHGKFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDPDgGLDLR 399
                         410       420       430
                  ....*....|....*....|....*....|
gi 386647928 2282 LEYATSLYARETIARMAKHLEQLLTAIAKA 2311
Cdd:cd20483   400 LEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
7451-7928 1.69e-70

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 247.48  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:cd05936     4 LLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIaaddeqaygedgsnLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG 7610
Cdd:cd05936    84 TPRELEHILNDSGAKALIVAVSFTDLLAAGAPLG--------------ERVALTPEDVAVLQYTSGTTGVPKGAMLTHRN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7611 LCSLKLMFAETL--RITEEDRVVQ----FASLSFDASCweiFKALFFGATLY-IPAKDTILdypLFESyMNENGITAAI- 7682
Cdd:cd05936   150 LVANALQIKAWLedLLEGDDVVLAalplFHVFGLTVAL---LLPLALGATIVlIPRFRPIG---VLKE-IRKHRVTIFPg 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7683 LPPTY-AIYLSPDR----LPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEASIVTSVwaASPDGLDlRSVPIGR 7755
Cdd:cd05936   223 VPTMYiALLNAPEFkkrdFSSLRLCISGGAPLPVEVAERFEELtgVPIVEGYGLTETSPVVAV--NPLDGPR-KPGSIGI 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7756 PIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWLPDGNIEYLGRID 7835
Cdd:cd05936   300 PLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVDRKK 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7836 HQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA--DRELTVSELRGTLSQELPGYMIPSYFVQLE 7913
Cdd:cd05936   373 DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLkeGASLTEEEIIAFCREQLAGYKVPRQVEFRD 452
                         490
                  ....*....|....*
gi 386647928 7914 QMPLTPNGKIDRNAL 7928
Cdd:cd05936   453 ELPKSAVGKILRREL 467
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
2340-2828 1.69e-70

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 248.95  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2340 DYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAG 2419
Cdd:PRK06187    1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2420 GAYVPIDPEYPEDRISYMLEDSSAQVLLAQ-------RRLQERVSFAGTVVTVDDEQAYAGDGSNLE------------- 2479
Cdd:PRK06187   81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDsefvpllAAILPQLPTVRTVIVEGDGPAAPLAPEVGEyeellaaasdtfd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2480 -SAVGPNDLAYIIYTSGTTGKPKGVMVEHhglcslKQMFANTLQINA------QDRVVQFASLsFDASCWEV-FQTLFFG 2551
Cdd:PRK06187  161 fPDIDENDAAAMLYTSGTTGHPKGVVLSH------RNLFLHSLAVCAwlklsrDDVYLVIVPM-FHVHAWGLpYLALMAG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2552 ATLYIPTK---ETILDYQWFERymsdngITTATLPPT--YAV--YLNPDHMpDFKRL---IAAGSASSLELLQQWKDK-- 2619
Cdd:PRK06187  234 AKQVIPRRfdpENLLDLIETER------VTFFFAVPTiwQMLlkAPRAYFV-DFSSLrlvIYGGAALPPALLREFKEKfg 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2620 VKYFNAYGPTEDSICTTIWTPSTEDISQLK---SVpiGGPIVNHRIYIVDAHYQPVPV--GVAGELCIAGVGLARGYLNR 2694
Cdd:PRK06187  307 IDLVQGYGMTETSPVVSVLPPEDQLPGQWTkrrSA--GRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNR 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2695 PDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA-HDDASG 2773
Cdd:PRK06187  385 PEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGvPDEKWG 457
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 2774 QKQLcAYFVA--DRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK06187  458 ERPV-AVVVLkpGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
3397-3821 6.61e-70

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 242.97  E-value: 6.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3397 IYALTPMQKGMwFHNTLnRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGWRGEPLQIVYRYKPVEFA 3476
Cdd:cd19545     1 IYPCTPLQEGL-MALTA-RQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3477 YEDLrhlaeaewsayLDQLVNDDKTRGFDLEQdALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAylr 3556
Cdd:cd19545    79 ESTS-----------LDEYLEEDRAAPMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG--- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3557 ndlSERPAAPSYSHYIEWLEKQDMEAAARYWTGFLAGYDSQ--TTLPQGKLHNKDGEYTEANIlrslgkslteRMSRIAk 3634
Cdd:cd19545   144 ---EPVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAvfPPLPSSRYQPRPDATLEHSI----------SLPSSA- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3635 QHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAALES 3714
Cdd:cd19545   210 SSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDM 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3715 GGYDYYPLYEIQAqsaqkqdLITHIMAFENFPMDEQIEQAGSYED-----GKLAITDVDIAEQTNYDFTLVV-MPGEELA 3788
Cdd:cd19545   290 IPFEHTGLQNIRR-------LGPDARAACNFQTLLVVQPALPSSTsesleLGIEEESEDLEDFSSYGLTLECqLSGSGLR 362
                         410       420       430
                  ....*....|....*....|....*....|...
gi 386647928 3789 VRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19545   363 VRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
5493-5724 7.39e-70

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 236.86  E-value: 7.39e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5493 VSSAQKRLYILhqlEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYRT 5572
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5573 S-------EAEAGEVVRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGES----- 5639
Cdd:COG4908    78 SalpeperEAELEELVAEEASRpFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLegepp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5640 -LAPLRIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAAE 5718
Cdd:COG4908   158 pLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                  ....*.
gi 386647928 5719 SGATLY 5724
Cdd:COG4908   238 HGATVN 243
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
6989-7413 1.09e-69

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 243.37  E-value: 1.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6989 IYTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPRGEPLQIVYRDKRIGFV 7068
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7069 YEDLSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQ 7148
Cdd:cd19547    81 LLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7149 GDRPEQKAAPAYSQYIEWLENQ--DSAAASAYWSNYLAGYegqTALPQEKAQKRSEGYVaEHVVCELDKELSERMNRAAK 7226
Cdd:cd19547   161 GREPQLSPCRPYRDYVRWIRARtaQSEESERFWREYLRDL---TPSPFSTAPADREGEF-DTVVHEFPEQLTRLVNEAAR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7227 QCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALES 7306
Cdd:cd19547   237 GYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATT 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7307 GRYDFYPLYEIQTQSAQKQ----ELINHLLVFENYPMDEQveqagGDDSGTLSITDVDVAEHTNYNFTVTVFPGDEIVVR 7382
Cdd:cd19547   317 AAHGHVPLAQIKSWASGERlsggRVFDNLVAFENYPEDNL-----PGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKLAFH 391
                         410       420       430
                  ....*....|....*....|....*....|.
gi 386647928 7383 FDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19547   392 FNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
3849-4337 2.59e-69

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 245.48  E-value: 2.59e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3849 EYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAG 3928
Cdd:PRK06187    1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3929 GAYIPIDPEYPEDRIRYMLEDSGAQALLTQ-------RHLRERVSFAGTFVAVDDEQAYHADGSNLE------------- 3988
Cdd:PRK06187   81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDsefvpllAAILPQLPTVRTVIVEGDGPAAPLAPEVGEyeellaaasdtfd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3989 -PVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLsFDASCWEI-FKALFFGATLYIP 4066
Cdd:PRK06187  161 fPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVIP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4067 TS---TTILDYPLFEsymnenGITATILPPT-YAAYLN-----PDRMPSLKKLITGGSAASVEFVQQWKDK--VLYFNAY 4135
Cdd:PRK06187  240 RRfdpENLLDLIETE------RVTFFFAVPTiWQMLLKaprayFVDFSSLRLVIYGGAALPPALLREFKEKfgIDLVQGY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4136 GPTEAS-IVTSIWDEASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPV--GVAGELCISGVGLARGYLNRPELTAEKFV 4212
Cdd:PRK06187  314 GMTETSpVVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETID 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4213 DNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVA 4292
Cdd:PRK06187  394 GG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL 466
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 4293 Q--RELTAAELRATMSQELPNYMIPS--YFVqlAQMPLTPNGKIDRKAL 4337
Cdd:PRK06187  467 KpgATLDAKELRAFLRGRLAKFKLPKriAFV--DELPRTSVGKILKRVL 513
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
401-743 3.89e-69

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 238.72  E-value: 3.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  401 HLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN-YIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDV 479
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAaSGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  480 AKLaglIEKQQISVMFITTAFFNVLVDMNPDC---LRHARAILFGGERVSVSHVRKALGHLGPgKIKHVYGPTESTVFAT 556
Cdd:cd04433    81 LEL---IEREKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPPELLERFEEAPGI-KLVNGYGLTETGGTVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  557 SYDVHEVEEGAVSIpiGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTG 636
Cdd:cd04433   157 TGPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------WYRTG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  637 DLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVA--DRSLPANEVRST 714
Cdd:cd04433   228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLrpGADLDAEELRAH 307
                         330       340
                  ....*....|....*....|....*....
gi 386647928  715 LSQELPAYMLPSYFVQLEQMPLTTNGKVD 743
Cdd:cd04433   308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
7451-7928 5.29e-69

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 246.18  E-value: 5.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFEN-----TQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVP 7525
Cdd:COG0365    14 CLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7526 IDPEYPEDRIRYMLEDSGAQVLLTQ-----------------------RHLQECVSFDGKVIAADDE------QAYGEDG 7576
Cdd:COG0365    94 VFPGFGAEALADRIEDAEAKVLITAdgglrggkvidlkekvdealeelPSLEHVIVVGRTGADVPMEgdldwdELLAAAS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7577 SNLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMFAETLRITEEDRVVQFASLSFDASCW-EIFKALFFGA 7653
Cdd:COG0365   174 AEFEPEpTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLLNGA 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7654 T--LYipakDTILDYP----LFEsYMNENGITAAILPPTY--------AIYLSPDRLPSLKKLITGGSAASVEFVQQWKD 7719
Cdd:COG0365   254 TvvLY----EGRPDFPdpgrLWE-LIEKYGVTVFFTAPTAiralmkagDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7720 --KVRYFNAYGPTEasiVTSVWAASPDGLDLRsvP--IGRPIANHQIFIVDSQNHMLPVGVAGELCISGA--GLARGYLN 7793
Cdd:COG0365   329 avGVPIVDGWGQTE---TGGIFISNLPGLPVK--PgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWN 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7794 RPELTAEKFVDnpflAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANG 7873
Cdd:COG0365   404 DPERYRETYFG----RFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIR 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 7874 QQQLCAY------FVADRELtVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:COG0365   480 GQVVKAFvvlkpgVEPSDEL-AKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
854-1261 6.40e-69

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 241.40  E-value: 6.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  854 PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVEHIR 933
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  934 ANEE-EADAAVKQFIRA-----FDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY----GGEDL- 1002
Cdd:cd20483    83 LSEAaDPEAALDQLVRNlrrqeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDLa 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1003 --PALRIQYKDYAVWQQSEAQKEQLKRQEAYWLEVFRGE------LPVlempTDYARPAVQSYAGNALRFELDAQKREGL 1074
Cdd:cd20483   163 tvPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIpdasklLPF----AKAERPPVKDYERSTVEATLDKELLARM 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1075 QRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETT 1154
Cdd:cd20483   239 KRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1155 LGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQ-NTENKEFRLPGLQLTPYPVEEHTSKFDLSLDIMESGDGFL-C 1232
Cdd:cd20483   319 LEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvHGKFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDPDGGLdL 398
                         410       420
                  ....*....|....*....|....*....
gi 386647928 1233 GIEYATALYKRETIERMAKHFEQLLTAIV 1261
Cdd:cd20483   399 RLEFSTTLYDSADMERFLDNFVTFLTSVI 427
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
4443-4854 8.72e-69

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 240.95  E-value: 8.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4443 YPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFE-LIDGEPVQRIYPEVDFAVET 4521
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4522 V---QASEQEAKAIVRDF-----IRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYS----G 4589
Cdd:cd19543    82 LdlsHLSEAEQEAELEALaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalgeG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4590 EELPGLRIQ-YKDYAVWqqseaqkeqLKRQ-----EAYWLEAFRG--ELPVLemPTDYARPAVQSYAGDTLDFRMNSEIS 4661
Cdd:cd19543   162 QPPSLPPVRpYRDYIAW---------LQRQdkeaaEAYWREYLAGfeEPTPL--PKELPADADGSYEPGEVSFELSAELT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4662 EGLKRIAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRtHADL---QSLIGMFVNTLAIRNYPAADKTFLSYLE 4738
Cdd:cd19543   231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAELpgiETMVGLFINTLPVRVRLDPDQTVLELLK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4739 DVKETTLGAFEHQTYPfeeLVDkLQmARDLSRNPLFDTMFSLQN-----TENKEMHLPGLHLTPYPTEYGMSkFDLSLDM 4813
Cdd:cd19543   310 DLQAQQLELREHEYVP---LYE-IQ-AWSEGKQALFDHLLVFENypvdeSLEEEQDEDGLRITDVSAEEQTN-YPLTVVA 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 386647928 4814 MEDsEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19543   384 IPG-EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
7452-7925 3.45e-68

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 239.43  E-value: 3.45e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7452 FEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYP 7531
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7532 EDRIRYMLEDSGAQVLLtqrhlqecvsfdgkviaaDDeqaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGL 7611
Cdd:cd17631    81 PPEVAYILADSGAKVLF------------------DD-------------------LALLMYTSGTTGRPKGAMLTHRNL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7612 CSLKLMFAETLRITEEDRVVQFASLS--FDASCWeIFKALFFGATLYIPAK---DTILDypLFEsymnENGITAAILPPT 7686
Cdd:cd17631   124 LWNAVNALAALDLGPDDVLLVVAPLFhiGGLGVF-TLPTLLRGGTVVILRKfdpETVLD--LIE----RHRVTSFFLVPT 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7687 --YAIYLSPD----RLPSLKKLITGGSAASVEFVQQWKDK-VRYFNAYGPTEASIVTSVwaASPDGLDLRSVPIGRPIAN 7759
Cdd:cd17631   197 miQALLQHPRfattDLSSLRAVIYGGAPMPERLLRALQARgVKFVQGYGMTETSPGVTF--LSPEDHRRKLGSAGRPVFF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7760 HQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWLPDGNIEYLGRIDHQVK 7839
Cdd:cd17631   275 VEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMII 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7840 IRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVAD--RELTVSELRGTLSQELPGYMIPSYFVQLEQMPL 7917
Cdd:cd17631   348 SGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRpgAELDEDELIAHCRERLARYKIPKSVEFVDALPR 427

                  ....*...
gi 386647928 7918 TPNGKIDR 7925
Cdd:cd17631   428 NATGKILK 435
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1442-1791 5.81e-68

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 235.26  E-value: 5.81e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVrLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRID 1521
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDV-FLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1522 PARLhywISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAId 1601
Cdd:cd04433    80 ALEL---IEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGI--KLVNGYGLTETGG- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1602 SSLYDEPLAKLPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegeRLY 1681
Cdd:cd04433   154 TVATGPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GWY 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1682 RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLS--EL 1759
Cdd:cd04433   225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeEL 304
                         330       340       350
                  ....*....|....*....|....*....|..
gi 386647928 1760 RSSLSQELPGYMIPSYFVQLEQLPLTANGKID 1791
Cdd:cd04433   305 RAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
5491-5902 9.63e-68

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 237.87  E-value: 9.63e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5491 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN-GEPVQRVYKEVNFAVEH 5569
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGlGEPLQVVLKDRKLPWRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5570 YR---TSEAEAGEVVRGFV-----RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMY----NG 5637
Cdd:cd19543    82 LDlshLSEAEQEAELEALAeedreRGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYaalgEG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5638 E--SLAPLRiQYKDYATWQQSEAQQEQmkrqEAYWLDMFRG--ELPVLelPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQ 5713
Cdd:cd19543   162 QppSLPPVR-PYRDYIAWLQRQDKEAA----EAYWREYLAGfeEPTPL--PKELPADADGSYEPGEVSFELSAELTARLQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5714 RIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRtHSDLQPI---IGMFVNTLAIRSYPDDKKTFRSFLDEVKE 5790
Cdd:cd19543   235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAELPGIetmVGLFINTLPVRVRLDPDQTVLELLKDLQA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5791 TMLGAYEHQSYPFEELvekaQPARDLSRnPLFDTLFALQN-----KETGELQLDGLRLTP-YPAEHTvaKFDLSVDVTEG 5864
Cdd:cd19543   314 QQLELREHEYVPLYEI----QAWSEGKQ-ALFDHLLVFENypvdeSLEEEQDEDGLRITDvSAEEQT--NYPLTVVAIPG 386
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 386647928 5865 sEGLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19543   387 -EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
6989-7413 1.17e-67

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 236.43  E-value: 1.17e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6989 IYTLTPMQKGMwFHTALdKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPRGEPLQIVYRDKRIGFV 7068
Cdd:cd19545     1 IYPCTPLQEGL-MALTA-RQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7069 YEDlshlpaderqaSVERLEQEDIARGFDLEQdALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYeayvQ 7148
Cdd:cd19545    79 EST-----------SLDEYLEEDRAAPMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY----Q 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7149 GDRPEQKaaPAYSQYIEWLENQDSAAASAYWSNYLAGYEGQ--TALPQEKAQKRSEGyVAEHVVceldkELSERMNRaak 7226
Cdd:cd19545   143 GEPVPQP--PPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAvfPPLPSSRYQPRPDA-TLEHSI-----SLPSSASS--- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7227 qcRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALES 7306
Cdd:cd19545   212 --GVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDM 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7307 GRYDFYPLYEIQTQSAQKQELIN--HLLVFEnyPMDEQVEQAGGDDsgTLSITDVDVAEHTNYNFTVTVFP-GDEIVVRF 7383
Cdd:cd19545   290 IPFEHTGLQNIRRLGPDARAACNfqTLLVVQ--PALPSSTSESLEL--GIEEESEDLEDFSSYGLTLECQLsGSGLRVRA 365
                         410       420       430
                  ....*....|....*....|....*....|
gi 386647928 7384 DYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19545   366 RYDSSVISEEQVERLLDQFEHVLQQLASAP 395
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
5032-5381 1.50e-67

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 234.10  E-value: 1.50e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5032 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVrLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRID 5111
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDV-FLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5112 PARLhywISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAId 5191
Cdd:cd04433    80 ALEL---IEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGI--KLVNGYGLTETGG- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5192 SSLYDEPLAKLPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegeRLY 5271
Cdd:cd04433   154 TVATGPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GWY 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5272 RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLS--EL 5349
Cdd:cd04433   225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeEL 304
                         330       340       350
                  ....*....|....*....|....*....|..
gi 386647928 5350 RSSLSQELPGYMIPSYFVQLEQLPLTANGKID 5381
Cdd:cd04433   305 RAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
3859-4337 1.87e-67

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 241.55  E-value: 1.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFE-----KSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIP 3933
Cdd:COG0365    14 CLDRHAEGRGDKVALIWEgedgeERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3934 IDPEYPEDRIRYMLEDSGAQALLT---------QRHLRERVSFA----------------GTFVAVDDEQAYH----ADG 3984
Cdd:COG0365    94 VFPGFGAEALADRIEDAEAKVLITadgglrggkVIDLKEKVDEAleelpslehvivvgrtGADVPMEGDLDWDellaAAS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3985 SNLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMFANTLQMTEQDRVVQFASLSFDASCW-EIFKALFFGA 4061
Cdd:COG0365   174 AEFEPEpTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLLNGA 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4062 TlyiptstTIL-----DYP----LFEsYMNENGITATILPPTY--------AAYLNPDRMPSLKKLITGGSAASVEFVQQ 4124
Cdd:COG0365   254 T-------VVLyegrpDFPdpgrLWE-LIEKYGVTVFFTAPTAiralmkagDEPLKKYDLSSLRLLGSAGEPLNPEVWEW 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4125 WKDKV---LYfNAYGPTEA-SIVTSiwdeasdSLGDRKSVP--IGRPLANHRIYVVDSHNRMLPVGVAGELCISG--VGL 4196
Cdd:COG0365   326 WYEAVgvpIV-DGWGQTETgGIFIS-------NLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4197 ARGYLNRPELTAEKFvdnpFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLA 4276
Cdd:COG0365   398 FRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 4277 REDANGQQQLVAYFV-----AQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:COG0365   474 VPDEIRGQVVKAFVVlkpgvEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
7441-7928 3.61e-67

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 239.32  E-value: 3.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7441 EYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAG 7520
Cdd:PRK06187    1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7521 GAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQECVS-------FDGKVIAADDEQAYGEDGSNLE------------- 7580
Cdd:PRK06187   81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAailpqlpTVRTVIVEGDGPAAPLAPEVGEyeellaaasdtfd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7581 -PVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLsFDASCWEI-FKALFFGATLYIP 7658
Cdd:PRK06187  161 fPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVIP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7659 AK---DTILDYPLFEsymnenGITAAILPPT-YAIYLS-----PDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAY 7727
Cdd:PRK06187  240 RRfdpENLLDLIETE------RVTFFFAVPTiWQMLLKaprayFVDFSSLRLVIYGGAALPPALLREFKEKfgIDLVQGY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7728 GPTEASIVTSVwAASPDGLD-----LRSVpiGRPIANHQIFIVDSQNHMLPV--GVAGELCISGAGLARGYLNRPELTAE 7800
Cdd:PRK06187  314 GMTETSPVVSV-LPPEDQLPgqwtkRRSA--GRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7801 KFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAY 7880
Cdd:PRK06187  391 TIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAV 463
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7881 FVA--DRELTVSELRGTLSQELPGYMIPS--YFVqlEQMPLTPNGKIDRNAL 7928
Cdd:PRK06187  464 VVLkpGATLDAKELRAFLRGRLAKFKLPKriAFV--DELPRTSVGKILKRVL 513
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
5492-5901 8.07e-67

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 235.23  E-value: 8.07e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5492 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYR 5571
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5572 TSEAEAGEV-----VRGFVRT-FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYN----GESLA 5641
Cdd:cd20483    83 LSEAADPEAaldqlVRNLRRQeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDalraGRDLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5642 PL---RIQYKDYATWQQSEAQQEQMKRQEAYWLDMFRGELPVLELptdYP-----RPAVRKFEGSLLQRQLEPKLGEGLQ 5713
Cdd:cd20483   163 TVpppPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKL---LPfakaeRPPVKDYERSTVEATLDKELLARMK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5714 RIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETML 5793
Cdd:cd20483   240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5794 GAYEHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKET-GELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSE-GLELS 5871
Cdd:cd20483   320 EAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVHGKfPEYDTGDFKFTDYDHYDIPTACDIALEAEEDPDgGLDLR 399
                         410       420       430
                  ....*....|....*....|....*....|
gi 386647928 5872 MEYSTALYTRETIERMAKHFEQLLTAIVQA 5901
Cdd:cd20483   400 LEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
2348-2828 1.38e-66

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 239.24  E-value: 1.38e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2348 HQLFEEQAERIPDHPAVVFEG-----QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAY 2422
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2423 VPIDPEYPEDRISYMLEDSSAQVLLA---QRR-------------LQERVSFAGTVVTVDD-------------EQAYAG 2473
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITadgGLRggkvidlkekvdeALEELPSLEHVIVVGRtgadvpmegdldwDELLAA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2474 DGSNLESA-VGPNDLAYIIYTSGTTGKPKGVMVEHHG-LCSLKQMFANTLQINAQDRVVQFASLSFDASCW-EVFQTLFF 2550
Cdd:COG0365   172 ASAEFEPEpTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLLN 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2551 GATLYI-------PTKETILdyqwfeRYMSDNGITTATLPPTY--------AVYLNPDHMPDFKRLIAAGSASSLELLQQ 2615
Cdd:COG0365   252 GATVVLyegrpdfPDPGRLW------ELIEKYGVTVFFTAPTAiralmkagDEPLKKYDLSSLRLLGSAGEPLNPEVWEW 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2616 WKDKVKY--FNAYGPTEdsICTTIwtpstedISQLKSVP-----IGGPIVNHRIYIVDAHYQPVPVGVAGELCIAG--VG 2686
Cdd:COG0365   326 WYEAVGVpiVDGWGQTE--TGGIF-------ISNLPGLPvkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPG 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2687 LARGYLNRPDLTAEKFvdnpFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVI 2766
Cdd:COG0365   397 MFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 2767 AHDDASGQKQLCAY------FVADRTMtVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:COG0365   473 GVPDEIRGQVVKAFvvlkpgVEPSDEL-AKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
2346-2830 2.74e-66

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 236.60  E-value: 2.74e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2346 TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI 2425
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2426 DPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFA-------GTVVTVDDEQAYAGDGSNLESA----------------V 2482
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPAlpgchdlRTLIIVGDPAHASEGHPGEEPAswpkllalgdadpphpV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2483 GPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATL----YIPT 2558
Cdd:TIGR03098  161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhdYLLP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2559 KETIldyqwfeRYMSDNGITT-ATLPPTYAVYLN----PDHMPDFKRLIAAGSA---SSLELLQQWKDKVKYFNAYGPTE 2630
Cdd:TIGR03098  241 RDVL-------KALEKHGITGlAAVPPLWAQLAQldwpESAAPSLRYLTNSGGAmprATLSRLRSFLPNARLFLMYGLTE 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2631 DSICTTIwtpsteDISQLKSVP--IGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFE 2708
Cdd:TIGR03098  314 AFRSTYL------PPEEVDRRPdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPF 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2709 PG-----ERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAH-DDASGQK-QLCAYF 2781
Cdd:TIGR03098  388 PGelhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVpDPTLGQAiVLVVTP 467
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 386647928  2782 VADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALPA 2830
Cdd:TIGR03098  468 PGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
274-747 3.59e-66

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 234.29  E-value: 3.59e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQ----LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERI 349
Cdd:cd17654     1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  350 RYMLEDSGTQVLLSQGHLqeRVSFsgtwiRLDDEEAYHEDGSNlesvngPEHLTYVIYTSGTTGKPKGNLTTHRNIIR-V 428
Cdd:cd17654    81 LTVMKKCHVSYLLQNKEL--DNAP-----LSFTPEHRHFNIRT------DECLAYVIHTSGTTGTPKIVAVPHKCILPnI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  429 VKNTNYIDVTgQDKLLQLSS-YSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLA-GLIEKQQISVMFITTAFFN---- 502
Cdd:cd17654   148 QHFRSLFNIT-SEDILFLTSpLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLAdILFKRHRITVLQATPTLFRrfgs 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  503 -VLVDMNPDCLRHARAILFGGERVSVSHVRKALGHLGPG-KIKHVYGPTESTVFATSYdvhEVEEGAVSIPIGGPISNTA 580
Cdd:cd17654   227 qSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGKGNRtRIFNIYGITEVSCWALAY---KVPEEDSPVQLGSPLLGTV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  581 IYIVNAQNKLQpigvAGElcVAGDGLARGYLnRPDLTAEKFADnpfapgerMYRTGDLARwLPDGTIEYVGRIDDQVKIR 660
Cdd:cd17654   304 IEVRDQNGSEG----TGQ--VFLGGLNRVCI-LDDEVTVPKGT--------MRATGDFVT-VKDGELFFLGRKDSQIKRR 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  661 GFRIELGEIEAHLLKLEAIEkATVVVRESangEKQLCAYYVaDRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNG 740
Cdd:cd17654   368 GKRINLDLIQQVIESCLGVE-SCAVTLSD---QQRLIAFIV-GESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHG 442

                  ....*..
gi 386647928  741 KVDRRAL 747
Cdd:cd17654   443 KVDKSEL 449
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
3398-3821 3.64e-66

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 233.46  E-value: 3.64e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3398 YALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVY-RYKPVEFA 3476
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEE-AGRYEQVVLdKTVRFRIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3477 YEDLRHLAEAEwsAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLR 3556
Cdd:cd19066    81 IIDLRNLADPE--ARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3557 NDLSERPAAPSYSHYIEWLEKQ----DMEAAARYWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERMSRI 3632
Cdd:cd19066   159 QKPTLPPPVGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3633 AKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEiaGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAAL 3712
Cdd:cd19066   239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3713 ESGGYDYYPLYEI-----QAQSAQKQDLITHIMAFENFPmdeqiEQAGSYEDGKLAITDVDIAEQTNYDFTLVVMPGE-- 3785
Cdd:cd19066   317 EAIEHQRVPFIELvrhlgVVPEAPKHPLFEPVFTFKNNQ-----QQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDPdg 391
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 386647928 3786 ELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19066   392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
7447-7930 4.90e-66

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 235.83  E-value: 4.90e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7447 TIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPI 7526
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7527 DPEYPEDRIRYMLEDSGAQVLLT--------QRHLQECVSFDGKVIAADDEQAyGEDGSNLEPV---------------- 7582
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTsserldllHPALPGCHDLRTLIIVGDPAHA-SEGHPGEEPAswpkllalgdadpphp 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7583 VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATL----YIP 7658
Cdd:TIGR03098  160 VIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhdYLL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7659 AKDTIldyplfeSYMNENGITA-AILPPTYA----IYLSPDRLPSLKKLI-TGGS--AASVEFVQQWKDKVRYFNAYGPT 7730
Cdd:TIGR03098  240 PRDVL-------KALEKHGITGlAAVPPLWAqlaqLDWPESAAPSLRYLTnSGGAmpRATLSRLRSFLPNARLFLMYGLT 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7731 EASIVTSVwaaSPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAG 7810
Cdd:TIGR03098  313 EAFRSTYL---PPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7811 -----ERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA-- 7883
Cdd:TIGR03098  390 elhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPpg 469
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 386647928  7884 DRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPA 7930
Cdd:TIGR03098  470 GEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
6990-7413 7.59e-66

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 232.30  E-value: 7.59e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6990 YTLTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPrGEPLQIVyRDKRIGFVY 7069
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEA-GRYEQVV-LDKTVRFRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7070 E--DLSHLpaDERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYV 7147
Cdd:cd19066    80 EiiDLRNL--ADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7148 QGDRPEQKAAPAYSQYIEWLENQ----DSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNR 7223
Cdd:cd19066   158 RQKPTLPPPVGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLRE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7224 AAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAeiPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAA 7303
Cdd:cd19066   238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7304 LESGRYDFYPLYEI-----QTQSAQKQELINHLLVFENYPmdeqvEQAGGDDSGTLSITDVDVAEHTNYNFTVTVFPG-- 7376
Cdd:cd19066   316 REAIEHQRVPFIELvrhlgVVPEAPKHPLFEPVFTFKNNQ-----QQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDpd 390
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 386647928 7377 DEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19066   391 GDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2931-3358 1.36e-65

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 231.53  E-value: 1.36e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2931 LTPIQHWFFEPQFAE--PHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFhKSENGyTAWNRAIGEGELYGLEV 3008
Cdd:cd19066     4 LSPMQRGMWFLKKLAtdPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAG-RYEQVVLDKTVRFRIEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3009 VDLKG-IEESAQAVEAKANEIQSSIDLEAGPFVKAGLFQCAD-GDHLLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEE 3086
Cdd:cd19066    82 IDLRNlADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADeRDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3087 LrFPAKTDAYRTWSEQLAAYAQSPVIERELAYWKRVAQ--TEVQPLPKDeQVDVSLQQDSESISIEWTREETEQLLKGVH 3164
Cdd:cd19066   162 T-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHglPPPLPLPKA-KRPSQVASYEVLTLEFFLRSEETKRLREVA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3165 RAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGResimTDIDITRTVGWFTSKYPVVLELEQGKDISYLLKKTKEDL 3244
Cdd:cd19066   240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3245 RGIPNKGIGYGICRYL-SAAKNDIAWGAEPEVSFNYLGQFDQDLQNSDigvsAHTGGKQSSDRQKRIFVLDINGMI-ADG 3322
Cdd:cd19066   316 REAIEHQRVPFIELVRhLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGG----FIFTTPVYTSSEGTVFDLDLEASEdPDG 391
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 386647928 3323 TLSLELSYNGKEYRRETMERLAASLQESLRVIIAHC 3358
Cdd:cd19066   392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
264-747 1.71e-65

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 232.84  E-value: 1.71e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  264 RLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPE 343
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  344 YPEERIRYMLEDSGTQVLLSQGHLQERVSfsgTWIRLDDEEAYHedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTHR 423
Cdd:cd05936    83 YTPRELEHILNDSGAKALIVAVSFTDLLA---AGAPLGERVALT-----------PEDVAVLQYTSGTTGVPKGAMLTHR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  424 NI---IRVVKNTNYIDVTGQDKLLQLSSYsfdgstFDIFG-------ALLNGAKLVLVPKETVLDVAKlagLIEKQQISV 493
Cdd:cd05936   149 NLvanALQIKAWLEDLLEGDDVVLAALPL------FHVFGltvalllPLALGATIVLIPRFRPIGVLK---EIRKHRVTI 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  494 MFITTAFFNVLVDmNPDC----LRHARAILFGGERVSVSHVRKALGHLGpGKIKHVYGPTE-STVFAtsydVHEVEEGAV 568
Cdd:cd05936   220 FPGVPTMYIALLN-APEFkkrdFSSLRLCISGGAPLPVEVAERFEELTG-VPIVEGYGLTEtSPVVA----VNPLDGPRK 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  569 SIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIE 648
Cdd:cd05936   294 PGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFF 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  649 YVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEkQLCAYYVA--DRSLPANEVRSTLSQELPAYMLP 725
Cdd:cd05936   367 IVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSGE-AVKAFVVLkeGASLTEEEIIAFCREQLAGYKVP 445
                         490       500
                  ....*....|....*....|..
gi 386647928  726 SYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05936   446 RQVEFRDELPKSAVGKILRREL 467
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
3868-4337 2.69e-65

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 231.59  E-value: 2.69e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQ----LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRI 3943
Cdd:cd17654     1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 RYMLEDSGAQALLTQRHLR-ERVSFAGTFVAVDDEQAYHadgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSL 4022
Cdd:cd17654    81 LTVMKKCHVSYLLQNKELDnAPLSFTPEHRHFNIRTDEC--------------LAYVIHTSGTTGTPKIVAVPHKCILPN 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4023 KLMFANTLQMTeQDRVVQFAS-LSFDASCWEIFKALFFGATL-YIPTSTTILDYPLFESYMNENGITATILPPT----YA 4096
Cdd:cd17654   147 IQHFRSLFNIT-SEDILFLTSpLTFDPSVVEIFLSLSSGATLlIVPTSVKVLPSKLADILFKRHRITVLQATPTlfrrFG 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4097 AYLNPDRM----PSLKKLITGGSA-ASVEFVQQWKDKVL---YFNAYGPTEasivTSIWDEASDSLGDRKSVPIGRPLAN 4168
Cdd:cd17654   226 SQSIKSTVlsatSSLRVLALGGEPfPSLVILSSWRGKGNrtrIFNIYGITE----VSCWALAYKVPEEDSPVQLGSPLLG 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4169 HRIYVVDSHNRMLPVGVAGELcISGVGLARGYLNRPELTaekfvdnpfepgerMYRTGDLVRwLPDGNLEYLGRIDHQVK 4248
Cdd:cd17654   302 TVIEVRDQNGSEGTGQVFLGG-LNRVCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDSQIK 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4249 IRGYRIELGEVETQLAKIDAVqEAIVLAREDangQQQLVAYFVAQ--RELTAAELRATMsqeLPNYMIPSYFVQLAQMPL 4326
Cdd:cd17654   366 RRGKRINLDLIQQVIESCLGV-ESCAVTLSD---QQRLIAFIVGEssSSRIHKELQLTL---LSSHAIPDTFVQIDKLPL 438
                         490
                  ....*....|.
gi 386647928 4327 TPNGKIDRKAL 4337
Cdd:cd17654   439 TSHGKVDKSEL 449
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
3860-4334 5.77e-65

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 230.19  E-value: 5.77e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3860 FEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYP 3939
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3940 EDRIRYMLEDSGAQALLtqrhlrervsfagtfvavDDeqayhadgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGL 4019
Cdd:cd17631    81 PPEVAYILADSGAKVLF------------------DD-------------------LALLMYTSGTTGRPKGAMLTHRNL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4020 CSLKLMFANTLQMTEQDRVVQFASLS--FDASCWeIFKALFFGATLYI---PTSTTILDypLFEsymnENGITATILPPT 4094
Cdd:cd17631   124 LWNAVNALAALDLGPDDVLLVVAPLFhiGGLGVF-TLPTLLRGGTVVIlrkFDPETVLD--LIE----RHRVTSFFLVPT 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4095 -YAAYLN-PD----RMPSLKKLITGGSAASVEFVQQWKDK-VLYFNAYGPTEASIVTSIWDEAsdsLGDRKSVPIGRPLA 4167
Cdd:cd17631   197 mIQALLQhPRfattDLSSLRAVIYGGAPMPERLLRALQARgVKFVQGYGMTETSPGVTFLSPE---DHRRKLGSAGRPVF 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4168 NHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermyRTGDLVRWLPDGNLEYLGRIDHQV 4247
Cdd:cd17631   274 FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMI 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4248 KIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMP 4325
Cdd:cd17631   347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRpgAELDEDELIAHCRERLARYKIPKSVEFVDALP 426

                  ....*....
gi 386647928 4326 LTPNGKIDR 4334
Cdd:cd17631   427 RNATGKILK 435
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
3855-4339 1.05e-64

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 231.98  E-value: 1.05e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3855 TIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPI 3934
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3935 DPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFA-------GTFVAVDDEQAYHADGSNLEPV----------------V 3991
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPAlpgchdlRTLIIVGDPAHASEGHPGEEPAswpkllalgdadpphpV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3992 GPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLyiptstTI 4071
Cdd:TIGR03098  161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV------VL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4072 LDYPLFESYMN---ENGITA-TILPPTYAAYLN----PDRMPSLKKLI-TGGS--AASVEFVQQWKDKVLYFNAYGPTEA 4140
Cdd:TIGR03098  235 HDYLLPRDVLKaleKHGITGlAAVPPLWAQLAQldwpESAAPSLRYLTnSGGAmpRATLSRLRSFLPNARLFLMYGLTEA 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4141 SIVTSIWDEasdsLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPG- 4219
Cdd:TIGR03098  315 FRSTYLPPE----EVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGe 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4220 ----ERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQR- 4294
Cdd:TIGR03098  391 lhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGg 470
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 386647928  4295 -ELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:TIGR03098  471 eELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
7443-7928 1.33e-64

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 231.72  E-value: 1.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7443 AREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGA 7522
Cdd:PRK07656    2 NEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7523 YVPIDPEYPEDRIRYMLEDSGAQVLLTQ-----------------RHLQEC-----VSFDGKVIAADDEQAYGEdGSNLE 7580
Cdd:PRK07656   82 VVPLNTRYTADEAAYILARGDAKALFVLglflgvdysattrlpalEHVVICeteedDPHTEKMKTFTDFLAAGD-PAERA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7581 PVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQfASLSFDASCWE--IFKALFFGATLYIP 7658
Cdd:PRK07656  161 PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLA-ANPFFHVFGYKagVNAPLMRGATILPL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7659 AK---DTILDypLFESYmnenGITAAILPPT--YAIYLSPDR----LPSLKKLITGGSAASVEFVQQWKDKVRYF---NA 7726
Cdd:PRK07656  240 PVfdpDEVFR--LIETE----RITVLPGPPTmyNSLLQHPDRsaedLSSLRLAVTGAASMPVALLERFESELGVDivlTG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7727 YGPTEASIVTSVwaaSPDGLDLRSVP--IGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVD 7804
Cdd:PRK07656  314 YGLSEASGVTTF---NRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDA 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7805 NPFLagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVAD 7884
Cdd:PRK07656  391 DGWL------HTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLK 464
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 386647928 7885 R--ELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK07656  465 PgaELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
6520-6950 1.61e-64

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 228.45  E-value: 1.61e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6520 EIGLTPIQRW-FFDQSLADL-HHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFrKSENGyAAWNRAIGEGELYS 6597
Cdd:cd19066     1 KIPLSPMQRGmWFLKKLATDpSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAG-RYEQVVLDKTVRFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6598 LEVADFRDVKSAEQAVEAKANEIQSSI-DLEVGPLFKAGLFQCAD-GDHLLLVIHHGVVDGVSWRILLEDVALGYEQAAK 6675
Cdd:cd19066    79 IEIIDLRNLADPEARLLELIDQIQQTIyDLERGPLVRVALFRLADeRDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6676 GEEVrLPAKTDSFRTWSEQLAAYAQSPAMENERAYW-EQIAQTA-VAPLPKDKqsdRSLQQDSESI--TIQWSRKETEQL 6751
Cdd:cd19066   159 QKPT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWtSYLHGLPpPLPLPKAK---RPSQVASYEVltLEFFLRSEETKR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6752 LKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGResimTDIDITRTVGWFTSKYPVLLQMEPGRSLSTRIKK 6831
Cdd:cd19066   235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6832 VKEDLRRIPNKGIGYG--LCRYLSAQPdGTVWGAEPEISFNYLGQFDQDLSNNDIGLspysSGLEMSDRQARSFILDING 6909
Cdd:cd19066   311 TKEQSREAIEHQRVPFieLVRHLGVVP-EAPKHPLFEPVFTFKNNQQQLGKTGGFIF----TTPVYTSSEGTVFDLDLEA 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 386647928 6910 MI-TDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAHC 6950
Cdd:cd19066   386 SEdPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
6989-7413 2.52e-64

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 227.19  E-value: 2.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6989 IYTLTPMQKGMwFHTALdKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNF-FSGPRGEPLQIVYRDKRIGF 7067
Cdd:cd19542     1 IYPCTPMQEGM-LLSQL-RSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSLDPPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7068 VyedlsHLPADErqASVERLEQEDIARGFDLEQdALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYeayv 7147
Cdd:cd19542    79 E-----EVETDE--DSLDALTRDLLDDPTLFGQ-PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7148 QGDRPEQkaAPAYSQYIEWLENQDSAAASAYWSNYLAGYEGqTALPQEKAQKRSEGYVAEHVVCeldkelSERMNRAAKQ 7227
Cdd:cd19542   147 NGQLLPP--APPFSDYISYLQSQSQEESLQYWRKYLQGASP-CAFPSLSPKRPAERSLSSTRRS------LAKLEAFCAS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7228 CRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALESG 7307
Cdd:cd19542   218 LGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7308 RYDFYPLYEIQTQSAQK--QELINHLLVFENYPMDEQVEQAGGDDSGTLSITDvdvaeHTNYNFTVTVFP-GDEIVVRFD 7384
Cdd:cd19542   298 PHQHLSLREIQRALGLWpsGTLFNTLVSYQNFEASPESELSGSSVFELSAAED-----PTEYPVAVEVEPsGDSLKVSLA 372
                         410       420
                  ....*....|....*....|....*....
gi 386647928 7385 YNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19542   373 YSTSVLSEEQAEELLEQFDDILEALLANP 401
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
5936-6422 2.98e-64

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 230.82  E-value: 2.98e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5936 TIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPI 6015
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6016 DPDYPEDRIRYMLEDSGAKLLLVQGHLLDRASFAD-------KLVNLNDDGAYHEDGSNLEPVNGPEHLTY--------- 6079
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALpgchdlrTLIIVGDPAHASEGHPGEEPASWPKLLALgdadpphpv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6080 -------VIYTSGTTGRPKGVMVEHRNVVRLVKN-TNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETI 6151
Cdd:TIGR03098  161 idsdmaaILYTSGSTGRPKGVVLSHRNLVAGAQSvATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6152 LDAVSlknAIQQYGINTMWLTAPLYNQLSQQD--SGMFAGLKTLIVGGDVLSvPHINRVLREHAGLS-IVNGYGPTEntT 6228
Cdd:TIGR03098  241 RDVLK---ALEKHGITGLAAVPPLWAQLAQLDwpESAAPSLRYLTNSGGAMP-RATLSRLRSFLPNArLFLMYGLTE--A 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6229 FSTTHTIVGE-QKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKF------VESSFLP 6301
Cdd:TIGR03098  315 FRSTYLPPEEvDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrplppfPGELHLP 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6302 GERCYrTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQK-QLCAYFVAEREL 6379
Cdd:TIGR03098  395 ELAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQAiVLVVTPPGGEEL 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 386647928  6380 TIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPA 6422
Cdd:TIGR03098  474 DRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1901-2312 3.35e-64

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 227.47  E-value: 3.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1901 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN-GEPVQRVYKEVNFAVEH 1979
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGlGEPLQVVLKDRKLPWRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1980 YR---TSEAEAGEVVRGFV-----RTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLY----NG 2047
Cdd:cd19543    82 LDlshLSEAEQEAELEALAeedreRGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYaalgEG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2048 E--SLATLRiQYKDYAVWqqseeqLERVKRQEA--YWLDMFRG--ELPVLemPTDYPRPAVRRFEGSTLSFRLDAGLNEA 2121
Cdd:cd19543   162 QppSLPPVR-PYRDYIAW------LQRQDKEAAeaYWREYLAGfeEPTPL--PKELPADADGSYEPGEVSFELSAELTAR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2122 LKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRtHGDL---QPLIGMFVNTLAIRNYPAGGKTFRSFLEEV 2198
Cdd:cd19543   233 LQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAELpgiETMVGLFINTLPVRVRLDPDQTVLELLKDL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2199 KETTLGAYEHQTYPfeeLVEkLQvPRDLSRNPIFDAMFVLQN-----TENEELQLDGLKLAPyPSGNTIARFDLTLDVTE 2273
Cdd:cd19543   312 QAQQLELREHEYVP---LYE-IQ-AWSEGKQALFDHLLVFENypvdeSLEEEQDEDGLRITD-VSAEEQTNYPLTVVAIP 385
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 386647928 2274 tGSGLECNLEYATSLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19543   386 -GEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
3854-4337 2.37e-63

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 227.86  E-value: 2.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3854 QTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIP 3933
Cdd:PRK07656    5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3934 IDPEYPEDRIRYMLEDSGAQALLTQRHL-------RERVSFAGTFVAVDDEQAY--------------HADGSNLEPVVG 3992
Cdd:PRK07656   85 LNTRYTADEAAYILARGDAKALFVLGLFlgvdysaTTRLPALEHVVICETEEDDphtekmktftdflaAGDPAERAPEVD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3993 PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQfASLSFDASCWE--IFKALFFGATLYI----- 4065
Cdd:PRK07656  165 PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLA-ANPFFHVFGYKagVNAPLMRGATILPlpvfd 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4066 PTSTtildyplFESYMNENgitATILP--PTYAAYL------NPDRMPSLKKLITGGSAASVEFVQQWKDK-----VLyf 4132
Cdd:PRK07656  244 PDEV-------FRLIETER---ITVLPgpPTMYNSLlqhpdrSAEDLSSLRLAVTGAASMPVALLERFESElgvdiVL-- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4133 NAYGPTEASIVTSIwdeasDSLGD-RKSVP--IGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAE 4209
Cdd:PRK07656  312 TGYGLSEASGVTTF-----NRLDDdRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4210 KfVDnpfepGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAY 4289
Cdd:PRK07656  387 A-ID-----ADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAY 460
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 4290 FVAQR--ELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK07656  461 VVLKPgaELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
2372-2831 1.13e-62

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 226.25  E-value: 1.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2372 TYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRR 2451
Cdd:cd17647    22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVIRA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2452 lqervsfAGTVvtvddeqayagdgsnlesaVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQ 2531
Cdd:cd17647   102 -------AGVV-------------------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2532 FASLSFDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITTATLPPTYAVYLNPDHMPDFKRLIAAGSASSLE 2611
Cdd:cd17647   156 LSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDIL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2612 L------LQQWKDKVKYFNAYGPTEDSICTTIW-TPSTED----ISQLKSV-PIGGPIVNHRIYIVDAH--YQPVPVGVA 2677
Cdd:cd17647   236 TkrdclrLQTLAENVRIVNMYGTTETQRAVSYFeVPSRSSdptfLKNLKDVmPAGRGMLNVQLLVVNRNdrTQICGIGEV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2678 GELCIAGVGLARGYLNRPDLTAEKFVDNPF-EPG---------------------ERMYRTGDLAKWLPDGTIEYLGRID 2735
Cdd:cd17647   316 GEIYVRAGGLAEGYRGLPELNKEKFVNNWFvEPDhwnyldkdnnepwrqfwlgprDRLYRTGDLGRYLPNGDCECCGRAD 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2736 HQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVA-------------------DRTMTVG------ 2790
Cdd:cd17647   396 DQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPrfdkpddesfaqedvpkevSTDPIVKgligyr 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 2791 ----ELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALPAP 2831
Cdd:cd17647   476 klikDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
2346-2828 1.14e-62

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 225.94  E-value: 1.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI 2425
Cdd:PRK07656    6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2426 DPEYPEDRISYMLEDSSAQVLLAQ-------RRLQERVSFAGTVVTVDDEQAYA--------------GDGSNLESAVGP 2484
Cdd:PRK07656   86 NTRYTADEAAYILARGDAKALFVLglflgvdYSATTRLPALEHVVICETEEDDPhtekmktftdflaaGDPAERAPEVDP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2485 NDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQ----FASLSFDASCWEVFQTlffGATLYIPTK- 2559
Cdd:PRK07656  166 DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAGVNAPLMR---GATILPLPVf 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2560 --ETILdyqwfeRYMSDNGITTATLPPT--YAVYLNPDHMP-DFK--RLIAAGSAS-SLELLQQWKDKvkyFN------A 2625
Cdd:PRK07656  243 dpDEVF------RLIETERITVLPGPPTmyNSLLQHPDRSAeDLSslRLAVTGAASmPVALLERFESE---LGvdivltG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2626 YGPTEDSICTTIWTPSTEdisqLKSVP--IGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKfV 2703
Cdd:PRK07656  314 YGLSEASGVTTFNRLDDD----RKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA-I 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2704 DnpfepGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVA 2783
Cdd:PRK07656  389 D-----ADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVL 463
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 2784 DRTMTVGE--LRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK07656  464 KPGAELTEeeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
284-750 1.63e-62

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 225.86  E-value: 1.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  284 RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLs 363
Cdd:cd17647    19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  364 qghlqervsfsgtwirlddeeayhedgsNLES---VNGPEHLTYVIYTSGTTGKPKGNLTTHRNIirvvknTNYID---- 436
Cdd:cd17647    98 ----------------------------VIRAagvVVGPDSNPTLSFTSGSEGIPKGVLGRHFSL------AYYFPwmak 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  437 ---VTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLV---DMNPD 510
Cdd:cd17647   144 rfnLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTaqaTTPFP 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  511 CLRHAraiLFGGERVSVSHVRKaLGHLGPG-KIKHVYGPTEsTVFATSY--------DVHEVEEGAVSIPIGGPISNTAI 581
Cdd:cd17647   224 KLHHA---FFVGDILTKRDCLR-LQTLAENvRIVNMYGTTE-TQRAVSYfevpsrssDPTFLKNLKDVMPAGRGMLNVQL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  582 YIVNA--QNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFA----------------------PGERMYRTGD 637
Cdd:cd17647   299 LVVNRndRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwlgPRDRLYRTGD 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  638 LARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPA--------- 708
Cdd:cd17647   379 LGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDdesfaqedv 458
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  709 --------------------NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAP 750
Cdd:cd17647   459 pkevstdpivkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
2351-2825 1.89e-62

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 222.87  E-value: 1.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2351 FEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYP 2430
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2431 EDRISYMLEDSSAQVLLaqrrlqervsfagtvvtvddeqayagdgsnlesavgpNDLAYIIYTSGTTGKPKGVMVEHHgl 2510
Cdd:cd17631    81 PPEVAYILADSGAKVLF-------------------------------------DDLALLMYTSGTTGRPKGAMLTHR-- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2511 cslkQMFANT------LQINAQDRVVQFASLS--FDASCWeVFQTLFFGATLYIPTK---ETILDYqwFERYmsdnGITT 2579
Cdd:cd17631   122 ----NLLWNAvnalaaLDLGPDDVLLVVAPLFhiGGLGVF-TLPTLLRGGTVVILRKfdpETVLDL--IERH----RVTS 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2580 ATLPPT--YAVYLNPD----HMPDFKRLIAAGSASSLELLQQWKDK-VKYFNAYGPTEDSICTTIWTPstED-ISQLKSV 2651
Cdd:cd17631   191 FFLVPTmiQALLQHPRfattDLSSLRAVIYGGAPMPERLLRALQARgVKFVQGYGMTETSPGVTFLSP--EDhRRKLGSA 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2652 piGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermyRTGDLAKWLPDGTIEYL 2731
Cdd:cd17631   269 --GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIV 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2732 GRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVAD--RTMTVGELRGELSGELPGYMIPAHF 2809
Cdd:cd17631   340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRpgAELDEDELIAHCRERLARYKIPKSV 419
                         490
                  ....*....|....*.
gi 386647928 2810 VQLERMPLTPNGKIDR 2825
Cdd:cd17631   420 EFVDALPRNATGKILK 435
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
3397-3821 2.68e-62

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 221.41  E-value: 2.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3397 IYALTPMQKGMwFHNTLnRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGW-RGEPLQIVYRYKPVEF 3475
Cdd:cd19542     1 IYPCTPMQEGM-LLSQL-RSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSaEGTFLQVVLKSLDPPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3476 ayEDLRHLAEAewsayLDQLVNDDKTRGFDLEQdALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYeayl 3555
Cdd:cd19542    79 --EEVETDEDS-----LDALTRDLLDDPTLFGQ-PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3556 rNDLSERPAaPSYSHYIEWLEKQDMEAAARYWTGFLAGYdSQTTLPQGKlhnkdgeyTEANILRSLgkSLTERMS----R 3631
Cdd:cd19542   147 -NGQLLPPA-PPFSDYISYLQSQSQEESLQYWRKYLQGA-SPCAFPSLS--------PKRPAERSL--SSTRRSLakleA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3632 IAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQEAA 3711
Cdd:cd19542   214 FCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQY 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3712 LESGGYDYYPLYEIQAQSAQK--QDLITHIMAFENFPMDEQIEQAGSyedgkLAITDVDIAEQTNYDFTL-VVMPGEELA 3788
Cdd:cd19542   294 LRSLPHQHLSLREIQRALGLWpsGTLFNTLVSYQNFEASPESELSGS-----SVFELSAAEDPTEYPVAVeVEPSGDSLK 368
                         410       420       430
                  ....*....|....*....|....*....|...
gi 386647928 3789 VRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19542   369 VSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
PRK05691 PRK05691
peptide synthase; Validated
2341-3188 8.89e-62

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 238.91  E-value: 8.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2341 YEADKTIHQLFEEQAERIPDHPAVVF------EGQQLTYRELNERANRLARTLQALGVKTDQPVgLMLERSLEMVVGMFA 2414
Cdd:PRK05691    5 FELPLTLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2415 VLKAGGAYVPIDP-----EYPEDRISYMLEDSSAQVLLAQRRLQE--------RVSFAGTVVTVDDEQAYAGDGSNlESA 2481
Cdd:PRK05691   84 CLYAGVIAVPAYPpesarRHHQERLLSIIADAEPRLLLTVADLRDsllqmeelAAANAPELLCVDTLDPALAEAWQ-EPA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2482 VGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQI--NAQDRVVQFASLSFDAS-CWEVFQTLFFGATLYIPT 2558
Cdd:PRK05691  163 LQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdlNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2559 KETILD--YQWFERYMSDNGitTATLPPTYAVYLNPDHMP-------DFKRLIAAGSASS---LELLQQWKDKV------ 2620
Cdd:PRK05691  243 PAYFLErpLRWLEAISEYGG--TISGGPDFAYRLCSERVSesalerlDLSRWRVAYSGSEpirQDSLERFAEKFaacgfd 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2621 --KYFNAYGPTEDSICTTIWTPST---------EDISQLKSVPIGGPIV--------NHRIYIVD-AHYQPVPVGVAGEL 2680
Cdd:PRK05691  321 pdSFFASYGLAEATLFVSGGRRGQgipaleldaEALARNRAEPGTGSVLmscgrsqpGHAVLIVDpQSLEVLGDNRVGEI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2681 CIAGVGLARGYLNRPDLTAEKFVDNpfePGERMYRTGDLAkWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASV 2760
Cdd:PRK05691  401 WASGPSIAHGYWRNPEASAKTFVEH---DGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEV 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2761 ---------------QEAIVIAHD-DASGQKQLCAYFVADRT-MTVGELRGElsgelpgymIPAHFVQLE--RMPLTPNG 2821
Cdd:PRK05691  477 vrkgrvaafavnhqgEEGIGIAAEiSRSVQKILPPQALIKSIrQAVAEACQE---------APSVVLLLNpgALPKTSSG 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2822 KIDRKALPA-------------PQGNASAGADYVAPRSEEEKVLADVWQAVLGAERVGATDHFFELGGDSIKSIQVSSRL 2888
Cdd:PRK05691  548 KLQRSACRLrladgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARL 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2889 HQA-GYKLEIRDLFKYPTVAQLSKHirpVARM-ADQGEVSGDVSLTPIQH--------------WFFEPQFAEphhFNQS 2952
Cdd:PRK05691  628 RDElGIDLNLRQLFEAPTLAAFSAA---VARQlAGGGAAQAAIARLPRGQalpqslaqnrlwllWQLDPQSAA---YNIP 701
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2953 VMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFhkSENGYTAWNRAIGEGElYGLEVVDLKGI---EESAQAVEAKANEIQ 3029
Cdd:PRK05691  702 GGLHLRGELDEAALRASFQRLVERHESLRTRF--YERDGVALQRIDAQGE-FALQRIDLSDLpeaEREARAAQIREEEAR 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3030 SSIDLEAGPFVKAGLFQCADGDHLLIV-IHHGVVDGVSWRILLEDLAIGYEQAVKGEELRF---PAKTDAYRTWSEQLAA 3105
Cdd:PRK05691  779 QPFDLEKGPLLRVTLVRLDDEEHQLLVtLHHIVADGWSLNILLDEFSRLYAAACQGQTAELaplPLGYADYGAWQRQWLA 858
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3106 YAQSpviERELAYWKRVAQTEVQPL------PKDEQVDVSLQQDSESISIEWTREeteqlLKGVHRAYNTEMNDILLAAL 3179
Cdd:PRK05691  859 QGEA---ARQLAYWKAQLGDEQPVLelatdhPRSARQAHSAARYSLRVDASLSEA-----LRGLAQAHQATLFMVLLAAF 930

                  ....*....
gi 386647928 3180 GMAVQKWSG 3188
Cdd:PRK05691  931 QALLHRYSG 939
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1303-1792 1.02e-61

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 220.56  E-value: 1.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1303 FEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 1382
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLEDSAASVLLtqthlqeraqqwgqtlqavlclddeaayaedasnvanvnepHDLAYVIYTSGTTGRPKGVMIE 1462
Cdd:cd17631    81 PPEVAYILADSGAKVLF-----------------------------------------DDLALLMYTSGTTGRPKGAMLT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1463 HRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTPA 1542
Cdd:cd17631   120 HRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPT 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1543 LIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERfgsQFRIINAYGVTEAAIDSSLY--DEPLAKLPEAGnvpi 1620
Cdd:cd17631   197 MIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR---GVKFVQGYGMTETSPGVTFLspEDHRRKLGSAG---- 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1621 gKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGR 1700
Cdd:cd17631   270 -RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDR 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1701 IDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAES--ELKLSELRSSLSQELPGYMIPSYFVQ 1778
Cdd:cd17631   342 KKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPgaELDEDELIAHCRERLARYKIPKSVEF 421
                         490
                  ....*....|....
gi 386647928 1779 LEQLPLTANGKIDR 1792
Cdd:cd17631   422 VDALPRNATGKILK 435
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
3397-3821 1.28e-61

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 219.88  E-value: 1.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3397 IYALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGWRGEPLQIVYR-----YK 3471
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDdlappWA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3472 PVEFAYEDLRHLAEaewsaYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTY 3551
Cdd:cd19547    81 LLDWSGEDPDRRAE-----LLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3552 EAYLRNDLSERPAAPSYSHYIEWLEKQDM--EAAARYWTGFLAGYDSQ--TTLPQgklhNKDGEYTeaNILRSLGKSLTE 3627
Cdd:cd19547   156 EELAHGREPQLSPCRPYRDYVRWIRARTAqsEESERFWREYLRDLTPSpfSTAPA----DREGEFD--TVVHEFPEQLTR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3628 RMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRV 3707
Cdd:cd19547   230 LVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3708 QEAALESGGYDYYPLYEIQAQSAQKQ----DLITHIMAFENFPMDEQIEqagsyEDGKLAITDVDIAEQTNYDFTLVVMP 3783
Cdd:cd19547   310 HRDLATTAAHGHVPLAQIKSWASGERlsggRVFDNLVAFENYPEDNLPG-----DDLSIQIIDLHAQEKTEYPIGLIVLP 384
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 386647928 3784 GEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19547   385 LQKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
7468-7923 2.41e-61

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 221.32  E-value: 2.41e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7468 ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVL 7547
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7548 LTQRHLQE-------CVSFDGKVIAADDEQAYGEDGSNL--------------EPVVGPNHLAYVIYTSGTTGKPKGVMV 7606
Cdd:cd05911    87 FTDPDGLEkvkeaakELGPKDKIIVLDDKPDGVLSIEDLlsptlgeededlppPLKDGKDDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7607 EHHGLCSLKLMFAETLRITEEDRVVQFASLSFD--ASCWEIFKALFFGATLYIPAKDtilDYPLFESYMNENGITAAILP 7684
Cdd:cd05911   167 SHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVIIMPKF---DSELFLDLIEKYKITFLYLV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7685 PTYAIYLS------PDRLPSLKKLITGGSAAS---VEFVQQWKDKVRYFNAYGPTEASIVTSVwaaSPDGLDLR-SVpiG 7754
Cdd:cd05911   244 PPIAAALAksplldKYDLSSLRVILSGGAPLSkelQELLAKRFPNATIKQGYGMTETGGILTV---NPDGDDKPgSV--G 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7755 RPIANHQIFIVDSQ-NHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGR 7833
Cdd:cd05911   319 RLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWL------HTGDIGYFDEDGYLYIVDR 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7834 IDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYM-----Ip 7906
Cdd:cd05911   393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrkPGEKLTEKEVKDYVAKKVASYKqlrggV- 471
                         490
                  ....*....|....*..
gi 386647928 7907 sYFVqlEQMPLTPNGKI 7923
Cdd:cd05911   472 -VFV--DEIPKSASGKI 485
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
5959-6423 2.76e-61

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 222.39  E-value: 2.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5959 KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRirymledsgaklllv 6038
Cdd:cd17647    19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--------------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6039 QGHLLDRASFAdKLVNLNDDGAyhedgsnlepVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVR----LVKNTNYVElNE 6114
Cdd:cd17647    84 QNIYLGVAKPR-GLIVIRAAGV----------VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYyfpwMAKRFNLSE-ND 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6115 QTHILQtgAVVFDASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTLI 6194
Cdd:cd17647   152 KFTMLS--GIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAF 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6195 VGGDVLSVPHINRVLREHAGLSIVNGYGPTEN---------TTFSTTHTIVGEQKEAVPIGKPINNSTAYIVD--SKLSL 6263
Cdd:cd17647   230 FVGDILTKRDCLRLQTLAENVRIVNMYGTTETqravsyfevPSRSSDPTFLKNLKDVMPAGRGMLNVQLLVVNrnDRTQI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6264 LPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFL----------------------PGERCYRTGDLARWLPDGTLE 6321
Cdd:cd17647   310 CGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwlgPRDRLYRTGDLGRYLPNGDCE 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6322 YKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE------------------------- 6376
Cdd:cd17647   390 CCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRfdkpddesfaqedvpkevstdpivk 469
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 6377 -----RELtIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPAP 6423
Cdd:cd17647   470 gligyRKL-IKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
8035-8410 3.66e-61

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 218.48  E-value: 3.66e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8035 PVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGF--EMANGEPVQRVYSDVEFAVEY 8112
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 SK-ADREEAVEIAQRFV-RPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGEELPPLRIQY 8190
Cdd:cd19532    83 VQiSDEAEVEEEFERLKnHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8191 KDYAAWQRSEAYAKRVKQQEGYW---LQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELAARHESTLY 8267
Cdd:cd19532   163 LDFAARQRQDYESGALDEDLAYWkseFSTLPEPLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVTPF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8268 MVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFE 8347
Cdd:cd19532   243 HFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFD 322
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 8348 ELVERLNVKRDASRNPVFDTMF--VLQNTEDRGIEADAFSLTPFVFDQTVaaqFDLTLSVAEDDG 8410
Cdd:cd19532   323 VLLDELGVPRSATHSPLFQVFInyRQGVAESRPFGDCELEGEEFEDARTP---YDLSLDIIDNPD 384
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
5936-6420 5.93e-61

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 220.93  E-value: 5.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPI 6015
Cdd:PRK07656    6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6016 DPDYPEDRIRYMLEDSGAKLLLVQGHLL-------DRASFADKLVNLNDDGAYHED------------GSNLEPVNG--P 6074
Cdd:PRK07656   86 NTRYTADEAAYILARGDAKALFVLGLFLgvdysatTRLPALEHVVICETEEDDPHTekmktftdflaaGDPAERAPEvdP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6075 EHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNT-NYVELNEQTHILqtgAV-----VFdASTFEIWGALLNGGRLYVVRn 6148
Cdd:PRK07656  166 DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWaEYLGLTEGDRYL---AAnpffhVF-GYKAGVNAPLMRGATILPLP- 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6149 etILDAVSLKNAIQQYGInTMWLTAP-LYNQLSQQDSGMFAGLKTL---IVGGDVLSVPHINRVlREHAGLSIV-NGYGP 6223
Cdd:PRK07656  241 --VFDPDEVFRLIETERI-TVLPGPPtMYNSLLQHPDRSAEDLSSLrlaVTGAASMPVALLERF-ESELGVDIVlTGYGL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6224 TENTTFsTTHTIVGEQKEAVP--IGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLp 6301
Cdd:PRK07656  317 SEASGV-TTFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWL- 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6302 gercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAER--EL 6379
Cdd:PRK07656  395 -----HTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPgaEL 469
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928 6380 TIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK07656  470 TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
3879-4332 6.65e-61

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 220.16  E-value: 6.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3879 QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQ 3958
Cdd:cd05911    10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3959 RHLRERVSFAGTFVA-------VDDEQAYHADGSNL--------------EPVVGPNHLAYVIYTSGTTGKPKGVMVEHH 4017
Cdd:cd05911    90 PDGLEKVKEAAKELGpkdkiivLDDKPDGVLSIEDLlsptlgeededlppPLKDGKDDTAAILYSSGTTGLPKGVCLSHR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4018 GLCSLKLMFANTLQMTEQDRVVQFASLSFD--ASCWEIFKALFFGATLYIptsTTILDYPLFESYMNENGITATILPPTY 4095
Cdd:cd05911   170 NLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVII---MPKFDSELFLDLIEKYKITFLYLVPPI 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4096 AAYL------NPDRMPSLKKLITGGSAAS---VEFVQQWKDKVLYFNAYGPTEASIVTSIWDEASDSLGdrkSVpiGRPL 4166
Cdd:cd05911   247 AAALakspllDKYDLSSLRVILSGGAPLSkelQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPG---SV--GRLL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4167 ANHRIYVVDSH-NRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDH 4245
Cdd:cd05911   322 PNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIVDRKKE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4246 QVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV--AQRELTAAELRATMSQELPNYM-----IpsYF 4318
Cdd:cd05911   396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrkPGEKLTEKEVKDYVAKKVASYKqlrggV--VF 473
                         490
                  ....*....|....
gi 386647928 4319 VQlaQMPLTPNGKI 4332
Cdd:cd05911   474 VD--EIPKSASGKI 485
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
4893-5382 1.29e-60

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 217.48  E-value: 1.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4893 FEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 4972
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLEDSAASVLLtqthlqeraqqwgqtlqaalclddeaayaedasnvanvnepHDLAYVIYTSGTTGRPKGVMIE 5052
Cdd:cd17631    81 PPEVAYILADSGAKVLF-----------------------------------------DDLALLMYTSGTTGRPKGAMLT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5053 HRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTPA 5132
Cdd:cd17631   120 HRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPT 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5133 LIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERfgsQFRIINAYGVTEAAIDSSLY--DEPLAKLPEAGnvpi 5210
Cdd:cd17631   197 MIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR---GVKFVQGYGMTETSPGVTFLspEDHRRKLGSAG---- 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5211 gKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGR 5290
Cdd:cd17631   270 -RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDR 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5291 IDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAHFTAE-SELKLSELRSSLSQELPGYMIPSYFVQ 5368
Cdd:cd17631   342 KKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEAVVAVVVPRPgAELDEDELIAHCRERLARYKIPKSVEF 421
                         490
                  ....*....|....
gi 386647928 5369 LEQLPLTANGKIDR 5382
Cdd:cd17631   422 VDALPRNATGKILK 435
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
8035-8429 3.01e-60

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 216.36  E-value: 3.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8035 PVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY-- 8112
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVid 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 --SKADREEAVE--IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLY----AGEEL- 8183
Cdd:cd20483    83 lsEAADPEAALDqlVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDLa 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8184 --PPLRIQYKDYAAWQRSEAYAKRVKQQEGYWLQTLAGELPVIEL----------PTDYERtstrsfegAELEFEADEAL 8251
Cdd:cd20483   163 tvPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKLlpfakaerppVKDYER--------STVEATLDKEL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8252 TQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEV 8331
Cdd:cd20483   235 LARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLEST 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8332 KETTLGAFEHQDYPFEELVERLNVKRDASRNPVFDTMFVLQ--------NTEDrgieadaFSLTPFVFDQtVAAQFDLTL 8403
Cdd:cd20483   315 KTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvhgkfpeyDTGD-------FKFTDYDHYD-IPTACDIAL 386
                         410       420
                  ....*....|....*....|....*...
gi 386647928 8404 SVAED-DGAIRGSFQYAAKLF-KATMIR 8429
Cdd:cd20483   387 EAEEDpDGGLDLRLEFSTTLYdSADMER 414
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
5938-6420 3.58e-60

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 220.37  E-value: 3.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5938 HQLFEEQAERIPDHLAVTFED-----KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAY 6012
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6013 VPIDPDYPEDRIRYMLEDSGAKLLLV------QGHLLDRASFADKL-------------------VNLNDDGAYHE---- 6063
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITadgglrGGKVIDLKEKVDEAleelpslehvivvgrtgadVPMEGDLDWDEllaa 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6064 DGSNLEPVN-GPEHLTYVIYTSGTTGRPKGVMVEHRNV-VRLVKNTNYVeLNeqthiLQTGAVVFDASTF--------EI 6133
Cdd:COG0365   172 ASAEFEPEPtDADDPLFILYTSGTTGKPKGVVHTHGGYlVHAATTAKYV-LD-----LKPGDVFWCTADIgwatghsyIV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6134 WGALLNGGRLyVVRNETIL--DAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAG-----LKTLIVGGDVLSVPHIN 6206
Cdd:COG0365   246 YGPLLNGATV-VLYEGRPDfpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydlssLRLLGSAGEPLNPEVWE 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6207 RVlREHAGLSIVNGYGPTEnttfsTTHTIVG--EQKEAVP--IGKPINNSTAYIVDSKLSLLPVGVWGELIVGGD--GVA 6280
Cdd:COG0365   325 WW-YEAVGVPIVDGWGQTE-----TGGIFISnlPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6281 RGYLNRPELTAEKFVesSFLPGerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVR 6360
Cdd:COG0365   399 RGYWNDPERYRETYF--GRFPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGV 474
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6361 EDESGQKQLCAYFV-----AERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:COG0365   475 PDEIRGQVVKAFVVlkpgvEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
5931-6420 4.04e-60

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 218.90  E-value: 4.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5931 YPSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGG 6010
Cdd:PRK06187    2 QDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6011 AYVPIDPDYPEDRIRYMLEDSGAKLLLVQGHL-------LDRASFADKLVNLNDDGAYHEDGSNLE--------PVNGP- 6074
Cdd:PRK06187   82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFvpllaaiLPQLPTVRTVIVEGDGPAAPLAPEVGEyeellaaaSDTFDf 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6075 ----EHLTYV-IYTSGTTGRPKGVMVEHRNvvrLVKNTNYVElneqTHILQTGAVVFDAST--FEI--WG----ALLNGG 6141
Cdd:PRK06187  162 pdidENDAAAmLYTSGTTGHPKGVVLSHRN---LFLHSLAVC----AWLKLSRDDVYLVIVpmFHVhaWGlpylALMAGA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6142 RLYVVRN---ETILDAVSLKNAIQQYGINTMW---LTAPLynqLSQQDsgmFAGLKTLIVGGDVLSvPHINRVLREHAGL 6215
Cdd:PRK06187  235 KQVIPRRfdpENLLDLIETERVTFFFAVPTIWqmlLKAPR---AYFVD---FSSLRLVIYGGAALP-PALLREFKEKFGI 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6216 SIVNGYGPTENT---TFST-THTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPV--GVWGELIVGGDGVARGYLNRPEL 6289
Cdd:PRK06187  308 DLVQGYGMTETSpvvSVLPpEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEA 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6290 TAEKFVESsflpgerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQL 6369
Cdd:PRK06187  388 TAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERP 460
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 6370 CAYFVAE--RELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK06187  461 VAVVVLKpgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1301-1795 7.00e-60

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 216.28  E-value: 7.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1301 ALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 1380
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1381 YPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAVlclddeaayaedasnvanVNEPHDLAYVIYTSGTTGRPKGVM 1460
Cdd:cd05936    83 YTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERV------------------ALTPEDVAVLQYTSGTTGVPKGAM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1461 IEHRSLV-NTAAGYRREYRLDQFPVRLLQLASFsFDVFvgdiART------LYNGGTMVICPkddRIDPARLHYWISEEK 1533
Cdd:cd05936   145 LTHRNLVaNALQIKAWLEDLLEGDDVVLAALPL-FHVF----GLTvalllpLALGATIVLIP---RFRPIGVLKEIRKHR 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1534 ITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAidsslydePLAKL- 1612
Cdd:cd05936   217 VTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTG--VPIVEGYGLTETS--------PVVAVn 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1613 -PEAGNVP--IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARW 1689
Cdd:cd05936   287 pLDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYM 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1690 MPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLS--ELRSSLSQEL 1767
Cdd:cd05936   360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTeeEIIAFCREQL 439
                         490       500
                  ....*....|....*....|....*...
gi 386647928 1768 PGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05936   440 AGYKVPRQVEFRDELPKSAVGKILRREL 467
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
261-749 1.51e-59

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 216.96  E-value: 1.51e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   261 TIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPI 340
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   341 DPEYPEERIRYMLEDSGTQVLLSQghlQERVSF----------SGTWIRLDDEEAYHEDGSNLESVNGPEHLTY------ 404
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTS---SERLDLlhpalpgchdLRTLIIVGDPAHASEGHPGEEPASWPKLLALgdadpp 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   405 ----------VIYTSGTTGKPKGNLTTHRNIIRVVKN-TNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPK 473
Cdd:TIGR03098  158 hpvidsdmaaILYTSGSTGRPKGVVLSHRNLVAGAQSvATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDY 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   474 ETVLDVAKlagLIEKQQISVMFITTAFFNVL--VDMNPDCLRHARAILFGGERV---SVSHVRKALGHlgpGKIKHVYGP 548
Cdd:TIGR03098  238 LLPRDVLK---ALEKHGITGLAAVPPLWAQLaqLDWPESAAPSLRYLTNSGGAMpraTLSRLRSFLPN---ARLFLMYGL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   549 TEStvFATSY-DVHEVEEGAVSipIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFA 627
Cdd:TIGR03098  312 TEA--FRSTYlPPEEVDRRPDS--IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPF 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   628 PG-----ERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEK-QLCAYY 700
Cdd:TIGR03098  388 PGelhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQAiVLVVTP 467
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 386647928   701 VADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPA 749
Cdd:TIGR03098  468 PGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1902-2312 1.72e-59

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 214.27  E-value: 1.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1902 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYR 1981
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1982 TSEAEA---GEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGE------SLAT 2052
Cdd:cd19546    86 VPATEEelpALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrapERAP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2053 LRIQYKDYAVWQQ-----SEEQLERVKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRFEGSTLSFRLDAGLNEALKRVAA 2127
Cdd:cd19546   166 LPLQFADYALWERellagEDDRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2128 ESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRT-HGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAY 2206
Cdd:cd19546   246 SAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREAR 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2207 EHQTYPFEELVEKLQVPRDLSRNPIFDAMFVLQNTEN---EELQLDGLKLAPYPSGNTIARFDLTLDVTET------GSG 2277
Cdd:cd19546   326 RHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNdpwDAPELPGLRTSPVPLGTEAMELDLSLALTERrnddgdPDG 405
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 386647928 2278 LECNLEYATSLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19546   406 LDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
5941-6417 1.76e-59

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 214.01  E-value: 1.76e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5941 FEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYP 6020
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6021 EDRIRYMLEDSGAKLLLvqghlldrasfadklvnlnDDGAYhedgsnlepvngpehltyVIYTSGTTGRPKGVMVEHRNV 6100
Cdd:cd17631    81 PPEVAYILADSGAKVLF-------------------DDLAL------------------LMYTSGTTGRPKGAMLTHRNL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6101 VRLVKNTNY-VELNEQ---------THILQTGAVVFdastfeiwGALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTMW 6170
Cdd:cd17631   124 LWNAVNALAaLDLGPDdvllvvaplFHIGGLGVFTL--------PTLLRGGTVVILRK---FDPETVLDLIERHRVTSFF 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6171 LTAPLYNQLSQQ---DSGMFAGLKTLIVGGDVLSVPHINRVLRehAGLSIVNGYGPTE---NTTF-STTHTIvgeqKEAV 6243
Cdd:cd17631   193 LVPTMIQALLQHprfATTDLSSLRAVIYGGAPMPERLLRALQA--RGVKFVQGYGMTEtspGVTFlSPEDHR----RKLG 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6244 PIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYK 6323
Cdd:cd17631   267 SAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIV 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6324 GRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAyFVAER---ELTIGELRAALSQELPNYMIPSH 6400
Cdd:cd17631   340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVA-VVVPRpgaELDEDELIAHCRERLARYKIPKS 418
                         490
                  ....*....|....*..
gi 386647928 6401 FVPLERMPLTPNGKIDR 6417
Cdd:cd17631   419 VEFVDALPRNATGKILK 435
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
6992-7233 2.12e-59

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 206.81  E-value: 2.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFhtaLDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGpRGEPLQIVYRDKRIGFVYED 7071
Cdd:COG4908     1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQRIDPDADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7072 LSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDR 7151
Cdd:COG4908    77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7152 PEQKAAPA-YSQYIEWLENQ----DSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAK 7226
Cdd:COG4908   157 PPLPELPIqYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236

                  ....*..
gi 386647928 7227 QCRVTVN 7233
Cdd:COG4908   237 AHGATVN 243
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
5961-6420 6.33e-59

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 213.10  E-value: 6.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQG 6040
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 HLLDRA-SFADKLVNLNddgayhedgsnlepVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVELNEQTHIL 6119
Cdd:cd17654    97 ELDNAPlSFTPEHRHFN--------------IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDIL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6120 Q-TGAVVFDASTFEIWGALLNGGRLYVVRNET-ILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMF-----AGLKT 6192
Cdd:cd17654   163 FlTSPLTFDPSVVEIFLSLSSGATLLIVPTSVkVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTvlsatSSLRV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6193 LIVGGDVLSVPHINRVLR-EHAGLSIVNGYGPTENTTFSTTHtIVGEQKEAVPIGKPINNSTAYIVDSKLSllpvGVWGE 6271
Cdd:cd17654   243 LALGGEPFPSLVILSSWRgKGNRTRIFNIYGITEVSCWALAY-KVPEEDSPVQLGSPLLGTVIEVRDQNGS----EGTGQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6272 LIVGgdGVARGYLNRPELTAekfVESSFlpgercYRTGDLARwLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVAS 6351
Cdd:cd17654   318 VFLG--GLNRVCILDDEVTV---PKGTM------RATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLG 385
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 6352 VkEATVIVREDesgQKQLCAYFVAEreltigELRAALSQEL-----PNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd17654   386 V-ESCAVTLSD---QQRLIAFIVGE------SSSSRIHKELqltllSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
255-747 7.49e-59

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 215.05  E-value: 7.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  255 DYPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAG 334
Cdd:PRK06187    1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  335 GAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHL-------QERVSFSGTWIRLDDEEAYHEDGSNLE----SVNGPEHLT 403
Cdd:PRK06187   81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFvpllaaiLPQLPTVRTVIVEGDGPAAPLAPEVGEyeelLAAASDTFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  404 YV----------IYTSGTTGKPKGNLTTHRNIirvVKNTN----YIDVTGQDKLLQLSSYsfdgstFDIFG------ALL 463
Cdd:PRK06187  161 FPdidendaaamLYTSGTTGHPKGVVLSHRNL---FLHSLavcaWLKLSRDDVYLVIVPM------FHVHAwglpylALM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  464 NGAKLVLvPKEtvLDVAKLAGLIEKQQISVMFITTAFFNVLVDmNPDC----LRHARAILFGGERVSVSHVRKALGHLGp 539
Cdd:PRK06187  232 AGAKQVI-PRR--FDPENLLDLIETERVTFFFAVPTIWQMLLK-APRAyfvdFSSLRLVIYGGAALPPALLREFKEKFG- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  540 GKIKHVYGPTEST---VFATsYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQP--IGVAGELCVAGDGLARGYLNRP 614
Cdd:PRK06187  307 IDLVQGYGMTETSpvvSVLP-PEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRP 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  615 DLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGE 693
Cdd:PRK06187  386 EATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgVPDEKWGE 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  694 KQLcAYYVA--DRSLPANEVRSTLSQELPAYMLPS--YFVqlEQMPLTTNGKVDRRAL 747
Cdd:PRK06187  459 RPV-AVVVLkpGATLDAKELRAFLRGRLAKFKLPKriAFV--DELPRTSVGKILKRVL 513
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
7460-7928 9.62e-59

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 212.72  E-value: 9.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFE----NTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:cd17654     1 PDRPALIIDqttsDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLLTQRHL-QECVSFDGKVIAADDEQAYGedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSL 7614
Cdd:cd17654    81 LTVMKKCHVSYLLQNKELdNAPLSFTPEHRHFNIRTDEC--------------LAYVIHTSGTTGTPKIVAVPHKCILPN 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7615 KLMFAETLRITEEDrVVQFAS-LSFDASCWEIFKALFFGATL-YIPAKDTILDYPLFESYMNENGITAAILPPT------ 7686
Cdd:cd17654   147 IQHFRSLFNITSED-ILFLTSpLTFDPSVVEIFLSLSSGATLlIVPTSVKVLPSKLADILFKRHRITVLQATPTlfrrfg 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7687 ----YAIYLSpdRLPSLKKLITGGSA-ASVEFVQQWK---DKVRYFNAYGPTEasivTSVWAASPDGLDLRS-VPIGRPI 7757
Cdd:cd17654   226 sqsiKSTVLS--ATSSLRVLALGGEPfPSLVILSSWRgkgNRTRIFNIYGITE----VSCWALAYKVPEEDSpVQLGSPL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7758 ANHQIFIVDSQNHmlpvGVAGELciSGAGLARGYLNRPELTAEKfvdnpflagERMYRTGDLARwLPDGNIEYLGRIDHQ 7837
Cdd:cd17654   300 LGTVIEVRDQNGS----EGTGQV--FLGGLNRVCILDDEVTVPK---------GTMRATGDFVT-VKDGELFFLGRKDSQ 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7838 VKIRGYRIELGEIEEQLLKIASVqETIVIARGDangQQQLCAYFVAD--RELTVSELRGTLsqeLPGYMIPSYFVQLEQM 7915
Cdd:cd17654   364 IKRRGKRINLDLIQQVIESCLGV-ESCAVTLSD---QQRLIAFIVGEssSSRIHKELQLTL---LSSHAIPDTFVQIDKL 436
                         490
                  ....*....|...
gi 386647928 7916 PLTPNGKIDRNAL 7928
Cdd:cd17654   437 PLTSHGKVDKSEL 449
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
261-747 9.82e-59

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 214.38  E-value: 9.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPI 340
Cdd:PRK07656    6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  341 DPEYPEERIRYMLEDSGTQVLLSQGHL-------QERVSFSGTWIRLDDEEAYHED------------GSNLESVNG--P 399
Cdd:PRK07656   86 NTRYTADEAAYILARGDAKALFVLGLFlgvdysaTTRLPALEHVVICETEEDDPHTekmktftdflaaGDPAERAPEvdP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  400 EHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNT-NYIDVTGQDKLLQLSSYsfdgstFDIFG-------ALLNGAKLVLV 471
Cdd:PRK07656  166 DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWaEYLGLTEGDRYLAANPF------FHVFGykagvnaPLMRGATILPL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  472 PketVLDVAKLAGLIEKQQISVMFITTAFFNVL---VDMNPDCLRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGP 548
Cdd:PRK07656  240 P---VFDPDEVFRLIETERITVLPGPPTMYNSLlqhPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  549 TESTVFATsydVHEVEEGAVSIP--IGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKF-ADNp 625
Cdd:PRK07656  317 SEASGVTT---FNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIdADG- 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  626 fapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEkQLCAYYVADR 704
Cdd:PRK07656  393 ------WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgVPDERLGE-VGKAYVVLKP 465
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 386647928  705 S--LPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK07656  466 GaeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
1299-1797 1.10e-58

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 214.65  E-value: 1.10e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1299 FHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 1378
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1379 PDYPSDRIQFMLEDSAASVLLT-------------QTHLQERAQQWGQTLQAVLCLDDEAAYA-EDASNVANVNEPH--- 1441
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVTsserldllhpalpGCHDLRTLIIVGDPAHASEGHPGEEPASwPKLLALGDADPPHpvi 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1442 --DLAYVIYTSGTTGRPKGVMIEHRSLVNTA---AGYRREYRLDqfpvRLLQLASFSFDVFVGDIARTLYNGGTMV---- 1512
Cdd:TIGR03098  162 dsDMAAILYTSGSTGRPKGVVLSHRNLVAGAqsvATYLENRPDD----RLLAVLPLSFDYGFNQLTTAFYVGATVVlhdy 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1513 ICPKDdridparLHYWISEEKITIFESTPALIIPF--MDYVAEhglDMSSMELLITSSDSCSVTDYRVLQERFgSQFRII 1590
Cdd:TIGR03098  238 LLPRD-------VLKALEKHGITGLAAVPPLWAQLaqLDWPES---AAPSLRYLTNSGGAMPRATLSRLRSFL-PNARLF 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1591 NAYGVTEAAIDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFV 1670
Cdd:TIGR03098  307 LMYGLTEAFRSTYLPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFR 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  1671 DSP-FVEGERLYRT----GDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQK-V 1743
Cdd:TIGR03098  383 PLPpFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTlGQAiV 462
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386647928  1744 LCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 1797
Cdd:TIGR03098  463 LVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7479-7928 1.53e-58

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 212.30  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7479 ERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGA----YVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQ 7554
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7555 E------CVSFDGKVIAADDEQAYGEDGSNLEPVVGPNhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEED 7628
Cdd:cd05922    81 DrlrdalPASPDPGTVLDADGIRAARASAPAHEVSHED-LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7629 RVVQFASLSFDASCWEIFKALFFGATLYIpAKDTILDYPLFESyMNENGITA-AILPPTYAIYLS----PDRLPSLKKLI 7703
Cdd:cd05922   160 RALTVLPLSYDYGLSVLNTHLLRGATLVL-TNDGVLDDAFWED-LREHGATGlAGVPSTYAMLTRlgfdPAKLPSLRYLT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7704 TGGSAASVEFVQQWKDKV---RYFNAYGPTEASIVTSVwaASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGEL 7780
Cdd:cd05922   238 QAGGRLPQETIARLRELLpgaQVYVMYGQTEATRRMTY--LPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEI 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7781 CISGAGLARGYLNRPELTAEKfvdnpfLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASV 7860
Cdd:cd05922   316 VHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7861 QETIVIARGDANGqQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05922   390 IEAAAVGLPDPLG-EKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
4889-5387 2.16e-58

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 213.49  E-value: 2.16e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4889 FHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 4968
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4969 PDYPSDRIQFMLEDSAASVLLT-------------QTHLQERAQQWGQTLQAALCLDDEAAYA-EDASNVANVNEPH--- 5031
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVTsserldllhpalpGCHDLRTLIIVGDPAHASEGHPGEEPASwPKLLALGDADPPHpvi 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5032 --DLAYVIYTSGTTGRPKGVMIEHRSLVNTA---AGYRREYRLDqfpvRLLQLASFSFDVFVGDIARTLYNGGTMV---- 5102
Cdd:TIGR03098  162 dsDMAAILYTSGSTGRPKGVVLSHRNLVAGAqsvATYLENRPDD----RLLAVLPLSFDYGFNQLTTAFYVGATVVlhdy 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5103 ICPKDdridparLHYWISEEKITIFESTPALII------------PFMDYVAEHGLDMSSMVLlitssdscsvtdyRVLQ 5170
Cdd:TIGR03098  238 LLPRD-------VLKALEKHGITGLAAVPPLWAqlaqldwpesaaPSLRYLTNSGGAMPRATL-------------SRLR 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5171 ERFgSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLN 5250
Cdd:TIGR03098  298 SFL-PNARLFLMYGLTEAFRSTYLPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWN 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5251 RPELTEEKFVDSP-FVEGERLYRT----GDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVR 5325
Cdd:TIGR03098  373 DPEKTAERFRPLPpFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGV 452
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928  5326 EDAK-GQK-VLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 5387
Cdd:TIGR03098  453 PDPTlGQAiVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1300-1795 2.74e-58

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 214.59  E-value: 2.74e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1300 HALFEKQAERTPEVAAVVYEND-----RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAY 1374
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1375 VPLDPDYPSDRIQFMLEDSAASVLLTQTHLQER------------AQQWGQTLQAVLCLDDEAA---------YAEDASN 1433
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITADGGLRGgkvidlkekvdeALEELPSLEHVIVVGRTGAdvpmegdldWDELLAA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1434 VANVNEPH-----DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYrreyrldqfpvrllqlASFSFDVFVGDI----ART 1504
Cdd:COG0365   172 ASAEFEPEptdadDPLFILYTSGTTGKPKGVVHTHGGYLVHAATT----------------AKYVLDLKPGDVfwctADI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1505 -------------LYNGGTMVICP-KDDRIDPARLhyW--ISEEKITIFESTPALIIPFM----DYVAEHglDMSSMELL 1564
Cdd:COG0365   236 gwatghsyivygpLLNGATVVLYEgRPDFPDPGRL--WelIEKYGVTVFFTAPTAIRALMkagdEPLKKY--DLSSLRLL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1565 ITSSDSCSVTDYRVLQERFGSQfrIINAYGVTE--AAIDSSLYDEPLaklpeagnVP--IGKAALNAKFYIVDAHLNPVP 1640
Cdd:COG0365   312 GSAGEPLNPEVWEWWYEAVGVP--IVDGWGQTEtgGIFISNLPGLPV--------KPgsMGKPVPGYDVAVVDEDGNPVP 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1641 VGVLGELCIGG--IGVARGYLNRPELTEEKFVDspfvEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIE 1718
Cdd:COG0365   382 PGEEGELVIKGpwPGMFRGYWNDPERYRETYFG----RFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIE 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1719 TQLLK----AE----GvreavvvVREDAKGQKVlCAY------FTAESELKlSELRSSLSQELPGYMIPSYFVQLEQLPL 1784
Cdd:COG0365   458 SALVShpavAEaavvG-------VPDEIRGQVV-KAFvvlkpgVEPSDELA-KELQAHVREELGPYAYPREIEFVDELPK 528
                         570
                  ....*....|.
gi 386647928 1785 TANGKIDRKAL 1795
Cdd:COG0365   529 TRSGKIMRRLL 539
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1301-1795 3.05e-58

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 213.23  E-value: 3.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1301 ALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 1380
Cdd:PRK07656    9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1381 YPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQA----VLCLDDEA--------------AYAEDASNVANVNePHD 1442
Cdd:PRK07656   89 YTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPAlehvVICETEEDdphtekmktftdflAAGDPAERAPEVD-PDD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1443 LAYVIYTSGTTGRPKGVMIEHRSLVNTA------AGYRREyrlDqfpvRLLQLASFsFDVF---VGDIArTLYNGGTMVI 1513
Cdd:PRK07656  168 VADILFTSGTTGRPKGAMLTHRQLLSNAadwaeyLGLTEG---D----RYLAANPF-FHVFgykAGVNA-PLMRGATILP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1514 CPKddrIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVtdyrVLQERFGSQFR---II 1590
Cdd:PRK07656  239 LPV---FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPV----ALLERFESELGvdiVL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1591 NAYGVTEAAidsslydePLAKLPEAGNVP------IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPEL 1664
Cdd:PRK07656  312 TGYGLSEAS--------GVTTFNRLDDDRktvagtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEA 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1665 TEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVL 1744
Cdd:PRK07656  384 TAAA------IDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 1745 CAYFTA--ESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK07656  458 KAYVVLkpGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
854-1264 3.41e-58

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 210.80  E-value: 3.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  854 PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYpEVEFA---VE 930
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIL-DADAArpeLP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  931 HIRANEEE-----ADAAVkqfiRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGG------ 999
Cdd:cd19546    85 VVPATEEElpallADRAA----HLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGArregra 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1000 -EDLPaLRIQYKDYAVWQQSEAQKEQ-----LKRQEAYWLEVFRGELPVLEMPTDYARPAVQSYAGNALRFELDAQKREG 1073
Cdd:cd19546   161 pERAP-LPLQFADYALWERELLAGEDdrdslIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHAR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1074 LQRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRT-HGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKE 1152
Cdd:cd19546   240 LMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVRE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1153 TTLGAFERQDYPFEELVDKLKLARDLSRNPLFDTMFTLQNTENKEF---RLPGLQLTPYPVEEHTSKFDLSLDIME---- 1225
Cdd:cd19546   320 AVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWdapELPGLRTSPVPLGTEAMELDLSLALTErrnd 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 386647928 1226 --SGDGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19546   400 dgDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
5957-6415 3.90e-58

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 212.07  E-value: 3.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5957 EDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLL 6036
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6037 LVQGHLLDRASFA-------DKLVNLNDDGAYHEDGSNL--------------EPVNGPEHLTYVIYTSGTTGRPKGVMV 6095
Cdd:cd05911    87 FTDPDGLEKVKEAakelgpkDKIIVLDDKPDGVLSIEDLlsptlgeededlppPLKDGKDDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6096 EHRNVV---RLVKNTNYVELNEQTHILqtGAVVFDAST--FEIWGALLNGGRLYVVRN---ETILDavslknAIQQYGIN 6167
Cdd:cd05911   167 SHRNLIanlSQVQTFLYGNDGSNDVIL--GFLPLYHIYglFTTLASLLNGATVIIMPKfdsELFLD------LIEKYKIT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6168 TMWLTAPLYNQLSQQ---DSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTEnTTFSTTHTIVGEQK-EAV 6243
Cdd:cd05911   239 FLYLVPPIAAALAKSpllDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTE-TGGILTVNPDGDDKpGSV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6244 piGKPINNSTAYIVDSKL-SLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEY 6322
Cdd:cd05911   318 --GRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWL------HTGDIGYFDEDGYLYI 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6323 KGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAALSQELPNYM---- 6396
Cdd:cd05911   390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKpgEKLTEKEVKDYVAKKVASYKqlrg 469
                         490       500
                  ....*....|....*....|
gi 386647928 6397 -IpsHFVPleRMPLTPNGKI 6415
Cdd:cd05911   470 gV--VFVD--EIPKSASGKI 485
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1323-1795 6.09e-58

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 210.02  E-value: 6.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 1402
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 HlqeraqqwgqtlqavlcLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRReyRLDQF 1482
Cdd:cd17654    97 E-----------------LDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRS--LFNIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1483 PVRLLQLASF-SFDVFVGDIARTLYNGGTMVICPKDDRIDPARL-HYWISEEKITIFESTPALIIPFMDYVAEHGL--DM 1558
Cdd:cd17654   158 SEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLaDILFKRHRITVLQATPTLFRRFGSQSIKSTVlsAT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1559 SSMELLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPeagnVPIGKAALNAKFYIVDAHLNP 1638
Cdd:cd17654   238 SSLRVLALGGEPFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSP----VQLGSPLLGTVIEVRDQNGSE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1639 VPvgvlGELCIGGI---GVARGYLNRPELTeekfvdspfvegerLYRTGDLARwMPDGNVDFIGRIDNQAKIRGYRIETG 1715
Cdd:cd17654   314 GT----GQVFLGGLnrvCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLD 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1716 EIETQLLKAEGVREAVVVVREDakgQKVLCAYFtaeSELKLSELRSSLSQE-LPGYMIPSYFVQLEQLPLTANGKIDRKA 1794
Cdd:cd17654   375 LIQQVIESCLGVESCAVTLSDQ---QRLIAFIV---GESSSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSE 448

                  .
gi 386647928 1795 L 1795
Cdd:cd17654   449 L 449
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
4913-5385 7.36e-58

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 210.02  E-value: 7.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 4992
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 HlqeraqqwgqtlqaalcLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRReyRLDQF 5072
Cdd:cd17654    97 E-----------------LDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRS--LFNIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5073 PVRLLQLASF-SFDVFVGDIARTLYNGGTMVICPKDDRIDPARL-HYWISEEKITIFESTPALIIPFMDYVAEHGL---D 5147
Cdd:cd17654   158 SEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLaDILFKRHRITVLQATPTLFRRFGSQSIKSTVlsaT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5148 MSSMVLLITSSDSCSVTDYRVLQERfGSQFRIINAYGVTEAAIDSSLYDEPLAKLPeagnVPIGKAALNAKFYIVDAHLN 5227
Cdd:cd17654   238 SSLRVLALGGEPFPSLVILSSWRGK-GNRTRIFNIYGITEVSCWALAYKVPEEDSP----VQLGSPLLGTVIEVRDQNGS 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5228 PVPvgvlGELCIGGI---GVARGYLNRPELTeekfvdspfvegerLYRTGDLARwMPDGNVDFIGRIDNQAKIRGYRIET 5304
Cdd:cd17654   313 EGT----GQVFLGGLnrvCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINL 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5305 GEIETQLLKAEGVREAVVVVREDakgQKVLCAHFtaeSELKLSELRSSLSQE-LPGYMIPSYFVQLEQLPLTANGKIDRK 5383
Cdd:cd17654   374 DLIQQVIESCLGVESCAVTLSDQ---QRLIAFIV---GESSSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKS 447

                  ..
gi 386647928 5384 AL 5385
Cdd:cd17654   448 EL 449
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
4891-5385 1.22e-57

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 209.73  E-value: 1.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4891 ALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 4970
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4971 YPSDRIQFMLEDSAASVLLTQTHLQEraqqwgqtlqaalCLDDEAAYAEDAsnvanVNEPHDLAYVIYTSGTTGRPKGVM 5050
Cdd:cd05936    83 YTPRELEHILNDSGAKALIVAVSFTD-------------LLAAGAPLGERV-----ALTPEDVAVLQYTSGTTGVPKGAM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5051 IEHRSLV-NTAAGYRREYRLDQFPVRLLQLASFsFDVFvgdiART------LYNGGTMVICPkddRIDPARLHYWISEEK 5123
Cdd:cd05936   145 LTHRNLVaNALQIKAWLEDLLEGDDVVLAALPL-FHVF----GLTvalllpLALGATIVLIP---RFRPIGVLKEIRKHR 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5124 ITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAidsslydePLAKL- 5202
Cdd:cd05936   217 VTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTG--VPIVEGYGLTETS--------PVVAVn 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5203 -PEAGNVP--IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARW 5279
Cdd:cd05936   287 pLDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYM 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5280 MPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLS--ELRSSLSQEL 5357
Cdd:cd05936   360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTeeEIIAFCREQL 439
                         490       500
                  ....*....|....*....|....*...
gi 386647928 5358 PGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05936   440 AGYKVPRQVEFRDELPKSAVGKILRREL 467
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
266-744 1.37e-57

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 208.62  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  266 FEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYP 345
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  346 EERIRYMLEDSGTQVLLsqghlqervsfsgtwirlDDeeayhedgsnlesvngpehLTYVIYTSGTTGKPKGNLTTHRNI 425
Cdd:cd17631    81 PPEVAYILADSGAKVLF------------------DD-------------------LALLMYTSGTTGRPKGAMLTHRNL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  426 IRVVKNTNY-IDVTGQDKLLQ-LSSYSFDGSTFDIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVMFITTAFFNV 503
Cdd:cd17631   124 LWNAVNALAaLDLGPDDVLLVvAPLFHIGGLGVFTLPTLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPTMIQA 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  504 LVDmNPDCLRHA----RAILFGGERVSVShVRKALGHLGPgKIKHVYGPTESTVFATSYDVHEVEEGAVSIpiGGPISNT 579
Cdd:cd17631   201 LLQ-HPRFATTDlsslRAVIYGGAPMPER-LLRALQARGV-KFVQGYGMTETSPGVTFLSPEDHRRKLGSA--GRPVFFV 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  580 AIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRIDDQVKI 659
Cdd:cd17631   276 EVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMIIS 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  660 RGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEkQLCAYYVAD--RSLPANEVRSTLSQELPAYMLPSYFVQLEQMPL 736
Cdd:cd17631   349 GGENVYPAEVEDVLYEHPAVAEVAVIgVPDEKWGE-AVVAVVVPRpgAELDEDELIAHCRERLARYKIPKSVEFVDALPR 427

                  ....*...
gi 386647928  737 TTNGKVDR 744
Cdd:cd17631   428 NATGKILK 435
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
4444-4854 2.52e-57

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 208.10  E-value: 2.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4444 PVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYpEVDFA---VE 4520
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIL-DADAArpeLP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4521 TVQASEQEAKAIVRDFI-RPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSG-------EEL 4592
Cdd:cd19546    85 VVPATEEELPALLADRAaHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGArregrapERA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4593 PgLRIQYKDYAVWQQSEAQKEQ-----LKRQEAYWLEAFRGELPVLEMPTDYARPAVQSYAGDTLDFRMNSEISEGLKRI 4667
Cdd:cd19546   165 P-LPLQFADYALWERELLAGEDdrdslIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4668 AAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRT-HADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLG 4746
Cdd:cd19546   244 AESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVRE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4747 AFEHQTYPFEELVDKLQMARDLSRNPLFDTMFSLQNTENKEM---HLPGLHLTPYPTEYGMSKFDLSLDMME------DS 4817
Cdd:cd19546   324 ARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWdapELPGLRTSPVPLGTEAMELDLSLALTErrnddgDP 403
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 386647928 4818 EGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19546   404 DGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
3400-3641 2.97e-57

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 200.65  E-value: 2.97e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3400 LTPMQKGMWFHNTlnrHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYKPVEFAYED 3479
Cdd:COG4908     1 LSPAQKRFLFLEP---GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQRIDPDADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3480 LRHLAEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLRNDL 3559
Cdd:COG4908    77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3560 SERPAAP-SYSHYIEWLEKQ----DMEAAARYWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERMSRIAK 3634
Cdd:COG4908   157 PPLPELPiQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236

                  ....*..
gi 386647928 3635 QHQVTVN 3641
Cdd:COG4908   237 AHGATVN 243
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
4890-5385 6.88e-57

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 210.35  E-value: 6.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4890 HALFEKQAECTPEAAAVVYEND-----RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAY 4964
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4965 VPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQ---------------------------QWGQTLQAALCLDDEAAY 5017
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKvidlkekvdealeelpslehvivvgrtGADVPMEGDLDWDELLAA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5018 AEDASNVANVnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYrreyrldqfpvrllqlASFSFDVFVGDI----AR 5093
Cdd:COG0365   172 ASAEFEPEPT-DADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATT----------------AKYVLDLKPGDVfwctAD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5094 T-------------LYNGGTMVICP-KDDRIDPARLhyW--ISEEKITIFESTPALIIPFM----DYVAEHglDMSSMVL 5153
Cdd:COG0365   235 IgwatghsyivygpLLNGATVVLYEgRPDFPDPGRL--WelIEKYGVTVFFTAPTAIRALMkagdEPLKKY--DLSSLRL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5154 LITSSDSCSVTDYRVLQERFGSQfrIINAYGVTE--AAIDSSLYDEPLaklpeagnVP--IGKAALNAKFYIVDAHLNPV 5229
Cdd:COG0365   311 LGSAGEPLNPEVWEWWYEAVGVP--IVDGWGQTEtgGIFISNLPGLPV--------KPgsMGKPVPGYDVAVVDEDGNPV 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5230 PVGVLGELCIGG--IGVARGYLNRPELTEEKFVDspfvEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEI 5307
Cdd:COG0365   381 PPGEEGELVIKGpwPGMFRGYWNDPERYRETYFG----RFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEI 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5308 ETQLLK----AE----GvreavvvVREDAKGQK-----VLCAHFTAESELKlSELRSSLSQELPGYMIPSYFVQLEQLPL 5374
Cdd:COG0365   457 ESALVShpavAEaavvG-------VPDEIRGQVvkafvVLKPGVEPSDELA-KELQAHVREELGPYAYPREIEFVDELPK 528
                         570
                  ....*....|.
gi 386647928 5375 TANGKIDRKAL 5385
Cdd:COG0365   529 TRSGKIMRRLL 539
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
282-742 8.79e-57

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 207.84  E-value: 8.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  282 EDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVL 361
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  362 LSQGHLQERVS-------FSGTWIRLDDEEAYHEDGSNLES--------------VNGPEHLTYVIYTSGTTGKPKGNLT 420
Cdd:cd05911    87 FTDPDGLEKVKeaakelgPKDKIIVLDDKPDGVLSIEDLLSptlgeededlppplKDGKDDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  421 THRNII---RVVKNTNYIDVTGQDKLLqlssySFdgSTFD-IFG------ALLNGAKLVLVPKetvLDVAKLAGLIEKQQ 490
Cdd:cd05911   167 SHRNLIanlSQVQTFLYGNDGSNDVIL-----GF--LPLYhIYGlfttlaSLLNGATVIIMPK---FDSELFLDLIEKYK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  491 ISVMFITTAFFNVLVdMNPDCLRHA----RAILFGGERVSvSHVRKALGHLGPGK-IKHVYGPTESTVFATSYDVHEVEE 565
Cdd:cd05911   237 ITFLYLVPPIAAALA-KSPLLDKYDlsslRVILSGGAPLS-KELQELLAKRFPNAtIKQGYGMTETGGILTVNPDGDDKP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  566 GAVsipiGGPISNTAIYIVNAQ-NKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPD 644
Cdd:cd05911   315 GSV----GRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDED 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  645 GTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKQLcAYYV--ADRSLPANEVRSTLSQELPA 721
Cdd:cd05911   385 GYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIgIPDEVSGELPR-AYVVrkPGEKLTEKEVKDYVAKKVAS 463
                         490       500
                  ....*....|....*....|....*...
gi 386647928  722 YmlpsY-------FVqlEQMPLTTNGKV 742
Cdd:cd05911   464 Y----KqlrggvvFV--DEIPKSASGKI 485
PRK12316 PRK12316
peptide synthase; Provisional
8016-8459 1.17e-56

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 222.14  E-value: 1.17e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8016 GLEQEEHSAIPV-IGERE-YYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGpLDRDRFEAVFRQLIERHETLRTGF-- 8091
Cdd:PRK12316 4083 GLDQARLDALPLpLGEIEdIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvw 4161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8092 EMANGEPVQRVYSDVE--FAVE--YSKADREEAVE--IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGA 8165
Cdd:PRK12316 4162 QGELGRPLQVVHKQVSlpFAELdwRGRADLQAALDalAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGW 4241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8166 SVGILQEEFSRLYAGEELPPLRIQYKDYAAW-QRSEAYAkrvkqQEGYWLQTLAGELPVIELPTDYERTSTRSFEG-AEL 8243
Cdd:PRK12316 4242 SNSQLLGEVLERYSGRPPAQPGGRYRDYIAWlQRQDAAA-----SEAFWREQLAALDEPTRLAQAIARADLRSANGyGEH 4316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8244 EFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRThAD---VEPIIGMFVNTLAIRNYPAG 8320
Cdd:PRK12316 4317 VRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRP-AElpgIEGQIGLFINTLPVIATPRA 4395
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8321 DKTFLSYLEEVKETTLGAFEHQDYPFEELverlnvKRDASR--NPVFDTMFVLQNTE-----DRGIEADAFSLTPFVFDQ 8393
Cdd:PRK12316 4396 QQSVVEWLQQVQRQNLALREHEHTPLYEI------QRWAGQggEALFDSLLVFENYPvsealQQGAPGGLRFGEVTNHEQ 4469
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 8394 TVaAQFDLTLSVAEddgAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQLNEPE 8459
Cdd:PRK12316 4470 TN-YPLTLAVGLGE---TLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKA 4531
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
2359-2828 1.24e-56

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 206.55  E-value: 1.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQ----LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRI 2434
Cdd:cd17654     1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 SYMLEDSSAQVLLAQRRL-QERVSFAGTVVTVDDEQAYAgdgsnlesavgpndLAYIIYTSGTTGKPKGVMVEHHGLCSL 2513
Cdd:cd17654    81 LTVMKKCHVSYLLQNKELdNAPLSFTPEHRHFNIRTDEC--------------LAYVIHTSGTTGTPKIVAVPHKCILPN 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2514 KQMFANTLQInAQDRVVQFAS-LSFDASCWEVFQTLFFGATL-YIPTKETILDYQWFERYMSDNGITTATLPPTyavYLN 2591
Cdd:cd17654   147 IQHFRSLFNI-TSEDILFLTSpLTFDPSVVEIFLSLSSGATLlIVPTSVKVLPSKLADILFKRHRITVLQATPT---LFR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2592 PDHMPDFKRLIAAGSAS------------SLELLQQWK---DKVKYFNAYGPTEdsicTTIWTpSTEDISQLKS-VPIGG 2655
Cdd:cd17654   223 RFGSQSIKSTVLSATSSlrvlalggepfpSLVILSSWRgkgNRTRIFNIYGITE----VSCWA-LAYKVPEEDSpVQLGS 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2656 PIVNHRIYIVDAHYQPVPVGVAGELcIAGVGLARGYLNRPDLTaekfvdnpfepgerMYRTGDLAKwLPDGTIEYLGRID 2735
Cdd:cd17654   298 PLLGTVIEVRDQNGSEGTGQVFLGG-LNRVCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKD 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2736 HQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDdasgQKQLCAYFVAD--RTMTVGELRGELsgeLPGYMIPAHFVQLE 2813
Cdd:cd17654   362 SQIKRRGKRINLDLIQQVIESCLGVESCAVTLSD----QQRLIAFIVGEssSSRIHKELQLTL---LSSHAIPDTFVQID 434
                         490
                  ....*....|....*
gi 386647928 2814 RMPLTPNGKIDRKAL 2828
Cdd:cd17654   435 KLPLTSHGKVDKSEL 449
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
5491-5902 1.43e-56

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 204.46  E-value: 1.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5491 YPVSSAQKrlYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEP--VQRVYKEVNFAVE 5568
Cdd:cd19542     2 YPCTPMQE--GMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtfLQVVLKSLDPPIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5569 HYRTSEAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGESLAPlRIQYK 5648
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPFS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5649 DYATWQQSEAQQEQMkrqeAYWLDMFRGELPVLELPTDYPRPAVRkfEGSLLQRQLEPklgegLQRIAAESGATLYMVLL 5728
Cdd:cd19542   159 DYISYLQSQSQEESL----QYWRKYLQGASPCAFPSLSPKRPAER--SLSSTRRSLAK-----LEAFCASLGVTLASLFQ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5729 AAYKVLLQKYTGQEDIVVGTPIAGRT--HSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAYEHQSYPFEEL 5806
Cdd:cd19542   228 AAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5807 VEKaqpARDLSRNPLFDTLFALQNKE-TGELQLDGLRLTPYPAEHTVAKFDLSVDVTEGSEGLELSMEYSTALYTRETIE 5885
Cdd:cd19542   308 QRA---LGLWPSGTLFNTLVSYQNFEaSPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAE 384
                         410
                  ....*....|....*..
gi 386647928 5886 RMAKHFEQLLTAIVQAP 5902
Cdd:cd19542   385 ELLEQFDDILEALLANP 401
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
263-757 9.43e-56

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 207.27  E-value: 9.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  263 HRLFEEQAERRPDAVAVTFED-----RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAY 337
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  338 VPIDPEYPEERIRYMLEDSGTQVLLSQ--------------------------------GHLQERVSFSGtWIRLDDEEA 385
Cdd:COG0365    92 SPVFPGFGAEALADRIEDAEAKVLITAdgglrggkvidlkekvdealeelpslehvivvGRTGADVPMEG-DLDWDELLA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  386 YHEDGSNLESVNgPEHLTYVIYTSGTTGKPKGNLTTHRNIirvvkntnyidvtgqdkLLQLSS---YSFD---GSTF--- 456
Cdd:COG0365   171 AASAEFEPEPTD-ADDPLFILYTSGTTGKPKGVVHTHGGY-----------------LVHAATtakYVLDlkpGDVFwct 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  457 -DI----------FGALLNGAKLVLVP-KETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRHA-----RAIL 519
Cdd:COG0365   233 aDIgwatghsyivYGPLLNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYdlsslRLLG 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  520 FGGERVS---VSHVRKALGHlgpgKIKHVYGPTEST-VFATSYDVHEVEEGAVSIPIGGpisnTAIYIVNAQNKLQPIGV 595
Cdd:COG0365   313 SAGEPLNpevWEWWYEAVGV----PIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPG----YDVAVVDEDGNPVPPGE 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  596 AGELCVAGD--GLARGYLNRPDLTAEKFadnpFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHL 673
Cdd:COG0365   385 EGELVIKGPwpGMFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESAL 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  674 LKLEAIEKATVVVRESANGEKQLCAY------YVADRSLpANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:COG0365   461 VSHPAVAEAAVVGVPDEIRGQVVKAFvvlkpgVEPSDEL-AKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
                         570
                  ....*....|
gi 386647928  748 PAPEESMETG 757
Cdd:COG0365   540 RKIAEGRPLG 549
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1308-1798 1.33e-55

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 205.44  E-value: 1.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1308 ERTPEVAAVVYENDR---LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSD 1384
Cdd:cd17647     3 ERTCVVETPSLNSSKtrsFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1385 RIQFMLEDSAASVLLTqthlqeraqqwgqtlqavlclddeaayAEDASNVANvnePHDLAYVIYTSGTTGRPKGVMIEHR 1464
Cdd:cd17647    83 RQNIYLGVAKPRGLIV---------------------------IRAAGVVVG---PDSNPTLSFTSGSEGIPKGVLGRHF 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1465 SLVNTAAGYRREYRL---DQFPVrllqLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTP 1541
Cdd:cd17647   133 SLAYYFPWMAKRFNLsenDKFTM----LSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTP 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 AL--IIpfmdyVAEHGLDMSSMELLITSSDSCSVTDYRVLQErFGSQFRIINAYGVTEAAIDSSLYDEP--------LAK 1611
Cdd:cd17647   209 AMgqLL-----TAQATTPFPKLHHAFFVGDILTKRDCLRLQT-LAENVRIVNMYGTTETQRAVSYFEVPsrssdptfLKN 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1612 LPEAgnVPIGKAALNAKFYIVDAH--LNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGE----------- 1678
Cdd:cd17647   283 LKDV--MPAGRGMLNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnne 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1679 -----------RLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAY 1747
Cdd:cd17647   361 pwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSY 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1748 FTAESELKLSE-----------------------------LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 1798
Cdd:cd17647   441 IVPRFDKPDDEsfaqedvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
4891-5385 1.35e-55

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 205.14  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4891 ALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 4970
Cdd:PRK07656    9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4971 YPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQ---TLQAALCLDDEAAYAE--------------DASNVANVNEPHDL 5033
Cdd:PRK07656   89 YTADEAAYILARGDAKALFVLGLFLGVDYSATTrlpALEHVVICETEEDDPHtekmktftdflaagDPAERAPEVDPDDV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5034 AYVIYTSGTTGRPKGVMIEHRSLVNTA------AGYRREyrlDqfpvRLLQLASFsFDVF---VGDIArTLYNGGTMVIC 5104
Cdd:PRK07656  169 ADILFTSGTTGRPKGAMLTHRQLLSNAadwaeyLGLTEG---D----RYLAANPF-FHVFgykAGVNA-PLMRGATILPL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5105 PKddrIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVtdyrVLQERFGSQFR---IIN 5181
Cdd:PRK07656  240 PV---FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPV----ALLERFESELGvdiVLT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5182 AYGVTEAAidsslydePLAKLPEAGNVP------IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELT 5255
Cdd:PRK07656  313 GYGLSEAS--------GVTTFNRLDDDRktvagtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEAT 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5256 EEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLC 5335
Cdd:PRK07656  385 AAA------IDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGK 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 5336 AHFTA--ESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK07656  459 AYVVLkpGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
853-1264 2.55e-55

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 201.44  E-value: 2.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  853 YPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVEFAVEHI 932
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  933 RANEEEA-DAAVKQFIRA-----FDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY----GGEDL 1002
Cdd:cd19533    82 DLSGDPDpEGAAQQWMQEdlrkpLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1003 PALriQYKDYAVWQQSEAQ---KEQLKRQEAYWLEVFRGELPvlemPTDYARPAVQSYAGnALRF--ELDAQKREGLQRI 1077
Cdd:cd19533   162 PPA--PFGSFLDLVEEEQAyrqSERFERDRAFWTEQFEDLPE----PVSLARRAPGRSLA-FLRRtaELPPELTRTLLEA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1078 ASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGA 1157
Cdd:cd19533   235 AEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1158 FERQDYPFEELVDKLKLARDLsrNPLFDTMFTLQNTEnkefrlPGLQLTPYPVEEHT----SKFDLSLDIMESGD--GFL 1231
Cdd:cd19533   315 LRHQRYRYEDLRRDLGLTGEL--HPLFGPTVNYMPFD------YGLDFGGVVGLTHNlssgPTNDLSIFVYDRDDesGLR 386
                         410       420       430
                  ....*....|....*....|....*....|...
gi 386647928 1232 CGIEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19533   387 IDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3878-4338 3.29e-55

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 201.37  E-value: 3.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3878 SQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLT 3957
Cdd:cd05934     2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3958 QrhlrervsfagtfvavddeqayhadgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDr 4037
Cdd:cd05934    82 D-------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4038 vVQFASLSF---DASCWEIFKALFFGATLYI----PTSTtildyplFESYMNENGITATILPPTYAAYL--NPDRM-PSL 4107
Cdd:cd05934   124 -VYLTVLPLfhiNAQAVSVLAALSVGATLVLlprfSASR-------FWSDVRRYGATVTNYLGAMLSYLlaQPPSPdDRA 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4108 KKL-ITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTsiwdeASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVG 4184
Cdd:cd05934   196 HRLrAAYGAPNPPELHEEFEERfgVRLLEGYGMTETIVGV-----IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4185 VAGELCISGV---GLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVET 4261
Cdd:cd05934   271 EPGELVIRGLrgwGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER 343
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 4262 QLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALP 4338
Cdd:cd05934   344 AILRHPAVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1901-2315 4.26e-55

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 201.06  E-value: 4.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1901 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHY 1980
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1981 RTSEAEAGE------VVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGE------ 2048
Cdd:cd19533    82 DLSGDPDPEgaaqqwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALlkgrpa 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2049 ------SLATLRIQYKDYavwQQSeeqlERVKRQEAYWLDMFRGELPV--LEMPTDYPRPAVRRFegstlSFRLDAGLNE 2120
Cdd:cd19533   162 ppapfgSFLDLVEEEQAY---RQS----ERFERDRAFWTEQFEDLPEPvsLARRAPGRSLAFLRR-----TAELPPELTR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2121 ALKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKE 2200
Cdd:cd19533   230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2201 TTLGAYEHQTYPFEELVeklqvpRDLSRNPIFDAMF-VLQNTENEELQLD----GLKLAPYPSGNTIarfDLTLDVTET- 2274
Cdd:cd19533   310 ELRSLLRHQRYRYEDLR------RDLGLTGELHPLFgPTVNYMPFDYGLDfggvVGLTHNLSSGPTN---DLSIFVYDRd 380
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 386647928 2275 -GSGLECNLEYATSLYARETIARmakHLEQLLTAIAKAPEAP 2315
Cdd:cd19533   381 dESGLRIDFDANPALYSGEDLAR---HQERLLRLLEEAAADP 419
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7469-7929 4.59e-55

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 200.98  E-value: 4.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7469 NTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLL 7548
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7549 TQrhlqecvsfdgkviaaddeqaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEED 7628
Cdd:cd05934    81 VD-------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7629 rvVQFASLSF---DASCWEIFKALFFGATLYIPAK-------DTILDYPlfESYMNENGITAAIL---PPtyaiylSPDR 7695
Cdd:cd05934   124 --VYLTVLPLfhiNAQAVSVLAALSVGATLVLLPRfsasrfwSDVRRYG--ATVTNYLGAMLSYLlaqPP------SPDD 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7696 LPSLKKLItGGSAASVEFVQQWKDK--VRYFNAYGPTEASIVTsvwaASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLP 7773
Cdd:cd05934   194 RAHRLRAA-YGAPNPPELHEEFEERfgVRLLEGYGMTETIVGV----IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELP 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7774 VGVAGELCISGA---GLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEI 7850
Cdd:cd05934   269 AGEPGELVIRGLrgwGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEV 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7851 EEQLLKIASVQETIVIARGDANGQQQLCAYFVAD--RELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05934   342 ERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421

                  .
gi 386647928 7929 P 7929
Cdd:cd05934   422 R 422
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
4443-4854 5.40e-55

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 200.67  E-value: 5.40e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4443 YPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVDFAVETV 4522
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4523 QAS-----EQEAKAIVRDFIR-PFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLY----SGEEL 4592
Cdd:cd19533    82 DLSgdpdpEGAAQQWMQEDLRkPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4593 PglRIQYKDYAVWQQSEAQKEQLKRQE---AYWLEAFRGELPvlemPTDYARPAVQSYAG---DTLDFRmnSEISEGLKR 4666
Cdd:cd19533   162 P--PAPFGSFLDLVEEEQAYRQSERFErdrAFWTEQFEDLPE----PVSLARRAPGRSLAflrRTAELP--PELTRTLLE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4667 IAAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTHADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLG 4746
Cdd:cd19533   234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRS 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4747 AFEHQTYPFEELVdklqmaRDL----SRNPLFDTMFSLQNTEnKEMHLPGLHLTPYPTEYGMSKfDLSLDMME--DSEGL 4820
Cdd:cd19533   314 LLRHQRYRYEDLR------RDLgltgELHPLFGPTVNYMPFD-YGLDFGGVVGLTHNLSSGPTN-DLSIFVYDrdDESGL 385
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 4821 ECSLEFATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19533   386 RIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
6825-6976 5.55e-55

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 190.56  E-value: 5.55e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6825 LSTRIKKVKEDLRRIPNKGIGYGLCRYLSAQPDGTVWGAEPEISFNYLGQFDQDLSNNDIGLSPYSSGLEMSDRQARSFI 6904
Cdd:TIGR01720    2 LGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKLAASPQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRPYA 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  6905 LDINGMITDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAHCAAKEWTELTPSDVQLKGLTVEELEQI 6976
Cdd:TIGR01720   82 LEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
7472-7923 6.69e-55

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 201.07  E-value: 6.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQR 7551
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 hlqecvSFDGKVIAADdeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVV 7631
Cdd:cd05903    82 ------RFRQFDPAAM-----------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7632 QFASLS-FDASCWEIFKALFFGATLYI-----PAKDTILdyplfesyMNENGITAAILPPTY------AIYLSPDRLPSL 7699
Cdd:cd05903   139 VASPMAhQTGFVYGFTLPLLLGAPVVLqdiwdPDKALAL--------MREHGVTFMMGATPFltdllnAVEEAGEPLSRL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7700 KKLITGGSAASVEFVQQWKD----KVryFNAYGPTE-ASIVTSVwaaSPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPV 7774
Cdd:cd05903   211 RTFVCGGATVPRSLARRAAEllgaKV--CSAYGSTEcPGAVTSI---TPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAP 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7775 GVAGELCISGAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRiDHQVKIR-GYRIELGEIEEQ 7853
Cdd:cd05903   286 GVEGELLSRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLEVEDL 357
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 7854 LLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLS-QELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:cd05903   358 LLGHPGVIEAAVVALPDERLGERACAVVVtkSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
2367-2823 7.73e-55

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 202.44  E-value: 7.73e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2367 EGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVL 2446
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2447 LAQRRLQERVSFAGT-------VVTVDDEQAYAGDGSNLESAV--------------GPNDLAYIIYTSGTTGKPKGVMV 2505
Cdd:cd05911    87 FTDPDGLEKVKEAAKelgpkdkIIVLDDKPDGVLSIEDLLSPTlgeededlppplkdGKDDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2506 EHHGLCSLKQMFANTLQINAQDRVVQFASLSFD--ASCWEVFQTLFFGATLYIPTKetiLDYQWFERYMSDNGITTATLP 2583
Cdd:cd05911   167 SHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATVIIMPK---FDSELFLDLIEKYKITFLYLV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2584 PTYAVYL--NPDH----MPDFKRLIAAGSASS---LELLQQWKDKVKYFNAYGPTEdSICTTIWTPSTEDisQLKSVpiG 2654
Cdd:cd05911   244 PPIAAALakSPLLdkydLSSLRVILSGGAPLSkelQELLAKRFPNATIKQGYGMTE-TGGILTVNPDGDD--KPGSV--G 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2655 GPIVNHRIYIVDAH-YQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGR 2733
Cdd:cd05911   319 RLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIVDR 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2734 IDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGELPGYMipahfvQ 2811
Cdd:cd05911   393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrkPGEKLTEKEVKDYVAKKVASYK------Q 466
                         490
                  ....*....|....*....
gi 386647928 2812 L-------ERMPLTPNGKI 2823
Cdd:cd05911   467 LrggvvfvDEIPKSASGKI 485
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
4914-5388 3.18e-54

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 201.59  E-value: 3.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4914 TYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTqth 4993
Cdd:cd17647    22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV--- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4994 lqeraqqwgqtLQAAlclddeaayaedasnvANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL---D 5070
Cdd:cd17647    99 -----------IRAA----------------GVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLsenD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5071 QFPVrllqLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPAL--IIpfmdyVAEHGLDM 5148
Cdd:cd17647   152 KFTM----LSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMgqLL-----TAQATTPF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5149 SSMVLLITSSDSCSVTDYRVLQErFGSQFRIINAYGVTEAAIDSSLYDEP--------LAKLPEAgnVPIGKAALNAKFY 5220
Cdd:cd17647   223 PKLHHAFFVGDILTKRDCLRLQT-LAENVRIVNMYGTTETQRAVSYFEVPsrssdptfLKNLKDV--MPAGRGMLNVQLL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5221 IVDAH--LNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGE----------------------RLYRTGDL 5276
Cdd:cd17647   300 VVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGDL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5277 ARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSE-------- 5348
Cdd:cd17647   380 GRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDEsfaqedvp 459
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 5349 ---------------------LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 5388
Cdd:cd17647   460 kevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2368-2829 5.34e-54

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 197.90  E-value: 5.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2368 GQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLL 2447
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2448 AqrrlqervsfagtvvtvddeqayagdgsnlesavgpnDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQD 2527
Cdd:cd05934    81 V-------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2528 rvVQFASLSF---DASCWEVFQTLFFGATLyiptkeTILDYQWFERYMSD---NGITTATLPPTYAVYL--NPDHMPDFK 2599
Cdd:cd05934   124 --VYLTVLPLfhiNAQAVSVLAALSVGATL------VLLPRFSASRFWSDvrrYGATVTNYLGAMLSYLlaQPPSPDDRA 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2600 -RL-IAAGSASSLELLQQWKDK--VKYFNAYGPTEDSICttIWTPSTEDIsqlKSVPIGGPIVNHRIYIVDAHYQPVPVG 2675
Cdd:cd05934   196 hRLrAAYGAPNPPELHEEFEERfgVRLLEGYGMTETIVG--VIGPRDEPR---RPGSIGRPAPGYEVRIVDDDGQELPAG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2676 VAGELCIAGV---GLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEE 2752
Cdd:cd05934   271 EPGELVIRGLrgwGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER 343
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2753 QLLKVASVQEAIVIAHDDASGQKQLCAYFVAD--RTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALP 2829
Cdd:cd05934   344 AILRHPAVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK05691 PRK05691
peptide synthase; Validated
5936-6780 6.01e-54

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 213.11  E-value: 6.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTF------EDKQLTYGELNERANRLARTLRNAGVQPDQMVgLMVERSLEMVVGMIAILKAG 6009
Cdd:PRK05691   10 TLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6010 GAYVPIDPdyPE-------DRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDGAYHEDGSNLEPVNG-------PE 6075
Cdd:PRK05691   89 VIAVPAYP--PEsarrhhqERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAwqepalqPD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTYVIYTSGTTGRPKGVMVEHRNVV---RLVKNTNYVELNEQTHILQTGAVVFDAStfeIWGALLNG---GRLYVVRNE 6149
Cdd:PRK05691  167 DIAFLQYTSGSTALPKGVQVSHGNLVaneQLIRHGFGIDLNPDDVIVSWLPLYHDMG---LIGGLLQPifsGVPCVLMSP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6150 TILDAVSLK--NAIQQYGINTMWLTAPLYNQLSQQDS-GMFAGL-----KTLIVGGDVLSVPHINRVLREHAGL-----S 6216
Cdd:PRK05691  244 AYFLERPLRwlEAISEYGGTISGGPDFAYRLCSERVSeSALERLdlsrwRVAYSGSEPIRQDSLERFAEKFAACgfdpdS 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6217 IVNGYGPTENTTF--------------------STTHTIVGEQKEAVPIGKPINNSTAYIVD-SKLSLLPVGVWGELIVG 6275
Cdd:PRK05691  324 FFASYGLAEATLFvsggrrgqgipaleldaealARNRAEPGTGSVLMSCGRSQPGHAVLIVDpQSLEVLGDNRVGEIWAS 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6276 GDGVARGYLNRPELTAEKFVEssfLPGERCYRTGDLArWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLK-VASVKE 6354
Cdd:PRK05691  404 GPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEReVEVVRK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6355 ATVIV----REDESG-----------QKQLCAyfvaerELTIGELRAALS---QElpnymIPSHFVPLE--RMPLTPNGK 6414
Cdd:PRK05691  480 GRVAAfavnHQGEEGigiaaeisrsvQKILPP------QALIKSIRQAVAeacQE-----APSVVLLLNpgALPKTSSGK 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6415 IDRRALPA-------------PQGNAPVGAEYVAPRTEQEKALAAVWQAVLGAERVGVTDHFFELGGDSIKSIQVSSRLH 6481
Cdd:PRK05691  549 LQRSACRLrladgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLR 628
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6482 QA-GYKLEIRDLFKYPTLAQLSQHiqpVARMI-DQGEVTGEIGLTPIQR-----------WFFDQSLADLHHFNQAFMLH 6548
Cdd:PRK05691  629 DElGIDLNLRQLFEAPTLAAFSAA---VARQLaGGGAAQAAIARLPRGQalpqslaqnrlWLLWQLDPQSAAYNIPGGLH 705
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6549 RKDRFDEAALRQVLQKLAEHHDALRTVFrkSENGYAAWNRAIGEGElYSLEVADFRDVKSAE---QAVEAKANEIQSSID 6625
Cdd:PRK05691  706 LRGELDEAALRASFQRLVERHESLRTRF--YERDGVALQRIDAQGE-FALQRIDLSDLPEAEreaRAAQIREEEARQPFD 782
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6626 LEVGPLFKAGLFQCADGDHLLLV-IHHGVVDGVSWRILLEDVALGYEQAAKGEEVRL---PAKTDSFRTWSEQLAAYAQS 6701
Cdd:PRK05691  783 LEKGPLLRVTLVRLDDEEHQLLVtLHHIVADGWSLNILLDEFSRLYAAACQGQTAELaplPLGYADYGAWQRQWLAQGEA 862
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6702 pamENERAYWEQIAQTAVAPLPKDKQSDRSLQQDSESitIQWSRKETEQL---LKKVHRAYNTEMNDILLTALGMAVQKW 6778
Cdd:PRK05691  863 ---ARQLAYWKAQLGDEQPVLELATDHPRSARQAHSA--ARYSLRVDASLseaLRGLAQAHQATLFMVLLAAFQALLHRY 937

                  ..
gi 386647928 6779 SG 6780
Cdd:PRK05691  938 SG 939
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
3868-4337 7.60e-54

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 199.90  E-value: 7.60e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADGSNLEPVVG-------------------PNHLAYVIYTSGTTGK 4008
Cdd:cd05959    98 EDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALllaelvaaeaeqlkpaathADDPAFWLYSSGSTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4009 PKGVMVEHHGLCSLKLMFA-NTLQMTEQDRVvqfaslsFDAScwEIFKALFFGATLYIPTS---TTILdYP------LFE 4078
Cdd:cd05959   178 PKGVVHLHADIYWTAELYArNVLGIREDDVC-------FSAA--KLFFAYGLGNSLTFPLSvgaTTVL-MPerptpaAVF 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4079 SYMNENGITATILPPT-YAAYLNPDRMP-----SLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEAsivTSIWdeA 4150
Cdd:cd05959   248 KRIRRYRPTVFFGVPTlYAAMLAAPNLPsrdlsSLRLCVSAGEALPAEVGERWKARfgLDILDGIGSTEM---LHIF--L 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4151 SDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVdnpfepGErMYRTGDLVR 4230
Cdd:cd05959   323 SNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYV 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4231 WLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQR-----ELTAAELRATM 4305
Cdd:cd05959   396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyedsEALEEELKEFV 475
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 4306 SQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05959   476 KDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1315-1795 1.14e-53

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 197.51  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1315 AVVYENDRLTYRELNERANRLARMLRAQG-VKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDS 1393
Cdd:cd05941     4 AIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1394 AASVLLtqthlqeraqqwgqtlqavlclddeaayaedasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGY 1473
Cdd:cd05941    84 EPSLVL------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1474 RREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDdriDPARLHYWISEEKITIFESTPALIIPFMDYVAE 1553
Cdd:cd05941   122 VDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTIYTRLLQYYEA 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1554 HGLDM--------SSMELLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAIDSSlydEPLAKLPEAGNVpiGKAAL 1625
Cdd:cd05941   199 HFTDPqfaraaaaERLRLMVSGSAALPVPTLEEWEAITGH--TLLERYGMTEIGMALS---NPLDGERRPGTV--GMPLP 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1626 NAKFYIVDAHLN-PVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRI-DN 1703
Cdd:cd05941   272 GVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsVD 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1704 QAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVlCAYFTAESE---LKLSELRSSLSQELPGYMIPSYFVQL 1779
Cdd:cd05941   346 IIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGERV-VAVVVLRAGaaaLSLEELKEWAKQRLAPYKRPRRLILV 424
                         490
                  ....*....|....*.
gi 386647928 1780 EQLPLTANGKIDRKAL 1795
Cdd:cd05941   425 DELPRNAMGKVNKKEL 440
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2378-2828 1.29e-53

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 197.66  E-value: 1.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2378 ERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGA----YVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQ 2453
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2454 ERVSFAGTVV----TVDDEQAYAGDGSNLES-AVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDR 2528
Cdd:cd05922    81 DRLRDALPASpdpgTVLDADGIRAARASAPAhEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2529 VVQFASLSFDASCWEVFQTLFFGATLYIpTKETILDyQWFERYMSDNGITT-ATLPPTYA----VYLNPDHMPDFKRLIA 2603
Cdd:cd05922   161 ALTVLPLSYDYGLSVLNTHLLRGATLVL-TNDGVLD-DAFWEDLREHGATGlAGVPSTYAmltrLGFDPAKLPSLRYLTQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2604 AGSASSLELLQQWKDKV---KYFNAYGPTEDSICTTIWTPSTEDiSQLKSvpIGGPIVNHRIYIVDAHYQPVPVGVAGEL 2680
Cdd:cd05922   239 AGGRLPQETIARLRELLpgaQVYVMYGQTEATRRMTYLPPERIL-EKPGS--IGLAIPGGEFEILDDDGTPTPPGEPGEI 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2681 CIAGVGLARGYLNRPDLTAEkfvdnPFEPGERMYrTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASV 2760
Cdd:cd05922   316 VHRGPNVMKGYWNDPPYRRK-----EGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 2761 QEAIVIAHDDASGQKqLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05922   390 IEAAAVGLPDPLGEK-LALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
5491-5905 1.51e-53

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 196.44  E-value: 1.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5491 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHY 5570
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5571 RTSEAEAGE------VVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNG---ESLA 5641
Cdd:cd19533    82 DLSGDPDPEgaaqqwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTAllkGRPA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5642 PLRIqYKDYATWQQSEAQQEQMKRQE---AYWLDMFRGELPVLELPTDYPRPAVrkfegSLLQRQLE--PKLGEGLQRIA 5716
Cdd:cd19533   162 PPAP-FGSFLDLVEEEQAYRQSERFErdrAFWTEQFEDLPEPVSLARRAPGRSL-----AFLRRTAElpPELTRTLLEAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5717 AESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAY 5796
Cdd:cd19533   236 EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5797 EHQSYPFEELVekaqpaRDL----SRNPLFDTLFALQNKETGeLQLDGLRLTPYPAEHTVAKfDLSVDVTE--GSEGLEL 5870
Cdd:cd19533   316 RHQRYRYEDLR------RDLgltgELHPLFGPTVNYMPFDYG-LDFGGVVGLTHNLSSGPTN-DLSIFVYDrdDESGLRI 387
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 386647928 5871 SMEYSTALYTRETIERmakHFEQLLTAIVQAPEAP 5905
Cdd:cd19533   388 DFDANPALYSGEDLAR---HQERLLRLLEEAAADP 419
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1299-1795 1.96e-53

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 199.26  E-value: 1.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1299 FHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 1378
Cdd:PRK06187    8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1379 PDYPSDRIQFMLEDSAASVLLT-QTHLQERAQQWGQ--TLQAVLCLDDEAAYAEDASNVANVN--------------EPH 1441
Cdd:PRK06187   88 IRLKPEEIAYILNDAEDRVVLVdSEFVPLLAAILPQlpTVRTVIVEGDGPAAPLAPEVGEYEEllaaasdtfdfpdiDEN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 DLAYVIYTSGTTGRPKGVMIEHRSLV------NTAAGYRREyrlDQFPVRLLQLASFSFDVFVgdiaRTLYNGGTMVIcP 1515
Cdd:PRK06187  168 DAAAMLYTSGTTGHPKGVVLSHRNLFlhslavCAWLKLSRD---DVYLVIVPMFHVHAWGLPY----LALMAGAKQVI-P 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1516 kdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQFriINAYGV 1595
Cdd:PRK06187  240 --RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDL--VQGYGM 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1596 TEAA-IDSSLY--DEPLAKLPEAGNVpiGKAALNAKFYIVDAHLNPVPV--GVLGELCIGGIGVARGYLNRPELTEEKFV 1670
Cdd:PRK06187  316 TETSpVVSVLPpeDQLPGQWTKRRSA--GRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETID 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1671 DSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLcAYFT 1749
Cdd:PRK06187  394 GG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPV-AVVV 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 1750 AESELKLS--ELRSSLSQELPGYMIPS--YFVqlEQLPLTANGKIDRKAL 1795
Cdd:PRK06187  466 LKPGATLDakELRAFLRGRLAKFKLPKriAFV--DELPRTSVGKILKRVL 513
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
7473-7928 2.84e-53

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 196.13  E-value: 2.84e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7473 TYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRH 7552
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7553 LQEcvsFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGV-----MVEHHGLCSlklmfAETLRITEE 7627
Cdd:TIGR01923   81 LEE---KDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVphtfrNHYASAVGS-----KENLGFTED 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7628 DRVVQFASLsFDASCWEI-FKALFFGATLYIPAKDTildyPLFESYMNENgITAAILPPTYAIYLSPDRLP--SLKKLIT 7704
Cdd:TIGR01923  153 DNWLLSLPL-YHISGLSIlFRWLIEGATLRIVDKFN----QLLEMIANER-VTHISLVPTQLNRLLDEGGHneNLRKILL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7705 GGSAASVEFVQQWKDK-VRYFNAYGPTEASivTSVWAASPDGLDLRSvPIGRPIANHQIFI-VDSQNHMlpvgvaGELCI 7782
Cdd:TIGR01923  227 GGSAIPAPLIEEAQQYgLPIYLSYGMTETC--SQVTTATPEMLHARP-DVGRPLAGREIKIkVDNKEGH------GEIMV 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  7783 SGAGLARGYLNRPELTaEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQE 7862
Cdd:TIGR01923  298 KGANLMKGYLYQGELT-PAFEQQGWF------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQE 370
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  7863 TIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:TIGR01923  371 AVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
6523-6764 3.76e-53

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 189.09  E-value: 3.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6523 LTPIQRWFFdQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGyaaWNRAIGEGELYSLEVAD 6602
Cdd:COG4908     1 LSPAQKRFL-FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGE---PVQRIDPDADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6603 FRDVKSAEQAVEAK---ANEIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEE 6678
Cdd:COG4908    77 LSALPEPEREAELEelvAEEASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6679 VRLPAKTDSFRTWSEQLAAYAQSPAMENERAYWEQIAQTA--VAPLPKDKQSDRSLQQDSESITIQWSRKETEQLLKKVh 6756
Cdd:COG4908   157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAppVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA- 235

                  ....*...
gi 386647928 6757 RAYNTEMN 6764
Cdd:COG4908   236 KAHGATVN 243
PRK08316 PRK08316
acyl-CoA synthetase; Validated
7443-7923 4.62e-53

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 198.23  E-value: 4.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7443 AREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGA 7522
Cdd:PRK08316    8 ARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7523 YVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQECV---------------------SFDGKVIAADDEQAyGEDGSNLEP 7581
Cdd:PRK08316   88 HVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAeaalallpvdtlilslvlggrEAPGGWLDFADWAE-AGSVAEPDV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7582 VVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQ----FASLSFDAscweifkalFFGATLYI 7657
Cdd:PRK08316  167 ELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHalplYHCAQLDV---------FLGPYLYV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7658 PAKDTILDYP----LFEsYMNENGITAAILPPTYAIYL--SPD----RLPSLKKLITGGSAASVEFVQQWKDK---VRYF 7724
Cdd:PRK08316  238 GATNVILDAPdpelILR-TIEAERITSFFAPPTVWISLlrHPDfdtrDLSSLRKGYYGASIMPVEVLKELRERlpgLRFY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7725 NAYGPTEASIVTSVwaASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVD 7804
Cdd:PRK08316  317 NCYGQTEIAPLATV--LGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7805 NPFlagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV-- 7882
Cdd:PRK08316  395 GWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVpk 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928 7883 ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:PRK08316  468 AGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
PRK07798 PRK07798
acyl-CoA synthetase; Validated
5936-6418 7.07e-53

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 197.80  E-value: 7.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPI 6015
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6016 DPDYPEDRIRYMLEDSGAKLLLVQghlldrASFADKLVNLNDD--GAYH----EDGSNLEPVNG------------PEHL 6077
Cdd:PRK07798   84 NYRYVEDELRYLLDDSDAVALVYE------REFAPRVAEVLPRlpKLRTlvvvEDGSGNDLLPGavdyedalaagsPERD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6078 --------TYVIYTSGTTGRPKGVMVEHRNVVRLVKN----------TNYVELNEQThILQTGAVVFD-------ASTFE 6132
Cdd:PRK07798  158 fgerspddLYLLYTGGTTGMPKGVMWRQEDIFRVLLGgrdfatgepiEDEEELAKRA-AAGPGMRRFPapplmhgAGQWA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6133 IWGALLNGGRLYVVRNETiLDAVSLKNAIQQYGINTMWLT-----APLYNQLSQQDSGMFAGLKTLIVGGDVLSvPHINR 6207
Cdd:PRK07798  237 AFAALFSGQTVVLLPDVR-FDADEVWRTIEREKVNVITIVgdamaRPLLDALEARGPYDLSSLFAIASGGALFS-PSVKE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6208 VLREH-AGLSIVNGYGPTEnTTFSTTHTIvgeQKEAVPIGKP---INNSTAyIVDSKLSLLPVGvwgeliVGGDG-VAR- 6281
Cdd:PRK07798  315 ALLELlPNVVLTDSIGSSE-TGFGGSGTV---AKGAVHTGGPrftIGPRTV-VLDEDGNPVEPG------SGEIGwIARr 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6282 -----GYLNRPELTAEKFVESSflpGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEAT 6356
Cdd:PRK07798  384 ghiplGYYKDPEKTAETFPTID---GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADAL 460
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 6357 VIVREDES-GQKqlCAYFVAERE---LTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRR 6418
Cdd:PRK07798  461 VVGVPDERwGQE--VVAVVQLREgarPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
3232-3384 8.89e-53

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 184.40  E-value: 8.89e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3232 DISYLLKKTKEDLRGIPNKGIGYGICRYLSAAKNDIAWGAEPEVSFNYLGQFDQDLQNSDIGVSAHTGGKQSSDRQKRIF 3311
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKLAASPQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRPY 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928  3312 VLDINGMIADGTLSLELSYNGKEYRRETMERLAASLQESLRVIIAHCVSKERAELTPSDVQFKGLSVEELEQI 3384
Cdd:TIGR01720   81 ALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
8035-8446 1.04e-52

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 194.62  E-value: 1.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8035 PVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYsDVEFA---VE 8111
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIL-DADAArpeLP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8112 YSKADREEAVE-IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGE------ELP 8184
Cdd:cd19546    85 VVPATEEELPAlLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrapERA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8185 PLRIQYKDYAAWQRSEAYAKR-----VKQQEGYWLQTLAGELPVIELPTDYERTSTRSFEGAELEFEADEALTQRLNELA 8259
Cdd:cd19546   165 PLPLQFADYALWERELLAGEDdrdslIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8260 ARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRT-HADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGA 8338
Cdd:cd19546   245 ESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREA 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8339 FEHQDYPFEELVERLNVKRDASRNPVFDTmfVLQNTEDRGIEADAFSL----TPFVFDQTVAAQFDLTLSVAE---DDGA 8411
Cdd:cd19546   325 RRHQDVPFERLAELLALPPSADRHPVFQV--ALDVRDDDNDPWDAPELpglrTSPVPLGTEAMELDLSLALTErrnDDGD 402
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 386647928 8412 ---IRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19546   403 pdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
2371-2823 1.64e-52

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 194.14  E-value: 1.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQR 2450
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2451 RLQERvsfagtvvtvdDEQAYagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVV 2530
Cdd:cd05903    82 RFRQF-----------DPAAM------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2531 QFASLS-FDASCWEVFQTLFFGATLYIptkETILDYQWFERYMSDNGITTATLPPTY------AVYLNPDHMPDFKRLIA 2603
Cdd:cd05903   139 VASPMAhQTGFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMMGATPFltdllnAVEEAGEPLSRLRTFVC 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2604 AGSASSLELLQQWKDK--VKYFNAYGPTEdsiCTTIWTPSTEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELC 2681
Cdd:cd05903   216 GGATVPRSLARRAAELlgAKVCSAYGSTE---CPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELL 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2682 IAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRiDHQVKIR-GYRIELGEIEEQLLKVASV 2760
Cdd:cd05903   293 SRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLEVEDLLLGHPGV 364
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 2761 QEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGE-LPGYMIPAHFVQLERMPLTPNGKI 2823
Cdd:cd05903   365 IEAAVVALPDERLGERACAVVVtkSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
4902-5385 2.57e-52

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 193.66  E-value: 2.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4902 EAAAVVYENDRLTYRELNERANRLARTLRAQG-VKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLtqthlqeraqqwgqtlqaalclddeaayaedasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd05941    81 TDSEPSLVL------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANV 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDdriDPARLHYWISEEKITIFESTPALIIPFMDY 5140
Cdd:cd05941   119 RALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTIYTRLLQY 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5141 VAEHGLDM--------SSMVLLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAIDSSlydEPLAKLPEAGNVpiGK 5212
Cdd:cd05941   196 YEAHFTDPqfaraaaaERLRLMVSGSAALPVPTLEEWEAITGH--TLLERYGMTEIGMALS---NPLDGERRPGTV--GM 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5213 AALNAKFYIVDAHLN-PVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRI 5291
Cdd:cd05941   269 PLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRS 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5292 -DNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVlCAHFTAESE---LKLSELRSSLSQELPGYMIPSYF 5366
Cdd:cd05941   343 sVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGERV-VAVVVLRAGaaaLSLEELKEWAKQRLAPYKRPRRL 421
                         490
                  ....*....|....*....
gi 386647928 5367 VQLEQLPLTANGKIDRKAL 5385
Cdd:cd05941   422 ILVDELPRNAMGKVNKKEL 440
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
293-747 3.42e-52

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 193.81  E-value: 3.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  293 ERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGA----YVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQ 368
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  369 ERVSFS-------GTWIRLDDEEAyheDGSNLESV-NGPEHLTYVIYTSGTTGKPKGNLTTHRNIIrvvKNTN----YID 436
Cdd:cd05922    81 DRLRDAlpaspdpGTVLDADGIRA---ARASAPAHeVSHEDLALLLYTSGSTGSPKLVRLSHQNLL---ANARsiaeYLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  437 VTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVL----VPKETVLDvaklagLIEKQQISVMFITTAFFNVL--VDMNPD 510
Cdd:cd05922   155 ITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLtndgVLDDAFWE------DLREHGATGLAGVPSTYAMLtrLGFDPA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  511 CLRHARAILFGGERVSVSHVRkALGHLGPG-KIKHVYGPTESTVFATSYDVHEVEEGAVSIpiGGPISNTAIYIVNAQNK 589
Cdd:cd05922   229 KLPSLRYLTQAGGRLPQETIA-RLRELLPGaQVYVMYGQTEATRRMTYLPPERILEKPGSI--GLAIPGGEFEILDDDGT 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  590 LQPIGVAGELCVAGDGLARGYLNRPDLTAEkfadnPFAPGERMYrTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEI 669
Cdd:cd05922   306 PTPPGEPGEIVHRGPNVMKGYWNDPPYRRK-----EGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  670 EAHLLKLEAIEKATVVVRESANGEKqLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05922   380 EAAARSIGLIIEAAAVGLPDPLGEK-LALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
5492-5902 4.63e-52

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 192.69  E-value: 4.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5492 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEVNFAVEHYR 5571
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5572 TSEAEA---GEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGE------SLAP 5642
Cdd:cd19546    86 VPATEEelpALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrapERAP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5643 LRIQYKDYATWQQSEAQQEQ-----MKRQEAYWLDMFRGELPVLELPTDYPRPAVRKFEGSLLQRQLEPKLGEGLQRIAA 5717
Cdd:cd19546   166 LPLQFADYALWERELLAGEDdrdslIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5718 ESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRT-HSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETMLGAY 5796
Cdd:cd19546   246 SAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREAR 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5797 EHQSYPFEELVEKAQPARDLSRNPLFDTLFALQNKETGEL---QLDGLRLTPYPAEHTVAKFDLSVDVTE------GSEG 5867
Cdd:cd19546   326 RHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWdapELPGLRTSPVPLGTEAMELDLSLALTErrnddgDPDG 405
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 386647928 5868 LELSMEYSTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19546   406 LDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3878-4337 7.57e-52

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 192.26  E-value: 7.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3878 SQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLT 3957
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3958 qrhlrervsfagtfvavddeqayhaDGSNlEPvvgpnhlAYVIYTSGTTGKPKGVMVEHHGLcslkLMFANTLQMTeQDR 4037
Cdd:cd05971    85 -------------------------DGSD-DP-------ALIIYTSGTTGPPKGALHAHRVL----LGHLPGVQFP-FNL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4038 VVQFASLSFDASCWE--------IFKALFFGATLYIPTSTTILDYPLFEsYMNENGITATILPPTY-----AAYLNPDRM 4104
Cdd:cd05971   127 FPRDGDLYWTPADWAwigglldvLLPSLYFGVPVLAHRMTKFDPKAALD-LMSRYGVTTAFLPPTAlkmmrQQGEQLKHA 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4105 P-SLKKLITGGSAASVEFVQQWKD--KVLYFNAYGPTEASIVTSiwdeASDSLGDRKSVPIGRPLANHRIYVVDSHNRML 4181
Cdd:cd05971   206 QvKLRAIATGGESLGEELLGWAREqfGVEVNEFYGQTECNLVIG----NCSALFPIKPGSMGKPIPGHRVAIVDDNGTPL 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4182 PVGVAGELCI---SGVGLArGYLNRPELTAEKFVDNPFepgermyRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGE 4258
Cdd:cd05971   282 PPGEVGEIAVelpDPVAFL-GYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAE 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4259 VETQLAKIDAVQEAIVLAREDANGQQQLVAYFV-AQRELT----AAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:cd05971   354 IEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlNPGETPsdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIR 433

                  ....
gi 386647928 4334 RKAL 4337
Cdd:cd05971   434 RREL 437
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3887-4337 1.17e-51

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 192.27  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3887 ERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGA----YIPIDPEYPEDRIRYMLEDSGAQALLTQRHLR 3962
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3963 ERVSFAGTfVAVD-----DEQAYHADGSNLE--PVVGPNhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQ 4035
Cdd:cd05922    81 DRLRDALP-ASPDpgtvlDADGIRAARASAPahEVSHED-LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4036 DRVVQFASLSFDASCWEIFKALFFGATLYIpTSTTILDYPLFESyMNENGITA-TILPPTYA----AYLNPDRMPSLKKL 4110
Cdd:cd05922   159 DRALTVLPLSYDYGLSVLNTHLLRGATLVL-TNDGVLDDAFWED-LREHGATGlAGVPSTYAmltrLGFDPAKLPSLRYL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4111 ITGGSAASVEFVQQWKDKV----LYFnAYGPTEASIVTSIWDEasdSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVA 4186
Cdd:cd05922   237 TQAGGRLPQETIARLRELLpgaqVYV-MYGQTEATRRMTYLPP---ERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4187 GELCISGVGLARGYLNRPELTAEkfvdnPFEPGERMYrTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKI 4266
Cdd:cd05922   313 GEIVHRGPNVMKGYWNDPPYRRK-----EGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 4267 DAVQEAIVLAREDANGqQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05922   387 GLIIEAAAVGLPDPLG-EKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2931-3172 1.80e-51

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 184.09  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2931 LTPIQHWFFepqFAEP--HHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHkSENGyTAWNRAIGEGELYgLEV 3008
Cdd:COG4908     1 LSPAQKRFL---FLEPgsNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFV-EEDG-EPVQRIDPDADLP-LEV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3009 VDLKGIEESAQAVEAK---ANEIQSSIDLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKG 3084
Cdd:COG4908    75 VDLSALPEPEREAELEelvAEEASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAALYAALLEG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3085 EELRFPAKTDAYRTWSEQLAAYAQSPVIERELAYWKRVAQ--TEVQPLPKDEQVDVSLQQDSESISIEWTREETEQLLKG 3162
Cdd:COG4908   155 EPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAgaPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKAL 234
                         250
                  ....*....|
gi 386647928 3163 VhRAYNTEMN 3172
Cdd:COG4908   235 A-KAHGATVN 243
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
4889-5385 2.92e-51

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 192.71  E-value: 2.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4889 FHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 4968
Cdd:PRK06187    8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4969 PDYPSDRIQFMLEDSAASVLLT-QTHLQERAQQWGQ--TLQAALCLDDEAAYAEDASNVANVN--------------EPH 5031
Cdd:PRK06187   88 IRLKPEEIAYILNDAEDRVVLVdSEFVPLLAAILPQlpTVRTVIVEGDGPAAPLAPEVGEYEEllaaasdtfdfpdiDEN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5032 DLAYVIYTSGTTGRPKGVMIEHRSLV------NTAAGYRREyrlDQFPVRLLQLASFSFDVFVgdiaRTLYNGGTMVIcP 5105
Cdd:PRK06187  168 DAAAMLYTSGTTGHPKGVVLSHRNLFlhslavCAWLKLSRD---DVYLVIVPMFHVHAWGLPY----LALMAGAKQVI-P 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5106 kdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQFriINAYGV 5185
Cdd:PRK06187  240 --RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDL--VQGYGM 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5186 TEAA-IDSSLY--DEPLAKLPEAGNVpiGKAALNAKFYIVDAHLNPVPV--GVLGELCIGGIGVARGYLNRPELTEEKFV 5260
Cdd:PRK06187  316 TETSpVVSVLPpeDQLPGQWTKRRSA--GRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETID 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5261 DSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLcAHFT 5339
Cdd:PRK06187  394 GG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPV-AVVV 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 5340 AESELKLS--ELRSSLSQELPGYMIPS--YFVqlEQLPLTANGKIDRKAL 5385
Cdd:PRK06187  466 LKPGATLDakELRAFLRGRLAKFKLPKriAFV--DELPRTSVGKILKRVL 513
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
2372-2828 4.30e-51

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 189.97  E-value: 4.30e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2372 TYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRR 2451
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2452 LQERVSfagTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGV-----MVEHHGLCSlkqmfANTLQINAQ 2526
Cdd:TIGR01923   81 LEEKDF---QADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVphtfrNHYASAVGS-----KENLGFTED 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2527 DR------VVQFASLSFdascweVFQTLFFGATLYIPTKetilDYQWFEryMSDNG-ITTATLPPT-YAVYLNPDHMPD- 2597
Cdd:TIGR01923  153 DNwllslpLYHISGLSI------LFRWLIEGATLRIVDK----FNQLLE--MIANErVTHISLVPTqLNRLLDEGGHNEn 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2598 FKRLIAAGSASSLELLQQWKDK-VKYFNAYGPTEdsICTTIWTPSTEDISQLKSVpiGGPIVNHRIYIvdahYQPVPVGV 2676
Cdd:TIGR01923  221 LRKILLGGSAIPAPLIEEAQQYgLPIYLSYGMTE--TCSQVTTATPEMLHARPDV--GRPLAGREIKI----KVDNKEGH 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2677 aGELCIAGVGLARGYLNRPDLTAEKFVDNPFEpgermyrTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLK 2756
Cdd:TIGR01923  293 -GEIMVKGANLMKGYLYQGELTPAFEQQGWFN-------TGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQ 364
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  2757 VASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:TIGR01923  365 HPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
4443-4854 6.63e-51

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 188.28  E-value: 6.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4443 YPVSSAQKrlYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEP--VQRIYPEVDFAVE 4520
Cdd:cd19542     2 YPCTPMQE--GMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtfLQVVLKSLDPPIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4521 TVQASEQEAKAIVRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGEELPGlRIQYK 4600
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPFS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4601 DYAVWQQSEAQKEQLkrqeAYWLEAFRGELPVLEMPTDYARPAVQSyagdtldFRMNSEISEGLKRIAAESGATLYMVLL 4680
Cdd:cd19542   159 DYISYLQSQSQEESL----QYWRKYLQGASPCAFPSLSPKRPAERS-------LSSTRRSLAKLEAFCASLGVTLASLFQ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4681 AAYTVLLQKYTAQEDVIVGTPIAGRT--HADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFEHQTYPFEEL 4758
Cdd:cd19542   228 AAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4759 VDKLQMARDLsrnPLFDTMFSLQNTENKEMHLPGLHLTPY------PTEYgmskfDLSLDMMEDSEGLECSLEFATALYK 4832
Cdd:cd19542   308 QRALGLWPSG---TLFNTLVSYQNFEASPESELSGSSVFElsaaedPTEY-----PVAVEVEPSGDSLKVSLAYSTSVLS 379
                         410       420
                  ....*....|....*....|..
gi 386647928 4833 RETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19542   380 EEQAEELLEQFDDILEALLANP 401
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
3868-4337 9.24e-51

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 190.60  E-value: 9.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKS--QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRY 3945
Cdd:cd05926     1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3946 MLEDSGAQALLTQR-----HLRERVSFAGTFV--AVDDEQAYHADGSN-------------LEPVVGPNHLAYVIYTSGT 4005
Cdd:cd05926    81 YLADLGSKLVLTPKgelgpASRAASKLGLAILelALDVGVLIRAPSAEslsnlladkknakSEGVPLPDDLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4006 TGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVV----------QFASL--------------SFDASC-WEIFKAlfFG 4060
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfhvhgLVASLlstlaaggsvvlppRFSASTfWPDVRD--YN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4061 ATLY--IPTSTTILdyplfesYMNENGITATILPP-----TYAAYLNPDRMPSLKKLItggsAASVefvqqwkdkvlyFN 4133
Cdd:cd05926   239 ATWYtaVPTIHQIL-------LNRPEPNPESPPPKlrfirSCSASLPPAVLEALEATF----GAPV------------LE 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4134 AYGPTEAS-IVTSiwdeasDSL--GDRKSVPIGRPLANhRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEK 4210
Cdd:cd05926   296 AYGMTEAAhQMTS------NPLppGPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEA 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4211 FVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYF 4290
Cdd:cd05926   369 AFKDGW------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAV 442
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 4291 VAQR--ELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05926   443 VLREgaSVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
2359-2828 1.12e-50

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 190.66  E-value: 1.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLAQRRLQERVSFAG--------TVVTVDDEQAYAGDGSNLE-----------SAVGPNDLAYIIYTSGTTGK 2499
Cdd:cd05959    98 EDSRARVVVVSGELAPVLAAALtksehtlvVLIVSGGAGPEAGALLLAElvaaeaeqlkpAATHADDPAFWLYSSGSTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2500 PKGVMVEHHGLCSLKQMFA-NTLQINAQDRVVQFASLSFdasCWEVFQTLFF----GATLYI----PTKETILDYqwFER 2570
Cdd:cd05959   178 PKGVVHLHADIYWTAELYArNVLGIREDDVCFSAAKLFF---AYGLGNSLTFplsvGATTVLmperPTPAAVFKR--IRR 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2571 YMSDngITTAtLPPTYAVYLNPDHMP--DFKRL---IAAGSASSLELLQQWKDK--VKYFNAYGPTEdsiCTTIWTPSTE 2643
Cdd:cd05959   253 YRPT--VFFG-VPTLYAAMLAAPNLPsrDLSSLrlcVSAGEALPAEVGERWKARfgLDILDGIGSTE---MLHIFLSNRP 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2644 DISQLKSVpiGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVdnpfepGErMYRTGDLAKWL 2723
Cdd:cd05959   327 GRVRYGTT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRD 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2724 PDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV-ADRTMTVGELRGEL----SG 2798
Cdd:cd05959   398 DDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlRPGYEDSEALEEELkefvKD 477
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 2799 ELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05959   478 RLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
5952-6420 1.20e-50

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 190.22  E-value: 1.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5952 LAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDS 6031
Cdd:cd05926     6 LVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6032 GAKLLLVQGH------------------------LLDRASFADKLVNLNDDGayheDGSNLEPVNGPEHLTYVIYTSGTT 6087
Cdd:cd05926    86 GSKLVLTPKGelgpasraasklglailelaldvgVLIRAPSAESLSNLLADK----KNAKSEGVPLPDDLALILHTSGTT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6088 GRPKGVMVEHRNVVRLVKN-TNYVELNEQT---------HI-------LQT----GAVV----FDASTFeiWgallnggr 6142
Cdd:cd05926   162 GRPKGVPLTHRNLAASATNiTNTYKLTPDDrtlvvmplfHVhglvaslLSTlaagGSVVlpprFSASTF--W-------- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6143 lyvvrnetildavslkNAIQQYGINtmWLTA-P-----LYNQLSQQDSGMFAGLKTLIVGGDVLSVPHINRvLREHAGLS 6216
Cdd:cd05926   232 ----------------PDVRDYNAT--WYTAvPtihqiLLNRPEPNPESPPPKLRFIRSCSASLPPAVLEA-LEATFGAP 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6217 IVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAyIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVE 6296
Cdd:cd05926   293 VLEAYGMTEAAHQMTSNPLPPGPRKPGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFK 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6297 SSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE 6376
Cdd:cd05926   372 DGWF------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR 445
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 386647928 6377 R--ELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05926   446 EgaSVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
8034-8446 2.10e-50

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 186.74  E-value: 2.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8034 YPVSSAQKrlFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGF--EMANGEPVQRVYSDVE-FAV 8110
Cdd:cd19542     2 YPCTPMQE--GMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLKSLDpPIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8111 EYSKADREEAVEIAQRFVRPFDLRKPPLlRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGEELPPlRIQY 8190
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDPTLFGQPPH-RLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8191 KDYAawqrSEAYAKRVKQQEGYWLQTLAGELPViELPTdyertsTRSFEGAELEFEADEALTQRLNELAARHESTLYMVL 8270
Cdd:cd19542   158 SDYI----SYLQSQSQEESLQYWRKYLQGASPC-AFPS------LSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8271 LSAYTVLLSKYSGQEDIIVGTPVAGRT--HADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEE 8348
Cdd:cd19542   227 QAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLRE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8349 LVERLNVKRDASRnpvFDTMFVLQNTEDRGIEADAFSLTPFVFDQTVAAQFDLTLSVAEDDGAIRGSFQYAAKLFKATMI 8428
Cdd:cd19542   307 IQRALGLWPSGTL---FNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQA 383
                         410
                  ....*....|....*...
gi 386647928 8429 RKMSKDLLAVLEQICGNP 8446
Cdd:cd19542   384 EELLEQFDDILEALLANP 401
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1323-1795 2.92e-50

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 189.06  E-value: 2.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ- 1401
Cdd:cd05926    15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPk 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 --------------------THLQERAQQWGQTLQAVLCLDDEAAYAEDAsnvanVNEPHDLAYVIYTSGTTGRPKGVMI 1461
Cdd:cd05926    95 gelgpasraasklglailelALDVGVLIRAPSAESLSNLLADKKNAKSEG-----VPLPDDLALILHTSGTTGRPKGVPL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1462 EHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPkddRIDPARLHYWISEEKITIFESTP 1541
Cdd:cd05926   170 THRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPP---RFSASTFWPDVRDYNATWYTAVP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 ALI-IPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDSSLYDEPLAKlPEAGNVPI 1620
Cdd:cd05926   247 TIHqILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAP--VLEAYGMTEAAHQMTSNPLPPGP-RKPGSVGK 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1621 GKaalNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfvEGERLYRTGDLARWMPDGNVDFIGR 1700
Cdd:cd05926   324 PV---GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA------FKDGWFRTGDLGYLDADGYLFLTGR 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1701 IDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAYFTAESELKLS-ELRSSLSQELPGYMIPSYFVQ 1778
Cdd:cd05926   395 IKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEEVAAAVVLREGASVTEeELRAFCRKHLAAFKVPKKVYF 474
                         490
                  ....*....|....*..
gi 386647928 1779 LEQLPLTANGKIDRKAL 1795
Cdd:cd05926   475 VDELPKTATGKIQRRKV 491
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
2359-2828 3.12e-50

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 189.06  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQ--QLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISY 2436
Cdd:cd05926     1 PDAPALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2437 MLEDSSAQVLL--------AQRRLQERVSF--------AGTVVTVDDEQ----AYAGDGSNLESAVGPNDLAYIIYTSGT 2496
Cdd:cd05926    81 YLADLGSKLVLtpkgelgpASRAASKLGLAilelaldvGVLIRAPSAESlsnlLADKKNAKSEGVPLPDDLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2497 TGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVV----------QFASLSfdascwevfQTLFFGATLYIPTKETILDY- 2565
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfhvhgLVASLL---------STLAAGGSVVLPPRFSASTFw 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2566 QWFERYmsdnGITTATLPPTYAVYLNPDHMPDFK------RLIAAGSAS----SLELLQQwKDKVKYFNAYGPTEDSICT 2635
Cdd:cd05926   232 PDVRDY----NATWYTAVPTIHQILLNRPEPNPEspppklRFIRSCSASlppaVLEALEA-TFGAPVLEAYGMTEAAHQM 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2636 TIwTPSTEDISQLKSVPIGgpiVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYR 2715
Cdd:cd05926   307 TS-NPLPPGPRKPGSVGKP---VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FR 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2716 TGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA-HDDASGQkQLCAYFV--ADRTMTVGEL 2792
Cdd:cd05926   377 TGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGvPDEKYGE-EVAAAVVlrEGASVTEEEL 455
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 2793 RGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05926   456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
7470-7928 5.15e-50

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 186.87  E-value: 5.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7470 TQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLT 7549
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7550 qrhlqecvsfdgkviaaddeqaygeDGSNlEPvvgpnhlAYVIYTSGTTGKPKGVMVEHHGLcslkLMFAETLRITEEdR 7629
Cdd:cd05971    85 -------------------------DGSD-DP-------ALIIYTSGTTGPPKGALHAHRVL----LGHLPGVQFPFN-L 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7630 VVQFASLSFDASCWE--------IFKALFFGATL--YIPAK---DTILDYplfesyMNENGITAAILPPTY-----AIYL 7691
Cdd:cd05971   127 FPRDGDLYWTPADWAwigglldvLLPSLYFGVPVlaHRMTKfdpKAALDL------MSRYGVTTAFLPPTAlkmmrQQGE 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7692 SPDRLP-SLKKLITGGSAASVEFVQQWKD--KVRYFNAYGPTEASIVTSvwaASPDGLDLRSVPIGRPIANHQIFIVDSQ 7768
Cdd:cd05971   201 QLKHAQvKLRAIATGGESLGEELLGWAREqfGVEVNEFYGQTECNLVIG---NCSALFPIKPGSMGKPIPGHRVAIVDDN 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7769 NHMLPVGVAGELCI----SGAGLarGYLNRPELTAEKFVdNPFLagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYR 7844
Cdd:cd05971   278 GTPLPPGEVGEIAVelpdPVAFL--GYWNNPSATEKKMA-GDWL------LTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7845 IELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV-----ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTP 7919
Cdd:cd05971   349 IGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTA 428

                  ....*....
gi 386647928 7920 NGKIDRNAL 7928
Cdd:cd05971   429 TGKIRRREL 437
PRK07798 PRK07798
acyl-CoA synthetase; Validated
2346-2824 6.36e-50

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 188.94  E-value: 6.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI 2425
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2426 DPEYPEDRISYMLEDSSAQVLLAQRRLQERV-----SFAG--TVVTVDDE--QAYAGDGSNLESAVG------------P 2484
Cdd:PRK07798   84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVaevlpRLPKlrTLVVVEDGsgNDLLPGAVDYEDALAagsperdfgersP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2485 NDLaYIIYTSGTTGKPKGVMVEHHGLcSLKQM----FANTLQINAQDRVVQFAS------------LSFDASCWEVFQTL 2548
Cdd:PRK07798  164 DDL-YLLYTGGTTGMPKGVMWRQEDI-FRVLLggrdFATGEPIEDEEELAKRAAagpgmrrfpappLMHGAGQWAAFAAL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2549 FFGATLYIPTKETiLDYQWFERYMSDNGITTATL-------PPTYAvyLNPDHMPDFKRLIAAGSASSL------ELLQQ 2615
Cdd:PRK07798  242 FSGQTVVLLPDVR-FDADEVWRTIEREKVNVITIvgdamarPLLDA--LEARGPYDLSSLFAIASGGALfspsvkEALLE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2616 WKDKVKYFNAYGPTEDSICTTIWTPStedisqlKSVPIGGPIV--NHRIYIVDAHYQPVPVGVAGELCIAGVG-LARGYL 2692
Cdd:PRK07798  319 LLPNVVLTDSIGSSETGFGGSGTVAK-------GAVHTGGPRFtiGPRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYY 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2693 NRPDLTAEKF--VDnpfepGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVI-AHD 2769
Cdd:PRK07798  392 KDPEKTAETFptID-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVgVPD 466
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2770 DASGQK-----QLcayfVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKID 2824
Cdd:PRK07798  467 ERWGQEvvavvQL----REGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
7462-7928 7.33e-50

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 186.13  E-value: 7.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7462 KAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLED 7541
Cdd:cd05919     1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7542 SGAQVLltqrhlqecvsfdgkVIAADDeqaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMFAE 7620
Cdd:cd05919    81 CEARLV---------------VTSADD-------------------IAYLLYSSGTTGPPKGVMHAHRDpLLFADAMARE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7621 TLRITEEDRVVQFASLSFdasCWEIFKALFFGatLYIPAKDTILD-YPLFESYMnengITAAILPPTY-----AIY---- 7690
Cdd:cd05919   127 ALGLTPGDRVFSSAKMFF---GYGLGNSLWFP--LAVGASAVLNPgWPTAERVL----ATLARFRPTVlygvpTFYanll 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7691 ----LSPDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEasIVTSVWAASPDglDLRSVPIGRPIANHQIFI 7764
Cdd:cd05919   198 dscaGSPDALRSLRLCVSAGEALPRGLGERWMEHfgGPILDGIGATE--VGHIFLSNRPG--AWRLGSTGRPVPGYEIRL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7765 VDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFvdnpflAGErMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYR 7844
Cdd:cd05919   274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7845 IELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSE-----LRGTLSQELPGYMIPSYFVQLEQMPLTP 7919
Cdd:cd05919   347 VSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslardIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                  ....*....
gi 386647928 7920 NGKIDRNAL 7928
Cdd:cd05919   427 TGKLQRFKL 435
PRK06178 PRK06178
acyl-CoA synthetase; Validated
2355-2828 8.04e-50

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 189.87  E-value: 8.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRI 2434
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 SYMLEDSSAQVLLAQRRLQERV---------------SFAGTV---------VTVDDEQAYAGDGSNLESA--------- 2481
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAPVVeqvraetslrhvivtSLADVLpaeptlplpDSLRAPRLAAAGAIDLLPAlractapvp 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2482 ---VGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVqfasLSFDASCW---EVFQTL---FFGA 2552
Cdd:PRK06178  203 lppPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVF----LSFLPEFWiagENFGLLfplFSGA 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2553 TLYIPTKetiLDYQWFERYMSDNGITTATLPPTYAVYL--NPD-HMPDFKRLIAAGSAS-----SLELLQQWKD---KVK 2621
Cdd:PRK06178  279 TLVLLAR---WDAVAFMAAVERYRVTRTVMLVDNAVELmdHPRfAEYDLSSLRQVRVVSfvkklNPDYRQRWRAltgSVL 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2622 YFNAYGPTEDSICTTIWTPSTEDISQLKSVPI--GGPIVNHRIYIVD-AHYQPVPVGVAGELCIAGVGLARGYLNRPDLT 2698
Cdd:PRK06178  356 AEAAWGMTETHTCDTFTAGFQDDDFDLLSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEAT 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2699 AEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDAsGQKQLC 2778
Cdd:PRK06178  436 AEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDP-DKGQVP 507
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2779 AYFV---ADRTMTVGELRGELSGELPGYMIPAHFVqLERMPLTPNGKIDRKAL 2828
Cdd:PRK06178  508 VAFVqlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
4913-5385 9.46e-50

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 187.52  E-value: 9.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 4992
Cdd:cd05926    15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 HLQERAQQWGQTLQAA---LCLDDEAAY----AEDASNVANVN---------EPHDLAYVIYTSGTTGRPKGVMIEHRSL 5056
Cdd:cd05926    95 GELGPASRAASKLGLAileLALDVGVLIrapsAESLSNLLADKknaksegvpLPDDLALILHTSGTTGRPKGVPLTHRNL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5057 VNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPkddRIDPARLHYWISEEKITIFESTPALI-I 5135
Cdd:cd05926   175 AASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPP---RFSASTFWPDVRDYNATWYTAVPTIHqI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5136 PFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDSSLYDEPLAKlPEAGNVPIGKaal 5215
Cdd:cd05926   252 LLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAP--VLEAYGMTEAAHQMTSNPLPPGP-RKPGSVGKPV--- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5216 NAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfvEGERLYRTGDLARWMPDGNVDFIGRIDNQA 5295
Cdd:cd05926   326 GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA------FKDGWFRTGDLGYLDADGYLFLTGRIKELI 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5296 KIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAHFTAESELKLS-ELRSSLSQELPGYMIPSYFVQLEQLP 5373
Cdd:cd05926   400 NRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEEVAAAVVLREGASVTEeELRAFCRKHLAAFKVPKKVYFVDELP 479
                         490
                  ....*....|..
gi 386647928 5374 LTANGKIDRKAL 5385
Cdd:cd05926   480 KTATGKIQRRKV 491
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
3869-4337 1.15e-49

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 185.96  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3869 DAVAVVFEKSQLTYGELNERANRLARTL-RDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLtqrhlrervsfagtfvavddeqayhadgsnlepvvgpnHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 4027
Cdd:cd05941    81 TDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4028 NTLQMTEQDRVVQ--------------FASL----------SFDASCWEIFKA-----LFFGA-TLYiptsTTILDYPlf 4077
Cdd:cd05941   123 DAWRWTEDDVLLHvlplhhvhglvnalLCPLfagasveflpKFDPKEVAISRLmpsitVFMGVpTIY----TRLLQYY-- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4078 esymnengiTATILPPTYAAYLNPDRMpslkKLITGGSAA-SVEFVQQWKDK----VLyfNAYGPTEASIVTSiwdeasD 4152
Cdd:cd05941   197 ---------EAHFTDPQFARAAAAERL----RLMVSGSAAlPVPTLEEWEAItghtLL--ERYGMTEIGMALS------N 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4153 SL-GDRKSVPIGRPLANHRIYVVD-SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVR 4230
Cdd:cd05941   256 PLdGERRPGTVGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGV 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4231 WLPDGNLEYLGRI-DHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRE---LTAAELRATMS 4306
Cdd:cd05941   330 VDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaaaLSLEELKEWAK 409
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 4307 QELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05941   410 QRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
275-747 1.63e-49

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 185.19  E-value: 1.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  275 DAVAVTFEDRQLTYGELNERANRLARTL-RNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSqghlqervsfsgtwirlddeeayhedgsnlesvngpehLTYVIYTSGTTGKPKGNLTTHRNIIRVVKN-T 432
Cdd:cd05941    81 TDSEPSLVLD--------------------------------------PALILYTSGTTGRPKGVVLTHANLAANVRAlV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  433 NYIDVTGQDKLLQ-LSSYSFDGSTFDIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVMFITTAFFNVL---VDMN 508
Cdd:cd05941   123 DAWRWTEDDVLLHvLPLHHVHGLVNALLCPLFAGASVEFLPK---FDPKEVAISRLMPSITVFMGVPTIYTRLlqyYEAH 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  509 PDCLRHARAILFGGERVSVS-------HVRKALGHLGPGKIKHVYGPTEsTVFATSYDVH-EVEEGAVsipiGGPISNTA 580
Cdd:cd05941   200 FTDPQFARAAAAERLRLMVSgsaalpvPTLEEWEAITGHTLLERYGMTE-IGMALSNPLDgERRPGTV----GMPLPGVQ 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  581 IYIV-NAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRI-DDQVK 658
Cdd:cd05941   275 ARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsVDIIK 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  659 IRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKqLCAYYVADRSLPA---NEVRSTLSQELPAYMLPSYFVQLEQM 734
Cdd:cd05941   349 SGGYKVSALEIERVLLAHPGVSECAVIgVPDPDWGER-VVAVVVLRAGAAAlslEELKEWAKQRLAPYKRPRRLILVDEL 427
                         490
                  ....*....|...
gi 386647928  735 PLTTNGKVDRRAL 747
Cdd:cd05941   428 PRNAMGKVNKKEL 440
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2372-2828 2.11e-49

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 184.94  E-value: 2.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2372 TYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVllaqrr 2451
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2452 lqervsfagtVVTvddeqayagDGSNlesavgpnDLAYIIYTSGTTGKPKGVMVEHHGLCSlkqmFANTLQInAQDRVVQ 2531
Cdd:cd05971    82 ----------LVT---------DGSD--------DPALIIYTSGTTGPPKGALHAHRVLLG----HLPGVQF-PFNLFPR 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2532 FASLSFDASCWE--------VFQTLFFGATL--YIPTK---ETILDYqwferyMSDNGITTATLPPTY-----AVYLNPD 2593
Cdd:cd05971   130 DGDLYWTPADWAwigglldvLLPSLYFGVPVlaHRMTKfdpKAALDL------MSRYGVTTAFLPPTAlkmmrQQGEQLK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2594 HMPDFKRLIAAGSASSLELLQQW-KD--KVKYFNAYGPTEDSICTTiwtpSTEDISQLKSVPIGGPIVNHRIYIVDAHYQ 2670
Cdd:cd05971   204 HAQVKLRAIATGGESLGEELLGWaREqfGVEVNEFYGQTECNLVIG----NCSALFPIKPGSMGKPIPGHRVAIVDDNGT 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2671 PVPVGVAGELCIA---GVGLArGYLNRPDLTAEKFVDNPFepgermyRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIEL 2747
Cdd:cd05971   280 PLPPGEVGEIAVElpdPVAFL-GYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2748 GEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMT-----VGELRGELSGELPGYMIPAHFVQLERMPLTPNGK 2822
Cdd:cd05971   352 AEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETpsdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGK 431

                  ....*.
gi 386647928 2823 IDRKAL 2828
Cdd:cd05971   432 IRRREL 437
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
3880-4332 3.17e-49

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 184.51  E-value: 3.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQR 3959
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 HLRERvsfagtfvavddeqayhadgsnlEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVV 4039
Cdd:cd05903    82 RFRQF-----------------------DPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4040 QFASLS-FDASCWEIFKALFFGATLYI-----PTSTTILdyplfesyMNENGITATILPPTYAAYL------NPDRMPSL 4107
Cdd:cd05903   139 VASPMAhQTGFVYGFTLPLLLGAPVVLqdiwdPDKALAL--------MREHGVTFMMGATPFLTDLlnaveeAGEPLSRL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4108 KKLITGGSAASVEFVQQWKDK--VLYFNAYGPTE-ASIVTSIwdeaSDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVG 4184
Cdd:cd05903   211 RTFVCGGATVPRSLARRAAELlgAKVCSAYGSTEcPGAVTSI----TPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4185 VAGELCISGVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRiDHQVKIR-GYRIELGEVETQL 4263
Cdd:cd05903   287 VEGELLSRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLEVEDLL 358
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 4264 AKIDAVQEAIVLAREDANGQQQLVAYFVAQR--ELTAAELRATMS-QELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:cd05903   359 LGHPGVIEAAVVALPDERLGERACAVVVTKSgaLLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5968-6420 5.97e-49

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 184.18  E-value: 5.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5968 ERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGA----YVPIDPDYPEDRIRYMLEDSGAKLLLVQGHLL 6043
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6044 DRASFA-----DKLVNLNDDGAYHeDGSNLEPV-NGPEHLTYVIYTSGTTGRPKGVMVEHRNvvrLVKNTN----YVELN 6113
Cdd:cd05922    81 DRLRDAlpaspDPGTVLDADGIRA-ARASAPAHeVSHEDLALLLYTSGSTGSPKLVRLSHQN---LLANARsiaeYLGIT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6114 EQTHILQTGAVVFDASTFEIWGALLNGGRLyVVRNETILDAvSLKNAIQQYGINTMWLTAPLYNQLSQQ--DSGMFAGLK 6191
Cdd:cd05922   157 ADDRALTVLPLSYDYGLSVLNTHLLRGATL-VLTNDGVLDD-AFWEDLREHGATGLAGVPSTYAMLTRLgfDPAKLPSLR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6192 TLIVGGDVLSVPHINRvLREHA-GLSIVNGYGPTENTTFSTT--HTIVGEQKEAvpIGKPINNSTAYIVDSKLSLLPVGV 6268
Cdd:cd05922   235 YLTQAGGRLPQETIAR-LRELLpGAQVYVMYGQTEATRRMTYlpPERILEKPGS--IGLAIPGGEFEILDDDGTPTPPGE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6269 WGELIVGGDGVARGYLNRPELTAEKFvessfLPGERCYrTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLK 6348
Cdd:cd05922   312 PGEIVHRGPNVMKGYWNDPPYRRKEG-----RGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 6349 VASVKEATVIVREDESGQKqLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05922   386 IGLIIEAAAVGLPDPLGEK-LALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
5961-6422 6.54e-49

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 183.47  E-value: 6.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQG 6040
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 HLLDRASfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYV-ELNEQTHIL 6119
Cdd:cd05969    81 ELYERTD--------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVlDLHPDDIYW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6120 QTGAVVFDASTFE-IWGALLNGGRLYVVRNEtiLDAVSLKNAIQQYGInTMWLTAPL-YNQLSQQDSGMFA-----GLKT 6192
Cdd:cd05969   135 CTADPGWVTGTVYgIWAPWLNGVTNVVYEGR--FDAESWYGIIERVKV-TVWYTAPTaIRMLMKEGDELARkydlsSLRF 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6193 LIVGGDVLSvPHINRVLREHAGLSIVNGYGPTEnttfstTHTIVGEQKEAVPI-----GKPINNSTAYIVDSKLSLLPVG 6267
Cdd:cd05969   212 IHSVGEPLN-PEAIRWGMEVFGVPIHDTWWQTE------TGSIMIANYPCMPIkpgsmGKPLPGVKAAVVDENGNELPPG 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6268 VWGELIVGGD--GVARGYLNRPEltaeKFvESSFLPGerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQ 6345
Cdd:cd05969   285 TKGILALKPGwpSMFRGIWNDEE----RY-KNSFIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESA 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6346 LLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGElraALSQELPNYM---IPSHFVPLE-----RMPLTPNGKIDR 6417
Cdd:cd05969   358 LMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD---ELKEEIINFVrqkLGAHVAPREiefvdNLPKTRSGKIMR 434

                  ....*
gi 386647928 6418 RALPA 6422
Cdd:cd05969   435 RVLKA 439
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
7437-7886 1.03e-48

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 187.23  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7437 NTAAEYAREQTIHGLFEEQAERMPEKAAV-VFENTQ---LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVG 7512
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALrEKEDGIwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7513 AFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQ---------------RHLQECVSFDGKVIAADDE-------Q 7570
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdqeqldkllevrdelPSLRHIVVLDPRGLRDDPRllsldelL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7571 AYGEDGSNLEPV------VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLS--FdASC 7642
Cdd:COG1022   162 ALGREVADPAELearraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAhvF-ERT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7643 WEIFkALFFGATLYIPAK-DTILDY-----P--------LFESYMneNGITAAI--LPPT--------------YAIYLS 7692
Cdd:COG1022   241 VSYY-ALAAGATVAFAESpDTLAEDlrevkPtfmlavprVWEKVY--AGIQAKAeeAGGLkrklfrwalavgrrYARARL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7693 PDRLPSL--------------KKL-----------ITGGSAASVEFvqqwkdkVRYFNA--------YGPTEASIVTSVW 7739
Cdd:COG1022   318 AGKSPSLllrlkhaladklvfSKLrealggrlrfaVSGGAALGPEL-------ARFFRAlgipvlegYGLTETSPVITVN 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7740 aaSPDGLDLRSVpiGRPIANHQIFIVDSqnhmlpvgvaGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDL 7819
Cdd:COG1022   391 --RPGDNRIGTV--GPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGWL------HTGDI 450
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7820 ARWLPDGNIEYLGRIDHQVKIR-GYRIELGEIEEQLLKIASVQETIVIarGDanGQQQLCAYFVADRE 7886
Cdd:COG1022   451 GELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV--GD--GRPFLAALIVPDFE 514
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
7438-7928 1.07e-48

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 186.03  E-value: 1.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7438 TAAEYAREQTIHGLFEEQAERMPEKAAVV------FENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIV 7511
Cdd:PRK13295   16 IAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7512 GAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRH-------------------LQECV--------SFDGKVI 7564
Cdd:PRK13295   96 LYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfdhaamarrlrpelpaLRHVVvvggdgadSFEALLI 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7565 AADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVvqfaslsFDASCWE 7644
Cdd:PRK13295  176 TPAWEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVI-------LMASPMA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7645 IFKALFFGATLYIPAKDT-----ILDYPLFESYMNENGIT---AA---ILPPTYAIYLSPDRLPSLKKLITGGSA---AS 7710
Cdd:PRK13295  249 HQTGFMYGLMMPVMLGATavlqdIWDPARAAELIRTEGVTftmAStpfLTDLTRAVKESGRPVSSLRTFLCAGAPipgAL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7711 VEFVQQ-WKDKVryFNAYGPTEASIVTSVWAASPDglDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLAR 7789
Cdd:PRK13295  329 VERARAaLGAKI--VSAWGMTENGAVTLTKLDDPD--ERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7790 GYLNRPELTAEkfvdnpflAGERMYRTGDLARWLPDGNIEYLGRiDHQVKIRG-YRIELGEIEEQLLKIASVQETIVIAR 7868
Cdd:PRK13295  405 GYLKRPQLNGT--------DADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAY 475
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 7869 GDANGQQQLCAYFV--ADRELTVSELRGTL-SQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK13295  476 PDERLGERACAFVVprPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
7439-7928 1.18e-48

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 185.35  E-value: 1.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7439 AAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMK 7518
Cdd:COG1021    18 EAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7519 AGGayVPID--PEYPEDRIRYMLEDSGAQVLLTQRH------------LQECVSFDGKVIAADD-------EQAYGEDGS 7577
Cdd:COG1021    98 AGA--IPVFalPAHRRAEISHFAEQSEAVAYIIPDRhrgfdyralareLQAEVPSLRHVLVVGDageftslDALLAAPAD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7578 NLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMfAETLRITEEDrvVQFASL----SFDASCWEIFKALFFG 7652
Cdd:COG1021   176 LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDyLYSVRAS-AEICGLDADT--VYLAALpaahNFPLSSPGVLGVLYAG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7653 ATLYI---PAKDTILdyPLFEsymnENGITAAIL-PPTYAIYL-SPDR----LPSLKKLITGGS------AASVE----- 7712
Cdd:COG1021   253 GTVVLapdPSPDTAF--PLIE----RERVTVTALvPPLALLWLdAAERsrydLSSLRVLQVGGAklspelARRVRpalgc 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7713 FVQQWkdkvryfnaYGPTEASI-VTSVwaasPDGLDLRSVPIGRPIANH-QIFIVDSQNHMLPVGVAGELCISGAGLARG 7790
Cdd:COG1021   327 TLQQV---------FGMAEGLVnYTRL----DDPEEVILTTQGRPISPDdEVRIVDEDGNPVPPGEVGELLTRGPYTIRG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7791 YLNRPELTAEKFVDNPFlagermYRTGDLARWLPDGNIEYLGRIDHQVkIR-GYRIELGEIEEQLLKIASVQETIVIARG 7869
Cdd:COG1021   394 YYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMP 466
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 7870 DANGQQQLCAYFVA-DRELTVSELRGTL-SQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:COG1021   467 DEYLGERSCAFVVPrGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1901-2312 1.35e-48

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 181.35  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1901 YPVSSAQKrlYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEP--VQRVYKEVNFAVE 1978
Cdd:cd19542     2 YPCTPMQE--GMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtfLQVVLKSLDPPIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1979 HYRTSEAEAGEVVRGFVRTFDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGESLATlRIQYK 2058
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPFS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2059 DYAVWQQSEEQlervKRQEAYWLDMFRGELPVLEMPTDYPRPAVRRfEGSTLSFRldaglnEALKRVAAESGATLYMVLL 2138
Cdd:cd19542   159 DYISYLQSQSQ----EESLQYWRKYLQGASPCAFPSLSPKRPAERS-LSSTRRSL------AKLEAFCASLGVTLASLFQ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2139 AAYNVMLQKYTGQEDIVIGTPIAGRT--HGDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTLGAYEHQTYPFEEL 2216
Cdd:cd19542   228 AAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2217 VEKLQVPRDLSRnpiFDAMFVLQNTE-NEELQLDGLKLAPYPSGNTIARFDLTLDVTETGSGLECNLEYATSLYARETIA 2295
Cdd:cd19542   308 QRALGLWPSGTL---FNTLVSYQNFEaSPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAE 384
                         410
                  ....*....|....*..
gi 386647928 2296 RMAKHLEQLLTAIAKAP 2312
Cdd:cd19542   385 ELLEQFDDILEALLANP 401
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
2338-2828 1.43e-48

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 184.96  E-value: 1.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2338 AADYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLK 2417
Cdd:COG1021    18 EAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2418 AGGayVPID--PEYPEDRISYMLEDSSAQVLLAQRR------------LQERVSFAGTVVTVDD-------EQAYAGDGS 2476
Cdd:COG1021    98 AGA--IPVFalPAHRRAEISHFAEQSEAVAYIIPDRhrgfdyralareLQAEVPSLRHVLVVGDageftslDALLAAPAD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2477 NLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHG-LCSLKQMfANTLQINAQDrvVQFASL----SFDASCWEVFQTLFFG 2551
Cdd:COG1021   176 LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDyLYSVRAS-AEICGLDADT--VYLAALpaahNFPLSSPGVLGVLYAG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2552 ATLYI---PTKETILDyqWFERYmsdnGIT-TATLPPTYAVYLnpDHMPDFKRLIaagsaSSLELLQ--------QWKDK 2619
Cdd:COG1021   253 GTVVLapdPSPDTAFP--LIERE----RVTvTALVPPLALLWL--DAAERSRYDL-----SSLRVLQvggaklspELARR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2620 VKyfNAYGPT--------------------EDSICTTIWTP-STEDisqlksvpiggpivnhRIYIVDAHYQPVPVGVAG 2678
Cdd:COG1021   320 VR--PALGCTlqqvfgmaeglvnytrlddpEEVILTTQGRPiSPDD----------------EVRIVDEDGNPVPPGEVG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2679 ELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRIDHQVkIR-GYRIELGEIEEQLLKV 2757
Cdd:COG1021   382 ELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAH 454
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2758 ASVQEAIVIA-HDDASGQKqLCAYFVA-DRTMTVGELRGELSG-ELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:COG1021   455 PAVHDAAVVAmPDEYLGER-SCAFVVPrGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1319-1790 1.84e-48

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 183.57  E-value: 1.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1319 ENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVL 1398
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1399 LTQTHLQER----AQQWGqTLQAVLCLDDEAAYAEDA----SNVANVNEPH----------DLAYVIYTSGTTGRPKGVM 1460
Cdd:cd05911    87 FTDPDGLEKvkeaAKELG-PKDKIIVLDDKPDGVLSIedllSPTLGEEDEDlppplkdgkdDTAAILYSSGTTGLPKGVC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1461 IEHRSLV-NTAAGYRREYRLDQFPVRLLQLASFsFDVFvGDIA--RTLYNGGTMVICPKDdriDPARLHYWISEEKITIF 1537
Cdd:cd05911   166 LSHRNLIaNLSQVQTFLYGNDGSNDVILGFLPL-YHIY-GLFTtlASLLNGATVIIMPKF---DSELFLDLIEKYKITFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1538 ESTPALIIpFMdyvAEHGL----DMSSMELLITSSDSCSvtdyRVLQERFGSQF---RIINAYGVTEAAIdsslydePLA 1610
Cdd:cd05911   241 YLVPPIAA-AL---AKSPLldkyDLSSLRVILSGGAPLS----KELQELLAKRFpnaTIKQGYGMTETGG-------ILT 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1611 KLPEAGNVP--IGKAALNAKFYIVDAHLNP-VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegERLYRTGDLA 1687
Cdd:cd05911   306 VNPDGDDKPgsVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIG 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1688 RWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSElrsslsQEL 1767
Cdd:cd05911   380 YFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE------KEV 453
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 1768 PGYM---IPSY--------FVqlEQLPLTANGKI 1790
Cdd:cd05911   454 KDYVakkVASYkqlrggvvFV--DEIPKSASGKI 485
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1320-1796 1.97e-48

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 181.72  E-value: 1.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1320 NDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL 1399
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1400 TqthlqeraqqwgqtlqavlclddeaayaedasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL 1479
Cdd:cd05934    81 V-----------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1480 DQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPkddRIDPARlhYW--ISEEKITIFEstpalIIPFMdyvaehgld 1557
Cdd:cd05934   120 GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP---RFSASR--FWsdVRRYGATVTN-----YLGAM--------- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1558 mssMELLITSSDSCSVTDYRV---------------LQERFGsqFRIINAYGVTEAAIdsslydePLAKLPEAGNVP--I 1620
Cdd:cd05934   181 ---LSYLLAQPPSPDDRAHRLraaygapnppelheeFEERFG--VRLLEGYGMTETIV-------GVIGPRDEPRRPgsI 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1621 GKAALNAKFYIVDAHLNPVPVGVLGELCI---GGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDF 1697
Cdd:cd05934   249 GRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYF 321
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1698 IGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLS--ELRSSLSQELPGYMIPSY 1775
Cdd:cd05934   322 VDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDpeELFAFCEGQLAYFKVPRY 401
                         490       500
                  ....*....|....*....|.
gi 386647928 1776 FVQLEQLPLTANGKIDRKALP 1796
Cdd:cd05934   402 IRFVDDLPKTPTEKVAKAQLR 422
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
853-1264 3.06e-48

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 180.19  E-value: 3.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  853 YPLSSAQKrlYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGI--EMVGGEPMQRIYPEVEFAVE 930
Cdd:cd19542     2 YPCTPMQE--GMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLKSLDPPIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  931 HIRANEEEADAAVKQFIRAFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGeDLPALRIQYK 1010
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-QLLPPAPPFS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1011 DYAVWQQSEAQKEQLkrqeAYWLEVFRGELPVLEMPTDYARPAVQSyagnaLRFELDAQKRegLQRIASENGATLYMVLL 1090
Cdd:cd19542   159 DYISYLQSQSQEESL----QYWRKYLQGASPCAFPSLSPKRPAERS-----LSSTRRSLAK--LEAFCASLGVTLASLFQ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1091 AAYTILLQKYTGQEDVVIGTPIAGRT--HGDLHPLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLGAFERQDYPFEEL 1168
Cdd:cd19542   228 AAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1169 VDKLKLARDLsrnPLFDTMFTLQNTENKEFRLPGLQLTPYPVEEH-TSKFDLSLDIMESGDGFLCGIEYATALYKRETIE 1247
Cdd:cd19542   308 QRALGLWPSG---TLFNTLVSYQNFEASPESELSGSSVFELSAAEdPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAE 384
                         410
                  ....*....|....*..
gi 386647928 1248 RMAKHFEQLLTAIVNNP 1264
Cdd:cd19542   385 ELLEQFDDILEALLANP 401
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
3397-3710 3.30e-48

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 180.71  E-value: 3.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3397 IYALTPMQKGMWFHNTLNRHGGAYIEQTL--FNVRGALniELFSRSWNELAARHAVLRTNFHsgWRG--EPLQIVYRYkp 3472
Cdd:cd19544     1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLlaFDSRARL--DAFLAALQQVIDRHDILRTAIL--WEGlsEPVQVVWRQ-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3473 VEFAYEDLRHLAEAEWSAYLDQLVNDDKTRgFDLEQDALMRVKVVR-TQEESFHVLWSFHHILMDGWCLPLIAKELfdty 3551
Cdd:cd19544    75 AELPVEELTLDPGDDALAQLRARFDPRRYR-LDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI---- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3552 EAYLRNDLSERPAAPSYSHYIEW-LEKQDMEAAARYWTGFLAGYDsQTTLPQGKL--HNKDGEYTEANilRSLGKSLTER 3628
Cdd:cd19544   150 QAILAGRAAALPPPVPYRNFVAQaRLGASQAEHEAFFREMLGDVD-EPTAPFGLLdvQGDGSDITEAR--LALDAELAQR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3629 MSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEIAGIEEMIGLFINTIPVRVSCeAEQSFADVMKRVQ 3708
Cdd:cd19544   227 LRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRL-GGRSVREAVRQTH 305

                  ..
gi 386647928 3709 EA 3710
Cdd:cd19544   306 AR 307
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
8034-8441 5.16e-48

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 180.26  E-value: 5.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8034 YPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAVEY- 8112
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHi 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 ---SKADREEAVE--IAQRFVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLY----AGEEL 8183
Cdd:cd19533    82 dlsGDPDPEGAAQqwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8184 PP------LRIQYKDyAAWQRSEAYAKrvkqQEGYWLQTLAGELPVIELPTDYERTSTrsfegAELEFEAD--EALTQRL 8255
Cdd:cd19533   162 PPapfgsfLDLVEEE-QAYRQSERFER----DRAFWTEQFEDLPEPVSLARRAPGRSL-----AFLRRTAElpPELTRTL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8256 NELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETT 8335
Cdd:cd19533   232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8336 LGAFEHQDYPFEELVERLnvKRDASRNPVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTVAaqfDLTLSVAE--DDGAIR 8413
Cdd:cd19533   312 RSLLRHQRYRYEDLRRDL--GLTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTN---DLSIFVYDrdDESGLR 386
                         410       420
                  ....*....|....*....|....*...
gi 386647928 8414 GSFQYAAKLFKATMIRKMSKDLLAVLEQ 8441
Cdd:cd19533   387 IDFDANPALYSGEDLARHQERLLRLLEE 414
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
5959-6420 6.08e-48

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 180.71  E-value: 6.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5959 KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLV 6038
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6039 qghlldrasfadklvnlnddgayheDGSNlEPvngpehlTYVIYTSGTTGRPKGVMVEHRnvVRLVKNTNYvelnEQTHI 6118
Cdd:cd05971    85 -------------------------DGSD-DP-------ALIIYTSGTTGPPKGALHAHR--VLLGHLPGV----QFPFN 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6119 L--QTGAVVFDASTFEIWGALLNG-------GRLYVVRNETILDAVSLKNAIQQYGINTMWLTAP---LYNQLSQQDSGM 6186
Cdd:cd05971   126 LfpRDGDLYWTPADWAWIGGLLDVllpslyfGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTalkMMRQQGEQLKHA 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6187 FAGLKTLIVGGDVLSvphinRVL----REHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAvPIGKPINNSTAYIVDSKLS 6262
Cdd:cd05971   206 QVKLRAIATGGESLG-----EELlgwaREQFGVEVNEFYGQTECNLVIGNCSALFPIKPG-SMGKPIPGHRVAIVDDNGT 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6263 LLPVGVWGELIVG-GDGVA-RGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELG 6340
Cdd:cd05971   280 PLPPGEVGEIAVElPDPVAfLGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPA 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6341 EIEEQLLKVASVKEATVIVREDESGQKQLCAYFV-AERELTIGELRAALsQELPNYMIPSHFVPLE-----RMPLTPNGK 6414
Cdd:cd05971   353 EIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlNPGETPSDALAREI-QELVKTRLAAHEYPREiefvnELPRTATGK 431

                  ....*.
gi 386647928 6415 IDRRAL 6420
Cdd:cd05971   432 IRRREL 437
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
7461-7928 6.43e-48

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 180.56  E-value: 6.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7461 EKAAVVFENTQLTYRELNERANRLARTLRAEG-VQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYML 7539
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7540 EDSGAQVLLtqrhlqecvsfdgkviaaddeqaygedgsnlepvvgpnHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFA 7619
Cdd:cd05941    81 TDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7620 ETLRITEEDRVVQ--------------FASL----------SFDASCWEIFKA-----LFFGA-TLYIpakdTILDYPlf 7669
Cdd:cd05941   123 DAWRWTEDDVLLHvlplhhvhglvnalLCPLfagasveflpKFDPKEVAISRLmpsitVFMGVpTIYT----RLLQYY-- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7670 esymnengiTAAILPPTYAIYLSPDRLpslkKLITGGSAA-SVEFVQQWKDKV--RYFNAYGPTEASIVTSVwaaspdGL 7746
Cdd:cd05941   197 ---------EAHFTDPQFARAAAAERL----RLMVSGSAAlPVPTLEEWEAITghTLLERYGMTEIGMALSN------PL 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7747 DLRSVP--IGRPIANHQIFIVD-SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermYRTGDLARWL 7823
Cdd:cd05941   258 DGERRPgtVGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVD 331
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7824 PDGNIEYLGRI-DHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRE---LTVSELRGTLSQE 7899
Cdd:cd05941   332 EDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaaaLSLEELKEWAKQR 411
                         490       500
                  ....*....|....*....|....*....
gi 386647928 7900 LPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05941   412 LAPYKRPRRLILVDELPRNAMGKVNKKEL 440
PRK08316 PRK08316
acyl-CoA synthetase; Validated
3854-4332 1.01e-47

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 182.44  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3854 QTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIP 3933
Cdd:PRK08316   11 QTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3934 IDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVDD-------------------EQAYHADG-SNLEPVVGP 3993
Cdd:PRK08316   91 VNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTlilslvlggreapggwldfADWAEAGSvAEPDVELAD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3994 NHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQ----FASLSFDAscweifkalFFGATLYIPTST 4069
Cdd:PRK08316  171 DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHalplYHCAQLDV---------FLGPYLYVGATN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4070 TILDYP----LFEsYMNENGITATILPPT-YAAYLN-PD----RMPSLKKLITGGSAASVEFVQQWKDK---VLYFNAYG 4136
Cdd:PRK08316  242 VILDAPdpelILR-TIEAERITSFFAPPTvWISLLRhPDfdtrDLSSLRKGYYGASIMPVEVLKELRERlpgLRFYNCYG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4137 PTE-ASIVTSIW-DEAsdslgDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDN 4214
Cdd:PRK08316  321 QTEiAPLATVLGpEEH-----LRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4215 PFepgermyRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV--A 4292
Cdd:PRK08316  396 WF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVpkA 468
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 386647928 4293 QRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK08316  469 GATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
3847-4337 1.13e-47

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 182.27  E-value: 1.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3847 AAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMK 3926
Cdd:COG1021    18 EAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3927 AGGayIPID--PEYPEDRIRYMLEDSGAQALLTQRH------------LRERVSF---------AGTFVAVDDeqAYHAD 3983
Cdd:COG1021    98 AGA--IPVFalPAHRRAEISHFAEQSEAVAYIIPDRhrgfdyralareLQAEVPSlrhvlvvgdAGEFTSLDA--LLAAP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3984 GSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMfANTLQMTEQDrvVQFASL----SFDASCWEIFKALF 4058
Cdd:COG1021   174 ADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDyLYSVRAS-AEICGLDADT--VYLAALpaahNFPLSSPGVLGVLY 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4059 FGATLYIPTSTTILD-YPLFEsymnENGITATIL-PPTYAAYLN-PDR----MPSLKKLITGGS------AASVE----- 4120
Cdd:COG1021   251 AGGTVVLAPDPSPDTaFPLIE----RERVTVTALvPPLALLWLDaAERsrydLSSLRVLQVGGAklspelARRVRpalgc 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4121 FVQQWkdkvlyfnaYG-------------PTEAsIVTSIwdeasdslgdrksvpiGRPLANH-RIYVVDSHNRMLPVGVA 4186
Cdd:COG1021   327 TLQQV---------FGmaeglvnytrlddPEEV-ILTTQ----------------GRPISPDdEVRIVDEDGNPVPPGEV 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4187 GELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDHQVkIR-GYRIELGEVETQLAK 4265
Cdd:COG1021   381 GELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLA 453
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4266 IDAVQEAIVLAREDANGQQQLVAYFVAQ-RELTAAELRATM-SQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:COG1021   454 HPAVHDAAVVAMPDEYLGERSCAFVVPRgEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
5961-6415 1.31e-47

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 179.50  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQG 6040
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 hLLDRASFADKlvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKN-TNYVELNEQTHIL 6119
Cdd:cd05903    82 -RFRQFDPAAM----------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQyAERLGLGPGDVFL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6120 -------QTGAVvfdaSTFEIwgALLNGGRLYVVRNETILDAVSLknaIQQYGINTMWLTAPLYNQLSqqDSGMFAG--- 6189
Cdd:cd05903   139 vaspmahQTGFV----YGFTL--PLLLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLL--NAVEEAGepl 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6190 --LKTLIVGGDvlSVPhinRVLREHA----GLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSL 6263
Cdd:cd05903   208 srLRTFVCGGA--TVP---RSLARRAaellGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGAT 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6264 LPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDEqVKIR-GYRIELGEI 6342
Cdd:cd05903   283 LAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWF-------RTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEV 354
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 6343 EEQLLKVASVKEATVIVREDESGQKQLCAYFVAER--ELTIGELRAALS-QELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:cd05903   355 EDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSgaLLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
5950-6420 1.34e-47

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 179.79  E-value: 1.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5950 DHLAVTFEDKQLTYGELNERANRLARTL-RNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLvqghllDRASfadklvnlnddgayhedgsnlepvngpehltyVIYTSGTTGRPKGVMVEHRNV---VR-LV 6104
Cdd:cd05941    81 TDSEPSLVL------DPAL--------------------------------ILYTSGTTGRPKGVVLTHANLaanVRaLV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6105 KNTNYVELNEQTHILQTGAV--VFDASTfeiwGALLNGGRLYVVRNetilDAVSLKNAIQQYGINTMWLTAP-LYNQLSQ 6181
Cdd:cd05941   123 DAWRWTEDDVLLHVLPLHHVhgLVNALL----CPLFAGASVEFLPK----FDPKEVAISRLMPSITVFMGVPtIYTRLLQ 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6182 QDSGMF-----------AGLKTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTEnTTFSTTHTIVGEQKeAVPIGKPIN 6250
Cdd:cd05941   195 YYEAHFtdpqfaraaaaERLRLMVSGSAALPVPTLEE-WEAITGHTLLERYGMTE-IGMALSNPLDGERR-PGTVGMPLP 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6251 NSTAYIVD-SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGDLARWLPDGTLEYKGRI-DE 6328
Cdd:cd05941   272 GVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsVD 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6329 QVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQKqLCAYFVAERE---LTIGELRAALSQELPNYMIPSHFVPL 6404
Cdd:cd05941   346 IIKSGGYKVSALEIERVLLAHPGVSECAVIgVPDPDWGER-VVAVVVLRAGaaaLSLEELKEWAKQRLAPYKRPRRLILV 424
                         490
                  ....*....|....*.
gi 386647928 6405 ERMPLTPNGKIDRRAL 6420
Cdd:cd05941   425 DELPRNAMGKVNKKEL 440
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
2336-2828 1.41e-47

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 182.56  E-value: 1.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2336 ATAADYEADKTIHQLFEEQAERIPDHPAVV------FEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMV 2409
Cdd:PRK13295   15 SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2410 VGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQ------------RRLQER---------------VSFAGTV 2462
Cdd:PRK13295   95 VLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPktfrgfdhaamaRRLRPElpalrhvvvvggdgaDSFEALL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2463 VTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDrVVQFASLSfdascw 2542
Cdd:PRK13295  175 ITPAWEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADD-VILMASPM------ 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2543 eVFQTLF-FGATLYIPTKET-ILDYQW----FERYMSDNGIT-TATLPP-----TYAVYLNPDHMPDFKRLIAAGSASSL 2610
Cdd:PRK13295  248 -AHQTGFmYGLMMPVMLGATaVLQDIWdparAAELIRTEGVTfTMASTPfltdlTRAVKESGRPVSSLRTFLCAGAPIPG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2611 ELLQQWKD--KVKYFNAYGPTEDSICTTIwtpSTEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLA 2688
Cdd:PRK13295  327 ALVERARAalGAKIVSAWGMTENGAVTLT---KLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNF 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2689 RGYLNRPDLTAEKFvdnpfepgERMYRTGDLAKWLPDGTIEYLGRiDHQVKIRG-YRIELGEIEEQLLKVASVQEAIVIA 2767
Cdd:PRK13295  404 GGYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVA 474
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2768 HDDASGQKQLCAYFV--ADRTMTVGELRGEL-SGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK13295  475 YPDERLGERACAFVVprPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
3872-4337 2.39e-47

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 178.81  E-value: 2.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3872 AVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSG 3951
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3952 AQALLTqrhlrervsfagtfvavddeqayHADGsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMFANTL 4030
Cdd:cd05919    83 ARLVVT-----------------------SADD-----------IAYLLYSSGTTGPPKGVMHAHRDpLLFADAMAREAL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4031 QMTEQDRVVQFASLSFdasCWEIFKALFFGatLYIPTSTTILDYPLFESYMNENGIT--ATIL---PPTYAAYL-----N 4100
Cdd:cd05919   129 GLTPGDRVFSSAKMFF---GYGLGNSLWFP--LAVGASAVLNPGWPTAERVLATLARfrPTVLygvPTFYANLLdscagS 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4101 PDRMPSLKKLITGGSAASVEFVQQWKDKVLY--FNAYGPTEasiVTSIWdeASDSLGDRKSVPIGRPLANHRIYVVDSHN 4178
Cdd:cd05919   204 PDALRSLRLCVSAGEALPRGLGERWMEHFGGpiLDGIGATE---VGHIF--LSNRPGAWRLGSTGRPVPGYEIRLVDEEG 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4179 RMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGE 4258
Cdd:cd05919   279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4259 VETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELT-----AAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:cd05919   352 VESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApqeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431

                  ....
gi 386647928 4334 RKAL 4337
Cdd:cd05919   432 RFKL 435
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
2362-2828 2.99e-47

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 178.42  E-value: 2.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2362 PAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDS 2441
Cdd:cd05919     2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2442 SAQVllaqrrlqervsfagtVVTVDDeqayagdgsnlesavgpnDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA-NT 2520
Cdd:cd05919    82 EARL----------------VVTSAD------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMArEA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2521 LQINAQDRVVQFASLSFdasCWEVFQTLFF----GATLYI----PTKETILdyqwferymsdngITTATLPPT------- 2585
Cdd:cd05919   128 LGLTPGDRVFSSAKMFF---GYGLGNSLWFplavGASAVLnpgwPTAERVL-------------ATLARFRPTvlygvpt 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2586 -YAVYL-----NPDHMPDFKRLIAAGSASSLELLQQWKDkvkYFNayGPTEDSICTT----IWTPSTEDISQLKSVpiGG 2655
Cdd:cd05919   192 fYANLLdscagSPDALRSLRLCVSAGEALPRGLGERWME---HFG--GPILDGIGATevghIFLSNRPGAWRLGST--GR 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2656 PIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRID 2735
Cdd:cd05919   265 PVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRAD 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2736 HQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGE-----LSGELPGYMIPAHFV 2810
Cdd:cd05919   338 DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARdihrhLLERLSAHKVPRRIA 417
                         490
                  ....*....|....*...
gi 386647928 2811 QLERMPLTPNGKIDRKAL 2828
Cdd:cd05919   418 FVDELPRTATGKLQRFKL 435
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4910-5386 4.98e-47

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 177.48  E-value: 4.98e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4910 NDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL 4989
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4990 TqthlqeraqqwgqtlqaalclddeaayaedasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL 5069
Cdd:cd05934    81 V-----------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5070 DQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPkddRIDPARlhYW--ISEEKITIFEstpalIIPFMdyvaehgld 5147
Cdd:cd05934   120 GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP---RFSASR--FWsdVRRYGATVTN-----YLGAM--------- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5148 mssMVLLITSSDSCSVTDYRV---------------LQERFGsqFRIINAYGVTEAAIdsslydePLAKLPEAGNVP--I 5210
Cdd:cd05934   181 ---LSYLLAQPPSPDDRAHRLraaygapnppelheeFEERFG--VRLLEGYGMTETIV-------GVIGPRDEPRRPgsI 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5211 GKAALNAKFYIVDAHLNPVPVGVLGELCI---GGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDF 5287
Cdd:cd05934   249 GRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAMRNGWF-------HTGDLGYRDADGFFYF 321
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5288 IGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLS--ELRSSLSQELPGYMIPSY 5365
Cdd:cd05934   322 VDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDpeELFAFCEGQLAYFKVPRY 401
                         490       500
                  ....*....|....*....|.
gi 386647928 5366 FVQLEQLPLTANGKIDRKALP 5386
Cdd:cd05934   402 IRFVDDLPKTPTEKVAKAQLR 422
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
5949-6420 5.19e-47

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 179.87  E-value: 5.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVQGHLLDRASFA--------------------DKLVNLNDDGAYHEDGsnLEPVN-GPEHLTYVIYTSGTT 6087
Cdd:cd05959    98 EDSRARVVVVSGELAPVLAAAltksehtlvvlivsggagpeAGALLLAELVAAEAEQ--LKPAAtHADDPAFWLYSSGST 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6088 GRPKGVMVEHRNvVRLVKNT---NYVELNEQTHILQTGAVVF-----DASTFEIW-GA--LLNGGRlyvVRNETILDAVS 6156
Cdd:cd05959   176 GRPKGVVHLHAD-IYWTAELyarNVLGIREDDVCFSAAKLFFayglgNSLTFPLSvGAttVLMPER---PTPAAVFKRIR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6157 LKNAIQQYGINTMWlTAPLYNQLSQQDSgmFAGLKTLIVGGDVLSVpHINRVLREHAGLSIVNGYGPTEnttfsTTHTIV 6236
Cdd:cd05959   252 RYRPTVFFGVPTLY-AAMLAAPNLPSRD--LSSLRLCVSAGEALPA-EVGERWKARFGLDILDGIGSTE-----MLHIFL 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6237 GEQKEAV---PIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVessflpGErCYRTGDLAR 6313
Cdd:cd05959   323 SNRPGRVrygTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYV 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6314 WLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIG-----ELRAAL 6388
Cdd:cd05959   396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSealeeELKEFV 475
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 6389 SQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05959   476 KDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
5921-6420 6.04e-47

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 180.63  E-value: 6.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5921 QRVFNATEAKYPSDKTIHQLFEEQAERIPDHLAVT------FEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVER 5994
Cdd:PRK13295   10 PRRAASIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5995 SLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQGHL--LDRASFADKL----------VNLNDDGA-- 6060
Cdd:PRK13295   90 WWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFrgFDHAAMARRLrpelpalrhvVVVGGDGAds 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6061 --------YHEDGSNLEPV-----NGPEHLTYVIYTSGTTGRPKGVMVEHRNVVrlvknTNYVELNEQTHiLQTGAVVFD 6127
Cdd:PRK13295  170 feallitpAWEQEPDAPAIlarlrPGPDDVTQLIYTSGTTGEPKGVMHTANTLM-----ANIVPYAERLG-LGADDVILM 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6128 ASTFEIWGALLNGGRLYVVRNET-----ILDAVSLKNAIQQYGIN-TMWLTAPLYN-----QLSQQDSgmfAGLKTLIVG 6196
Cdd:PRK13295  244 ASPMAHQTGFMYGLMMPVMLGATavlqdIWDPARAAELIRTEGVTfTMASTPFLTDltravKESGRPV---SSLRTFLCA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6197 GDVLSVPHINRVlREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGG 6276
Cdd:PRK13295  321 GAPIPGALVERA-RAALGAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6277 DGVARGYLNRPELTAEKFvessflpgERCYRTGDLARWLPDGTLEYKGRiDEQVKIRG-YRIELGEIEEQLLKVASVKEA 6355
Cdd:PRK13295  400 CSNFGGYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQV 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 6356 TVIVREDESGQKQLCAYFV--AERELTIGELRAAL-SQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK13295  471 AIVAYPDERLGERACAFVVprPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5958-6421 6.43e-47

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 177.10  E-value: 6.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5958 DKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLL 6037
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6038 VQghlldrasfadklvnlnddgayhedgsnlepvngpehLTYVIYTSGTTGRPKGVMVEHRNVVRL-VKNTNYVELNEQ- 6115
Cdd:cd05934    81 VD-------------------------------------PASILYTSGTTGPPKGVVITHANLTFAgYYSARRFGLGEDd 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6116 THILQTGAVVFDASTFEIWGALLNGGRLyvvrneTILDAVSLKN---AIQQYGIN-TMWLTAPLYNQLSQQDSGMFAGLK 6191
Cdd:cd05934   124 VYLTVLPLFHINAQAVSVLAALSVGATL------VLLPRFSASRfwsDVRRYGATvTNYLGAMLSYLLAQPPSPDDRAHR 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6192 TLIVGGdVLSVPHINRVLREHAGLSIVNGYGPTEnttfsTTHTIVGEQKEAVP---IGKPINNSTAYIVDSKLSLLPVGV 6268
Cdd:cd05934   198 LRAAYG-APNPPELHEEFEERFGVRLLEGYGMTE-----TIVGVIGPRDEPRRpgsIGRPAPGYEVRIVDDDGQELPAGE 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6269 WGELIV---GGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQ 6345
Cdd:cd05934   272 PGELVIrglRGWGFFKGYYNMPEATAEAMRNGWF-------HTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERA 344
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 6346 LLKVASVKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALP 6421
Cdd:cd05934   345 ILRHPAVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
2354-2828 1.23e-46

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 178.23  E-value: 1.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2354 QAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDR 2433
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2434 ISYMLEDSSAQVLLAQRRLQERVsFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMvehhglcsl 2513
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKL-IPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI--------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2514 kQMFAN----------TLQINAQDR---VVQF---ASLSFdascweVFQTLFFGATLYIPTKetiLDYQWFERYMSDNGI 2577
Cdd:PRK03640  161 -QTYGNhwwsavgsalNLGLTEDDCwlaAVPIfhiSGLSI------LMRSVIYGMRVVLVEK---FDAEKINKLLQTGGV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2578 TTATLPPTY-----AVYLNPDHMPDFKRLIAAGSASSLELLQQWKDK-VKYFNAYGPTEdsICTTIWTPSTEDI-SQLKS 2650
Cdd:PRK03640  231 TIISVVSTMlqrllERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKgIPVYQSYGMTE--TASQIVTLSPEDAlTKLGS 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2651 VpiGGPIVNHRIYIVDaHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermyRTGDLAKWLPDGTIEY 2730
Cdd:PRK03640  309 A--GKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYV 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2731 LGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFV 2810
Cdd:PRK03640  379 LDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFY 458
                         490
                  ....*....|....*...
gi 386647928 2811 QLERMPLTPNGKIDRKAL 2828
Cdd:PRK03640  459 FVEELPRNASGKLLRHEL 476
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
4909-5380 1.46e-46

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 177.79  E-value: 1.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4909 ENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVL 4988
Cdd:cd05911     7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4989 LTQTHLQERAQQWGQTLQAA---LCLDDEAAYAEDA----SNVANVNEPH----------DLAYVIYTSGTTGRPKGVMI 5051
Cdd:cd05911    87 FTDPDGLEKVKEAAKELGPKdkiIVLDDKPDGVLSIedllSPTLGEEDEDlppplkdgkdDTAAILYSSGTTGLPKGVCL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5052 EHRSLV-NTAAGYRREYRLDQFPVRLLQLASFsFDVFvGDIA--RTLYNGGTMVICPKDdriDPARLHYWISEEKITIFE 5128
Cdd:cd05911   167 SHRNLIaNLSQVQTFLYGNDGSNDVILGFLPL-YHIY-GLFTtlASLLNGATVIIMPKF---DSELFLDLIEKYKITFLY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5129 STPALIIpFMdyvAEHGL----DMSSMVLLITSSDSCSvtdyRVLQERFGSQF---RIINAYGVTEAAIdsslydePLAK 5201
Cdd:cd05911   242 LVPPIAA-AL---AKSPLldkyDLSSLRVILSGGAPLS----KELQELLAKRFpnaTIKQGYGMTETGG-------ILTV 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5202 LPEAGNVP--IGKAALNAKFYIVDAHLNP-VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegERLYRTGDLAR 5278
Cdd:cd05911   307 NPDGDDKPgsVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIGY 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5279 WMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSElrsslsQELP 5358
Cdd:cd05911   381 FDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE------KEVK 454
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 5359 GYM---IPSY--------FVqlEQLPLTANGKI 5380
Cdd:cd05911   455 DYVakkVASYkqlrggvvFV--DEIPKSASGKI 485
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
7456-7928 3.19e-46

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 177.56  E-value: 3.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:cd05959    14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLLTQRHLQECVSFDGK--------VIAADDEQA------YGEDGSNLEPVVGP-----NHLAYVIYTSG 7596
Cdd:cd05959    94 AYYLEDSRARVVVVSGELAPVLAAALTksehtlvvLIVSGGAGPeagallLAELVAAEAEQLKPaathaDDPAFWLYSSG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7597 TTGKPKGVMVEHHGLCSLKLMFAE-TLRITEEDRVVQFASLSFdasCWEIFKALFF----GATLYI----PAKDTILDyp 7667
Cdd:cd05959   174 STGRPKGVVHLHADIYWTAELYARnVLGIREDDVCFSAAKLFF---AYGLGNSLTFplsvGATTVLmperPTPAAVFK-- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7668 lfesYMNENGITAAILPPT-YAIYLSPDRLP-----SLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEA-SIVTSv 7738
Cdd:cd05959   249 ----RIRRYRPTVFFGVPTlYAAMLAAPNLPsrdlsSLRLCVSAGEALPAEVGERWKARfgLDILDGIGSTEMlHIFLS- 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7739 waASPDglDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVdnpflaGErMYRTGD 7818
Cdd:cd05959   324 --NRPG--RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGD 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7819 LARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV-----ADRELTVSELR 7893
Cdd:cd05959   393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALEEELK 472
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 386647928 7894 GTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05959   473 EFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
PRK07798 PRK07798
acyl-CoA synthetase; Validated
3855-4333 5.26e-46

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 177.38  E-value: 5.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3855 TIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPI 3934
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3935 DPEYPEDRIRYMLEDSGAQALLTQRHLRERV-----SFAG--TFVAVDDE--QAYHADGSNLEPVV---GPNHLA----- 3997
Cdd:PRK07798   84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVaevlpRLPKlrTLVVVEDGsgNDLLPGAVDYEDALaagSPERDFgersp 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3998 ---YVIYTSGTTGKPKGVMVEHH-----GLCSLKLMFANTLqMTEQDRVVQFAS-----------LSFDASCWEIFKALF 4058
Cdd:PRK07798  164 ddlYLLYTGGTTGMPKGVMWRQEdifrvLLGGRDFATGEPI-EDEEELAKRAAAgpgmrrfpappLMHGAGQWAAFAALF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4059 FGATLYIPTSTTiLDYPLFESYMNENGITATIL------PPTYAAYLNPDR--MPSLKKLITGGSAASVEFVQQWKD--- 4127
Cdd:PRK07798  243 SGQTVVLLPDVR-FDADEVWRTIEREKVNVITIvgdamaRPLLDALEARGPydLSSLFAIASGGALFSPSVKEALLEllp 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4128 KVLYFNAYGPTEA----SIVTSiwdeasdslgdRKSVPIGRPL--ANHRIYVVDSHNRMLPVGvagelciSGVG--LAR- 4198
Cdd:PRK07798  322 NVVLTDSIGSSETgfggSGTVA-----------KGAVHTGGPRftIGPRTVVLDEDGNPVEPG-------SGEIgwIARr 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4199 -----GYLNRPELTAEKF--VDnpfepGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQE 4271
Cdd:PRK07798  384 ghiplGYYKDPEKTAETFptID-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAD 458
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 4272 AIVLAREDAN-GQQqlVAYFVAQRE---LTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:PRK07798  459 ALVVGVPDERwGQE--VVAVVQLREgarPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6992-7413 6.42e-46

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 174.43  E-value: 6.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSgPRGEPLQIVYRDKRIGFVYED 7071
Cdd:cd20484     4 LSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEE-EDGVPFQKIEPSKPLSFQEED 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7072 LSHLPADERQASVerleQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDR 7151
Cdd:cd20484    83 ISSLKESEIIAYL----REKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7152 PEQKAAPA-YSQYIEW----LENQDSAAASAYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAK 7226
Cdd:cd20484   159 PTLASSPAsYYDFVAWeqdmLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFAR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7227 QCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEipGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALES 7306
Cdd:cd20484   239 SQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7307 GRYDFYPlYEIQTQSAQKQELINHLLVFENYPMDEQVEQAGG------DDSGTLSITDVD-VAEHTNYNFTVTVFPG-DE 7378
Cdd:cd20484   317 LDHAAYP-FPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTSlqqflaEYQDVLSIEFVEgIHQEGEYELVLEVYEQeDR 395
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 386647928 7379 IVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd20484   396 FTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1288-1723 6.49e-46

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 177.46  E-value: 6.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1288 PAAPDAPENEVFHALfEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQ-GVKPNQLVGILADRSADLLVGALA 1366
Cdd:PRK08314    2 PKSLTLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1367 VWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQT--LQAVLC------LDDEAAYA---------- 1428
Cdd:PRK08314   81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNlrLRHVIVaqysdyLPAEPEIAvpawlraepp 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1429 ------------EDASNVANVNEPH-----DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLAS 1491
Cdd:PRK08314  161 lqalapggvvawKEALAAGLAPPPHtagpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1492 FSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLhywISEEKITIFESTPALIIPFMDYVAEHGLDMSSmeLLITSSDSC 1571
Cdd:PRK08314  241 FHVTGMVHSMNAPIYAGATVVLMPRWDREAAARL---IERYRVTHWTNIPTMVVDFLASPGLAERDLSS--LRYIGGGGA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1572 SVTDY--RVLQERFGSQFriINAYGVTE--AAIDSSLYDEPlaKLPEAGnVPigkaalnakFYIVDAH------LNPVPV 1641
Cdd:PRK08314  316 AMPEAvaERLKELTGLDY--VEGYGLTEtmAQTHSNPPDRP--KLQCLG-IP---------TFGVDARvidpetLEELPP 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1642 GVLGELCIGGIGVARGYLNRPELTEEKFVDspfVEGERLYRTGDLARWMPDGN---VDFIGRIDNQAkirGYRIETGEIE 1718
Cdd:PRK08314  382 GEVGEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYffiTDRLKRMINAS---GFKVWPAEVE 455

                  ....*
gi 386647928 1719 TQLLK 1723
Cdd:PRK08314  456 NLLYK 460
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
2360-2828 6.92e-46

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 174.79  E-value: 6.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2360 DHPAVVFEGQQLTYRELNERANRLARTLQALG-VKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLaqrrlqervsfagtvvtvddeqayagdgsnlesavgpnDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA 2518
Cdd:cd05941    81 TDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2519 NTLQINAQDRVVQ--------------FASLSFDASCweVFQTlFFGATLYIPTKEtildyqwferymsDNGITTATLPP 2584
Cdd:cd05941   123 DAWRWTEDDVLLHvlplhhvhglvnalLCPLFAGASV--EFLP-KFDPKEVAISRL-------------MPSITVFMGVP 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2585 TyaVY--------LNPDHMPDFK-------RLIAAGSAS-SLELLQQWKDKVKYF--NAYGPTEDSICTTiwTPstedis 2646
Cdd:cd05941   187 T--IYtrllqyyeAHFTDPQFARaaaaerlRLMVSGSAAlPVPTLEEWEAITGHTllERYGMTEIGMALS--NP------ 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2647 qLKSVPIGG------PIVNHRIyIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLA 2720
Cdd:cd05941   257 -LDGERRPGtvgmplPGVQARI-VDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLG 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2721 KWLPDGTIEYLGRI-DHQVKIRGYRIELGEIEEQLLKVASVQEAIVI-AHDDASGQKqLCAYFVAD---RTMTVGELRGE 2795
Cdd:cd05941   329 VVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIgVPDPDWGER-VVAVVVLRagaAALSLEELKEW 407
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 2796 LSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05941   408 AKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1308-1798 1.03e-45

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 176.33  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1308 ERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQ 1387
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1388 FMLEDSAASVLLT-QTHLQERAQQWGQ---TLQAVLCLDD---------EAAYAEDASNVAnVNEPHDLAYVIYTSGTTG 1454
Cdd:PRK06188  103 YVLEDAGISTLIVdPAPFVERALALLArvpSLKHVLTLGPvpdgvdllaAAAKFGPAPLVA-AALPPDIAGLAYTGGTTG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1455 RPKGVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSfDVFVGDIARTLYNGGTMVICPKddrIDPARLHYWISEEKI 1534
Cdd:PRK06188  182 KPKGVMGTHRSIATMAQIQLAEWEWPADP-RFLMCTPLS-HAGGAFFLPTLLRGGTVIVLAK---FDPAEVLRAIEEQRI 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1535 TIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQFriINAYGVTEAAIdsslydePLAKLPE 1614
Cdd:PRK06188  257 TATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIF--AQYYGQTEAPM-------VITYLRK 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1615 AGNVPI--------GKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDL 1686
Cdd:PRK06188  328 RDHDPDdpkrltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-------WLHTGDV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1687 ARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLS--ELRSSLS 1764
Cdd:PRK06188  401 AREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDaaELQAHVK 480
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 1765 QELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 1798
Cdd:PRK06188  481 ERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
3846-4337 1.50e-45

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 176.40  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3846 TAAEYQQEQTIHGLFEEQALRNPDAVAVV------FEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVV 3919
Cdd:PRK13295   16 IAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3920 GIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLR------------------ERV---------SFAGTFV 3972
Cdd:PRK13295   96 LYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaamarrlrpelpalRHVvvvggdgadSFEALLI 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3973 AVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDrVVQFAS-LSFDAScw 4051
Cdd:PRK13295  176 TPAWEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADD-VILMASpMAHQTG-- 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4052 eifkalfFGATLYIPT---STTIL----DYPLFESYMNENGITAT------ILPPTYAAYLNPDRMPSLKKLITGGSA-- 4116
Cdd:PRK13295  253 -------FMYGLMMPVmlgATAVLqdiwDPARAAELIRTEGVTFTmastpfLTDLTRAVKESGRPVSSLRTFLCAGAPip 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4117 -ASVEFVQQ-WKDKVLyfNAYGPTEASIVTSIWDEASDslgDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGV 4194
Cdd:PRK13295  326 gALVERARAaLGAKIV--SAWGMTENGAVTLTKLDDPD---ERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4195 GLARGYLNRPELTAEKFvdnpfepgERMYRTGDLVRWLPDGNLEYLGRiDHQVKIRG-YRIELGEVETQLAKIDAVQEAI 4273
Cdd:PRK13295  401 SNFGGYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVA 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 4274 VLAREDANGQQQLVAYFV--AQRELTAAELRATM-SQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK13295  472 IVAYPDERLGERACAFVVprPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
5960-6420 2.86e-45

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 172.66  E-value: 2.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5960 QLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVq 6039
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6040 ghlldrasfadklvnlnddgayhedGSNLEpvngpeHLTYVIYTSGTTGRPKGVMVEHR----NVVRLVKNTNYvelneq 6115
Cdd:cd05935    80 -------------------------GSELD------DLALIPYTSGTTGLPKGCMHTHFsaaaNALQSAVWTGL------ 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6116 thilqTGAVVFDAST--FEIWG------ALLNGGRLYVVRneTILDAVSLKNAIQQYGInTMWLTAP-----LYNQLSQQ 6182
Cdd:cd05935   123 -----TPSDVILACLplFHVTGfvgslnTAVYVGGTYVLM--ARWDRETALELIEKYKV-TFWTNIPtmlvdLLATPEFK 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6183 DSGmFAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTEntTFSTTHTIVGEQKEAVPIGKPINNSTAYIVD-SKL 6261
Cdd:cd05935   195 TRD-LSSLKVLTGGGAPMP-PAVAEKLLKLTGLRFVEGYGLTE--TMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6262 SLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVEssfLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGE 6341
Cdd:cd05935   271 RELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAE 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVIVREDESGQKQLCAYFVAEREL----TIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDR 6417
Cdd:cd05935   348 VEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgkvTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILW 427

                  ...
gi 386647928 6418 RAL 6420
Cdd:cd05935   428 RLL 430
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
5926-6358 4.73e-45

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 176.06  E-value: 4.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5926 ATEAKYPSDKTIHQLFEEQAERIPDHLAV-TFEDKQ---LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVG 6001
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALrEKEDGIwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6002 MIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQGH--------LLDRASFADKLVNLNDDGAYH----------- 6062
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQeqldklleVRDELPSLRHIVVLDPRGLRDdprllsldell 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6063 EDGSNLEPVN---------GPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTN-YVELNEQT---------HILQTGA 6123
Cdd:COG1022   162 ALGREVADPAelearraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLeRLPLGPGDrtlsflplaHVFERTV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6124 VVFdastfeiwgALLNGGRLYVVRN-ETILDavslknAIQQYGInTMWLTAP-----LYNQLSQQ--DSGMFAG------ 6189
Cdd:COG1022   242 SYY---------ALAAGATVAFAESpDTLAE------DLREVKP-TFMLAVPrvwekVYAGIQAKaeEAGGLKRklfrwa 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6190 -------------------------------------------LKTLIVGGDVLSvPHINRVLREhAGLSIVNGYGPTEN 6226
Cdd:COG1022   306 lavgrryararlagkspslllrlkhaladklvfsklrealggrLRFAVSGGAALG-PELARFFRA-LGIPVLEGYGLTET 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6227 TTFSTTHTiVGEQKeavP--IGKPINNSTAYIVDSklsllpvgvwGELIVGGDGVARGYLNRPELTAEKFVEssflpgER 6304
Cdd:COG1022   384 SPVITVNR-PGDNR---IgtVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA------DG 443
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6305 CYRTGDLARWLPDGTLEYKGRIDEQVKIR-GYRIELGEIEEQLLKVASVKEATVI 6358
Cdd:COG1022   444 WLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
5961-6420 5.27e-45

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 173.96  E-value: 5.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQG 6040
Cdd:cd05904    33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 HLLDR-ASFADKLVNLND---DGAYHEDGSNLEPVNGP-------EHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNY 6109
Cdd:cd05904   113 ELAEKlASLALPVVLLDSaefDSLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6110 VELNEQTHILQTGAVVfdaSTFEIWG-------ALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTMWLTAPLYNQLSQQ 6182
Cdd:cd05904   193 GEGSNSDSEDVFLCVL---PMFHIYGlssfalgLLRLGATVVVMPR---FDLEELLAAIERYKVTHLPVVPPIVLALVKS 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6183 DSGM---FAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHtiVGEQKEAVP---IGKPINNSTAYI 6256
Cdd:cd05904   267 PIVDkydLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC--FAPEKDRAKygsVGRLVPNVEAKI 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6257 VD-SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGY 6335
Cdd:cd05904   345 VDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWL------HTGDLCYIDEDGYLFIVDRLKELIKYKGF 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6336 RIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGElraalsQELPNYmIPSHFVPLER--------- 6406
Cdd:cd05904   419 QVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE------DEIMDF-VAKQVAPYKKvrkvafvda 491
                         490
                  ....*....|....
gi 386647928 6407 MPLTPNGKIDRRAL 6420
Cdd:cd05904   492 IPKSPSGKILRKEL 505
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
2337-2828 5.30e-45

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 173.28  E-value: 5.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2337 TAADYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVL 2416
Cdd:cd05920     7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2417 KAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQErvsfagtvvtvDDEQAYAgdgsnLESAVGPNDLAYIIYTSGT 2496
Cdd:cd05920    87 RLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAG-----------FDHRALA-----RELAESIPEVALFLLSGGT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2497 TGKPKGVMVEHHGLCSLKQMFANTLQINAQDR--VVQFASLSFDASCWEVFQTLFFGATLYI---PTKETILDyqwferY 2571
Cdd:cd05920   151 TGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVylAVLPAAHNFPLACPGVLGTLLAGGRVVLapdPSPDAAFP------L 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2572 MSDNGIT-TATLPPTYAVYLN----PDHMPDFKRLIAAGSAS-SLEL-----------LQQWkdkvkyfnaYGPTEDSIC 2634
Cdd:cd05920   225 IEREGVTvTALVPALVSLWLDaaasRRADLSSLRLLQVGGARlSPALarrvppvlgctLQQV---------FGMAEGLLN 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2635 TTIWTPSTEDI--SQlksvpiGGPIVNH-RIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepge 2711
Cdd:cd05920   296 YTRLDDPDEVIihTQ------GRPMSPDdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF---- 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2712 rmYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVA-DRTMTVG 2790
Cdd:cd05920   366 --YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLrDPPPSAA 443
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 386647928 2791 ELRGELSG-ELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05920   444 QLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
7470-7928 6.09e-45

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 173.97  E-value: 6.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7470 TQLTYRELNERANRLARTLRAEGVQADQPVGLMI---ERSLEMIvgaFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQV 7546
Cdd:cd12119    24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELY---YAVPGMGAVLHTINPRLFPEQIAYIINHAEDRV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7547 LLTQRHLQ--------ECVSFDGKVIAADDEQAYGEDGSNLE---------------PVVGPNHLAYVIYTSGTTGKPKG 7603
Cdd:cd12119   101 VFVDRDFLplleaiapRLPTVEHVVVMTDDAAMPEPAGVGVLayeellaaespeydwPDFDENTAAAICYTSGTTGNPKG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7604 VMVEHHG--LCSLKLMFAETLRITEEDRVVQFASLsFDASCWEI-FKALFFGATLYIPAKDtiLDYPLFESYMNENGITA 7680
Cdd:cd12119   181 VVYSHRSlvLHAMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLPGPY--LDPASLAELIEREGVTF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7681 AILPPTYAIYL------SPDRLPSLKKLITGGSAASVEFVQQWKDK-VRYFNAYGPTEAS------IVTSVWAASP--DG 7745
Cdd:cd12119   258 AAGVPTVWQGLldhleaNGRDLSSLRRVVIGGSAVPRSLIEAFEERgVRVIHAWGMTETSplgtvaRPPSEHSNLSedEQ 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7746 LDLRSVPiGRPIANHQIFIVDSQNHMLPV-GVA-GELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWL 7823
Cdd:cd12119   338 LALRAKQ-GRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RTGDVATID 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7824 PDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA--DRELTVSELRGTLSQELP 7901
Cdd:cd12119   410 EDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLkeGATVTAEELLEFLADKVA 489
                         490       500
                  ....*....|....*....|....*..
gi 386647928 7902 GYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd12119   490 KWWLPDDVVFVDEIPKTSTGKIDKKAL 516
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
3846-4337 8.00e-45

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 172.51  E-value: 8.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3846 TAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIM 3925
Cdd:cd05920     7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3926 KAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRErvsFAGTFVAVdDEQAYHADgsnlepvvgpnhLAYVIYTSGT 4005
Cdd:cd05920    87 RLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAG---FDHRALAR-ELAESIPE------------VALFLLSGGT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4006 TGKPKGVMVEHHGLCSLKLMFANTLQMTEQDR--VVQFASLSFDASCWEIFKALFFGATLYIPTSTTILD-YPLFEsymn 4082
Cdd:cd05920   151 TGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVylAVLPAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAaFPLIE---- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4083 ENGITATILPP------TYAAYLNPDRMPSLKKLITGGS------AASVEFV-----QQWkdkvlyfnaYGPTEASIVTS 4145
Cdd:cd05920   227 REGVTVTALVPalvslwLDAAASRRADLSSLRLLQVGGArlspalARRVPPVlgctlQQV---------FGMAEGLLNYT 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4146 IWDeasDSlGDRKSVPIGRPLANH-RIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYR 4224
Cdd:cd05920   298 RLD---DP-DEVIIHTQGRPMSPDdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YR 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4225 TGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVA-QRELTAAELRA 4303
Cdd:cd05920   368 TGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLrDPPPSAAQLRR 447
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 386647928 4304 TMSQ-ELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05920   448 FLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
4457-4851 9.95e-45

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 170.06  E-value: 9.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4457 QLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVdfavetVQAseQEAKAI-VRD 4535
Cdd:cd19537    16 QLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSP------PRV--QRVDTLdVWK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4536 FI-RPFDLAKPPLLRVglielAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGEELPGLRIQYKDYAVWQQSEAQkeq 4614
Cdd:cd19537    88 EInRPFDLEREDPIRV-----FISPDTLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWSRPASP--- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4615 lkRQEAYWLEAFRGeLPVLEMPtdyARPAVQSYAGDTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQE 4694
Cdd:cd19537   160 --EDLDFWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4695 DVIVGTPIAGRTHADLQSLIGMFVNTLAIR-NYP-AADKTFLSYLEDVKETTLGAFEHqTYPFEELVDKLQMARDLSRNP 4772
Cdd:cd19537   234 DIVLGAPYLNRTSEEDMETVGLFLEPLPIRiRFPsSSDASAADFLRAVRRSSQAALAH-AIPWHQLLEHLGLPPDSPNHP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4773 LFDTM--FSLQNTENKEMHLPGlhLTPYPTEYGMSKFDLsldMME----DSEGLECSLEFATALYKRETIERMAKHFEQL 4846
Cdd:cd19537   313 LFDVMvtFHDDRGVSLALPIPG--VEPLYTWAEGAKFPL---MFEftalSDDSLLLRLEYDTDCFSEEEIDRIESLILAA 387

                  ....*
gi 386647928 4847 LTAIV 4851
Cdd:cd19537   388 LELLV 392
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
8034-8446 1.05e-44

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 170.71  E-value: 1.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8034 YPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGF-EMANGEPVQRVYSDVEFAVEY 8112
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFiEDGLGQPVQVVHRQAQVPVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8113 ----SKADREEAVE--IAQRFVRPFDLRKPPLLRVGLI-EVEPERHILMLDMHHIISDGASVGILQEEFSRLYAG----- 8180
Cdd:cd19536    82 ldltPLEEQLDPLRayKEETKIRRFDLGRAPLVRAALVrKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQlleyk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8181 -EELPPlRIQYKDYAAWQRSEAYAkrvKQQEGYWLQTLAG-ELPVieLPTDYERTSTRSFEGAELEFEADEALTQRlnEL 8258
Cdd:cd19536   162 pLSLPP-AQPYRDFVAHERASIQQ---AASERYWREYLAGaTLAT--LPALSEAVGGGPEQDSELLVSVPLPVRSR--SL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8259 AARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTH--ADVEPIIGMFVNTLAIRnYPAGDKTFLSYLEEVKETTL 8336
Cdd:cd19536   234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLR-VTLSEETVEDLLKRAQEQEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8337 GAFEHQDYPFEelverlNVKRDASRNPVFDTMFVLQN-TEDRGIEA---DAFSLTPFVFDQTVaAQFDLTLSVAEDDGAI 8412
Cdd:cd19536   313 ESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHfDLDFGLPEwgsDEGMRRGLLFSEFK-SNYDVNLSVLPKQDRL 385
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 8413 RGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19536   386 ELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
5953-6420 1.14e-44

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 171.11  E-value: 1.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5953 AVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSG 6032
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6033 AKLLLVQGhlldrasfadklvnlnDDGAYhedgsnlepvngpehltyVIYTSGTTGRPKGVMVEHRNVVRLVK--NTNYV 6110
Cdd:cd05919    83 ARLVVTSA----------------DDIAY------------------LLYSSGTTGPPKGVMHAHRDPLLFADamAREAL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6111 ELNEQTHILQTGAVVFDAST-FEIWGALLNGGRLYVVRNETILDAVsLKNAIQQ-----YGINTMWLTAPLYNQLSQQDs 6184
Cdd:cd05919   129 GLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWPTAERV-LATLARFrptvlYGVPTFYANLLDSCAGSPDA- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6185 gmFAGLKTLIVGGDVLSVpHINRVLREHAGLSIVNGYGPTENTtfsttHTIVGEQKEAVPI---GKPINNSTAYIVDSKL 6261
Cdd:cd05919   207 --LRSLRLCVSAGEALPR-GLGERWMEHFGGPILDGIGATEVG-----HIFLSNRPGAWRLgstGRPVPGYEIRLVDEEG 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6262 SLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESsflpgerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGE 6341
Cdd:cd05919   279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGE-----LRAALSQELPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:cd05919   352 VESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslardIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431

                  ....
gi 386647928 6417 RRAL 6420
Cdd:cd05919   432 RFKL 435
PRK06178 PRK06178
acyl-CoA synthetase; Validated
3864-4337 2.02e-44

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 173.69  E-value: 2.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRI 3943
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 RYMLEDSGAQALLTQRHL-------RERVSFAGTFVA-----------------VDDEQAYHADGSNL------------ 3987
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLapvveqvRAETSLRHVIVTsladvlpaeptlplpdsLRAPRLAAAGAIDLlpalractapvp 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3988 EPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVqfasLSFDASCW---E----IFkALFFG 4060
Cdd:PRK06178  203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVF----LSFLPEFWiagEnfglLF-PLFSG 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4061 ATLYIPT---STTILDypLFESYmnenGITATILP----------PTYAAY----LNPDRMPS-LKKLitggsaaSVEFV 4122
Cdd:PRK06178  278 ATLVLLArwdAVAFMA--AVERY----RVTRTVMLvdnavelmdhPRFAEYdlssLRQVRVVSfVKKL-------NPDYR 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4123 QQWKD---KVLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPI--GRPLANHRIYVVD-SHNRMLPVGVAGELCISGVGL 4196
Cdd:PRK06178  345 QRWRAltgSVLAEAAWGMTETHTCDTFTAGFQDDDFDLLSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSL 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4197 ARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLA 4276
Cdd:PRK06178  425 LKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVG 497
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 4277 REDANGQQQLVAYFV--AQRELTAAELRATMSQELPNYMIPSYFVqLAQMPLTPNGKIDRKAL 4337
Cdd:PRK06178  498 RPDPDKGQVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
PRK06178 PRK06178
acyl-CoA synthetase; Validated
7456-7928 2.32e-44

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 173.30  E-value: 2.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLLTQRHLQECV-------------------------------SFDGKVIAADDEQAY-----GEDGSNL 7579
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAPVVeqvraetslrhvivtsladvlpaeptlplpdSLRAPRLAAAGAIDLlpalrACTAPVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7580 EPVVGPNHLAYVIYTSGTTGKPKGVMvEHHGlcSLKLMFAETLRIT---EEDRVVqfasLSFDASCW---E----IFkAL 7649
Cdd:PRK06178  203 LPPPALDALAALNYTGGTTGMPKGCE-HTQR--DMVYTAAAAYAVAvvgGEDSVF----LSFLPEFWiagEnfglLF-PL 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7650 FFGATLYIPAK-DTILDYPLFESYmnenGITAAILPPTYAIYL--SPD----RLPSLKKlitggsAASVEFV-------- 7714
Cdd:PRK06178  275 FSGATLVLLARwDAVAFMAAVERY----RVTRTVMLVDNAVELmdHPRfaeyDLSSLRQ------VRVVSFVkklnpdyr 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7715 QQWKD---KVRYFNAYGPTEASIVTSVWAASPDG-LDLRSVPI--GRPIANHQIFIVDSQNH-MLPVGVAGELCISGAGL 7787
Cdd:PRK06178  345 QRWRAltgSVLAEAAWGMTETHTCDTFTAGFQDDdFDLLSQPVfvGLPVPGTEFKICDFETGeLLPLGAEGEIVVRTPSL 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7788 ARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIA 7867
Cdd:PRK06178  425 LKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVG 497
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 7868 RGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPSYFVqLEQMPLTPNGKIDRNAL 7928
Cdd:PRK06178  498 RPDPDKGQVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
6992-7413 2.56e-44

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 169.87  E-value: 2.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPRGEPLQIVYRDKRIGFVYED 7071
Cdd:cd19539     4 LSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7072 LSHlPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDR 7151
Cdd:cd19539    84 LSD-PDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7152 PEQKAAPA-YSQYIEWLENQDS----AAASAYWSNYLAGYEgQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAK 7226
Cdd:cd19539   163 APLPELRQqYKEYAAWQREALAapraAELLDFWRRRLRGAE-PTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7227 QCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAeiPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEAALES 7306
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7307 GRYDFYPLYEIQTQSAQKQELINHLLV-----FENYP---MDEQVEQAGGDDSGTLSITDVDVaehtnyNFTVTVFPGDe 7378
Cdd:cd19539   320 QRHQELPFQQLVAELPVDRDAGRHPLVqivfqVTNAPageLELAGGLSYTEGSDIPDGAKFDL------NLTVTEEGTG- 392
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 386647928 7379 IVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19539   393 LRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
6992-7413 2.58e-44

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 169.91  E-value: 2.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPrGEPLQIVYRDKRIGFvyeD 7071
Cdd:cd19540     4 LSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDD-GGPYQVVLPAAEARP---D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7072 LSHLPADErqASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDR 7151
Cdd:cd19540    80 LTVVDVTE--DELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7152 PEQKAAPA-YSQYI----EWL---ENQDSAAAS--AYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERM 7221
Cdd:cd19540   158 PDWAPLPVqYADYAlwqrELLgdeDDPDSLAARqlAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7222 NRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEipGIEEMIGLFINTIPVRVACQPEESFADVMGRMQE 7301
Cdd:cd19540   238 AALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDE--ALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7302 AALESgrYD-----FYPLYEI--QTQSAQKQELINHLLVFENYPmDEQVEQAGgddsgtLSITDVDVAEHT---NYNFTV 7371
Cdd:cd19540   316 TDLAA--FAhqdvpFERLVEAlnPPRSTARHPLFQVMLAFQNTA-AATLELPG------LTVEPVPVDTGVakfDLSFTL 386
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 7372 TVFPGDE-----IVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19540   387 TERRDADgapagLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
5928-6420 2.67e-44

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 172.25  E-value: 2.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5928 EAKYPSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILK 6007
Cdd:COG1021    18 EAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6008 AGGayVPIDPdYPEDR---IRYMLEDSGAKLLLVQGH--LLDRASFADKLVNLND-----------------DGAYHEDG 6065
Cdd:COG1021    98 AGA--IPVFA-LPAHRraeISHFAEQSEAVAYIIPDRhrGFDYRALARELQAEVPslrhvlvvgdageftslDALLAAPA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6066 SNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHR----NVVRLVKntnYVELNEQTHILqtgAVV-----FDASTFEIWGA 6136
Cdd:COG1021   175 DLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVRASAE---ICGLDADTVYL---AALpaahnFPLSSPGVLGV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6137 LLNGGRLYVVRNETILDAVSLknaIQQYGIN---------TMWLTAPlynqlsQQDSGMFAGLKTLIVGGDVLSVPHINR 6207
Cdd:COG1021   249 LYAGGTVVLAPDPSPDTAFPL---IERERVTvtalvpplaLLWLDAA------ERSRYDLSSLRVLQVGGAKLSPELARR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6208 VlREHAGLSIVNGYGPTE---NTT--FSTTHTIVGEQkeavpiGKPInnSTA---YIVDSKLSLLPVGVWGELIVGGDGV 6279
Cdd:COG1021   320 V-RPALGCTLQQVFGMAEglvNYTrlDDPEEVILTTQ------GRPI--SPDdevRIVDEDGNPVPPGEVGELLTRGPYT 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6280 ARGYLNRPELTAEKFVESSFlpgercYRTGDLARWLPDGTLEYKGRIDEQVkIR-GYRIELGEIEEQLLKVASVKEATVI 6358
Cdd:COG1021   391 IRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVV 463
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6359 VREDES-GQKqLCAYFVA-ERELTIGELRAAL-SQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:COG1021   464 AMPDEYlGER-SCAFVVPrGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
4878-5313 2.78e-44

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 172.84  E-value: 2.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4878 PAAPDAPENEAFHALfEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQ-GVKPNQLVGILADRSADLLVGALA 4956
Cdd:PRK08314    2 PKSLTLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4957 VWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQT--LQAALC------LDDEAAYA---------- 5018
Cdd:PRK08314   81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNlrLRHVIVaqysdyLPAEPEIAvpawlraepp 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5019 ------------EDASNVANVNEPH-----DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLAS 5081
Cdd:PRK08314  161 lqalapggvvawKEALAAGLAPPPHtagpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5082 FSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLhywISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSC 5161
Cdd:PRK08314  241 FHVTGMVHSMNAPIYAGATVVLMPRWDREAAARL---IERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAM 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5162 SVTDYRVLQERFGSQFriINAYGVTE--AAIDSSLYDEPlaKLPEAGnVPigkaalnakFYIVDAH------LNPVPVGV 5233
Cdd:PRK08314  318 PEAVAERLKELTGLDY--VEGYGLTEtmAQTHSNPPDRP--KLQCLG-IP---------TFGVDARvidpetLEELPPGE 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5234 LGELCIGGIGVARGYLNRPELTEEKFVDspfVEGERLYRTGDLARWMPDGN---VDFIGRIDNQAkirGYRIETGEIETQ 5310
Cdd:PRK08314  384 VGEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYffiTDRLKRMINAS---GFKVWPAEVENL 457

                  ...
gi 386647928 5311 LLK 5313
Cdd:PRK08314  458 LYK 460
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
3879-4337 2.81e-44

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 172.04  E-value: 2.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3879 QLTYGELNERANRLARTLRDAGVRPDQLVGLMV---ERSLEMVVGIMAImkaGGAYIPIDPEYPEDRIRYMLEDSGAQAL 3955
Cdd:cd12119    25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGM---GAVLHTINPRLFPEQIAYIINHAEDRVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3956 LTQRHL-------RERVSFAGTFVAVDDEQAYHADGSNLE----------------PVVGPNHLAYVIYTSGTTGKPKGV 4012
Cdd:cd12119   102 FVDRDFlplleaiAPRLPTVEHVVVMTDDAAMPEPAGVGVlayeellaaespeydwPDFDENTAAAICYTSGTTGNPKGV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4013 MVEHHG--LCSLKLMFANTLQMTEQDRVVQFASLsFDASCWEI-FKALFFGATLYIPTSTtiLDYPLFESYMNENGITAT 4089
Cdd:cd12119   182 VYSHRSlvLHAMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLPGPY--LDPASLAELIEREGVTFA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4090 ILPPT----YAAYL--NPDRMPSLKKLITGGSAASVEFVQQWKDK-VLYFNAYGPTEAS-IVTSIW---DEASDSLGDRK 4158
Cdd:cd12119   259 AGVPTvwqgLLDHLeaNGRDLSSLRRVVIGGSAVPRSLIEAFEERgVRVIHAWGMTETSpLGTVARppsEHSNLSEDEQL 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4159 SVPI--GRPLANHRIYVVDSHNRMLPV-GVA-GELCISGVGLARGYLNRPELTAEKFVDNPFepgermyRTGDLVRWLPD 4234
Cdd:cd12119   339 ALRAkqGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RTGDVATIDED 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4235 GNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAyFVAQRE---LTAAELRATMSQELPN 4311
Cdd:cd12119   412 GYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLA-VVVLKEgatVTAEELLEFLADKVAK 490
                         490       500
                  ....*....|....*....|....*.
gi 386647928 4312 YMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd12119   491 WWLPDDVVFVDEIPKTSTGKIDKKAL 516
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
3399-3821 3.34e-44

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 169.48  E-value: 3.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3399 ALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGWRGEPLQIVyryKPVEFAYE 3478
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEI---LPPGPAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3479 DLRHL--AEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLR 3556
Cdd:cd19539    80 EVRDLsdPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3557 NDLSERPAAP-SYSHYIEW----LEKQDMEAAARYWTGFLAGYDS---QTTLPQGKLHNKDGEYTEAnilrSLGKSLTER 3628
Cdd:cd19539   160 GPAAPLPELRqQYKEYAAWqreaLAAPRAAELLDFWRRRLRGAEPtalPTDRPRPAGFPYPGADLRF----ELDAELVAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3629 MSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAeiAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQ 3708
Cdd:cd19539   236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3709 EAALESGGYDYYPLYEIQAQSAQKQDLITH-----IMAFENFPMDEQIEQAG-SYEDGKLAITDvdiaeqTNYDFTLVVM 3782
Cdd:cd19539   314 KALVDAQRHQELPFQQLVAELPVDRDAGRHplvqiVFQVTNAPAGELELAGGlSYTEGSDIPDG------AKFDLNLTVT 387
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 386647928 3783 P-GEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19539   388 EeGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
283-748 3.35e-44

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 169.01  E-value: 3.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  283 DRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLL 362
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  363 SQghlqervsfsgtwirlddeeayhedgsnlesvngpehLTYVIYTSGTTGKPKGNLTTHRNI-IRVVKNTNYIDVTGQD 441
Cdd:cd05934    81 VD-------------------------------------PASILYTSGTTGPPKGVVITHANLtFAGYYSARRFGLGEDD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  442 KLL-QLSSYSFDGSTFDIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVmfittafFNVLVDMnpdclrhARAILF 520
Cdd:cd05934   124 VYLtVLPLFHINAQAVSVLAALSVGATLVLLPR---FSASRFWSDVRRYGATV-------TNYLGAM-------LSYLLA 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  521 GGERVSVSH--VRKALGHLGPGKIKH------------VYGPTEsTVFATsydVHEVEEGAVSIPIGGPISNTAIYIVNA 586
Cdd:cd05934   187 QPPSPDDRAhrLRAAYGAPNPPELHEefeerfgvrlleGYGMTE-TIVGV---IGPRDEPRRPGSIGRPAPGYEVRIVDD 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  587 QNKLQPIGVAGELCV---AGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFR 663
Cdd:cd05934   263 DGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGEN 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  664 IELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVAD--RSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGK 741
Cdd:cd05934   336 ISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEK 415

                  ....*..
gi 386647928  742 VDRRALP 748
Cdd:cd05934   416 VAKAQLR 422
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4920-5385 5.80e-44

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 169.54  E-value: 5.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4920 ERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGA----YVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQ 4995
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4996 ER-AQQWGQTLQAALCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPv 5074
Cdd:cd05922    81 DRlRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5075 RLLQLASFSFDVFVGDIARTLYNGGTMVICPK----DDRIDPARLHywiseeKITIFESTPALI------------IPFM 5138
Cdd:cd05922   160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDgvldDAFWEDLREH------GATGLAGVPSTYamltrlgfdpakLPSL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5139 DYVAEHGLDMSSMVLlitssdscsvtdyrvlqERFGSQF---RIINAYGVTEAAIDSSLYD-EPLAKLPEAgnvpIGKAA 5214
Cdd:cd05922   234 RYLTQAGGRLPQETI-----------------ARLRELLpgaQVYVMYGQTEATRRMTYLPpERILEKPGS----IGLAI 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5215 LNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQ 5294
Cdd:cd05922   293 PGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRM 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5295 AKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKV-LCAhfTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLP 5373
Cdd:cd05922   367 IKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLaLFV--TAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELP 444
                         490
                  ....*....|..
gi 386647928 5374 LTANGKIDRKAL 5385
Cdd:cd05922   445 LTASGKVDYAAL 456
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
286-742 5.81e-44

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 169.10  E-value: 5.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSqg 365
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  366 hlqervsfSGTWIRLDDEEAyhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTHRNIIR-VVKNTNYIDVTGQDKLL 444
Cdd:cd05903    80 --------PERFRQFDPAAM-------------PDAVALLLFTSGTTGEPKGVMHSHNTLSAsIRQYAERLGLGPGDVFL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  445 QLSSYS-FDGSTFDIFGALLNGAKLVLvpkETVLDVAKLAGLIEKQQISVMFITTAFFNVL---VDMNPDCLRHARAILF 520
Cdd:cd05903   139 VASPMAhQTGFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMMGATPFLTDLlnaVEEAGEPLSRLRTFVC 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  521 GGERVSVSHVRKALGHLGpGKIKHVYGPTESTVFATSYDvhEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELC 600
Cdd:cd05903   216 GGATVPRSLARRAAELLG-AKVCSAYGSTECPGAVTSIT--PAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELL 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  601 VAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDqVKIR-GFRIELGEIEAHLLKLEAI 679
Cdd:cd05903   293 SRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLLGHPGV 364
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  680 EKATVVVRESANGEKQLCAYYV--ADRSLPANEVRSTLS-QELPAYMLPSYFVQLEQMPLTTNGKV 742
Cdd:cd05903   365 IEAAVVALPDERLGERACAVVVtkSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1330-1795 7.92e-44

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 169.16  E-value: 7.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1330 ERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGA----YVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQ 1405
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1406 ER-AQQWGQTLQAVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPv 1484
Cdd:cd05922    81 DRlRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1485 RLLQLASFSFDVFVGDIARTLYNGGTMVICPK----DDRIDPARLHywiseeKITIFESTPALI------------IPFM 1548
Cdd:cd05922   160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDgvldDAFWEDLREH------GATGLAGVPSTYamltrlgfdpakLPSL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1549 DYVAEHGLDMSSmellitssdscsvtdyrVLQERFGSQF---RIINAYGVTEAAIDSSLYD-EPLAKLPEAgnvpIGKAA 1624
Cdd:cd05922   234 RYLTQAGGRLPQ-----------------ETIARLRELLpgaQVYVMYGQTEATRRMTYLPpERILEKPGS----IGLAI 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1625 LNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQ 1704
Cdd:cd05922   293 PGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRM 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1705 AKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKV-LCAyfTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLP 1783
Cdd:cd05922   367 IKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLaLFV--TAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELP 444
                         490
                  ....*....|..
gi 386647928 1784 LTANGKIDRKAL 1795
Cdd:cd05922   445 LTASGKVDYAAL 456
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
854-1263 7.95e-44

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 167.36  E-value: 7.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  854 PLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEvefaveHIR 933
Cdd:cd19537     3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSS------PPR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  934 AnEEEADAAVKQFI-RAFDLAKPPLLRVglieLAPERHLLMFdMHHIVSDGISMDVLVEEFARLYGGEDLPALRIQYKDY 1012
Cdd:cd19537    77 V-QRVDTLDVWKEInRPFDLEREDPIRV----FISPDTLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1013 AVWQQSEAQkeqlkRQEAYWLEVFRGeLPVLEMPtdyARPAVQSYAGNALRFELDAQKREGLQRIASENGATLYMVLLAA 1092
Cdd:cd19537   151 TAWSRPASP-----EDLDFWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1093 YTILLQKYTGQEDVVIGTPIAGRTH-GDLHpLIGMFVNTLAIR-NYP-AADKTFLSYLEDVKETTLGAFERQdYPFEELV 1169
Cdd:cd19537   222 VALALQDLSDRTDIVLGAPYLNRTSeEDME-TVGLFLEPLPIRiRFPsSSDASAADFLRAVRRSSQAALAHA-IPWHQLL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1170 DKLKLARDLSRNPLFDTM--FTLQNTENKEFRLPGLQltpyPVEEHT--SKFDLSLDIME-SGDGFLCGIEYATALYKRE 1244
Cdd:cd19537   300 EHLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVE----PLYTWAegAKFPLMFEFTAlSDDSLLLRLEYDTDCFSEE 375
                         410
                  ....*....|....*....
gi 386647928 1245 TIERMAKHFEQLLTAIVNN 1263
Cdd:cd19537   376 EIDRIESLILAALELLVEG 394
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
5935-6420 8.76e-44

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 170.00  E-value: 8.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5935 KTIHQLFEEQAERIPDHLAVTFEDKQ--LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAY 6012
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6013 VPIDPDYPEDRIRYMLEDSGAKLLLVQ-GHLLDRASFAD-----KLVNLNDDGAYHEDGSNLE-PVNGPEHLTYVIYTSG 6085
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAVIAvDAQVMDAIFQSgvrvlALSDLVGLGEPESAGPLIEdPPREPEQPAFVFYTSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6086 TTGRPKGVMVEHRNV------------VRLVKNTNYVELNEQTHILQTGAVVFdastfeiwGALLNGGRLYVVRNETILD 6153
Cdd:cd05923   161 TTGLPKGAVIPQRAAesrvlfmstqagLRHGRHNVVLGLMPLYHVIGFFAVLV--------AALALDGTYVVVEEFDPAD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6154 AVSLknaIQQYGINTMWLTAPLYNQLSQqdSGMFAGLK-----TLIVGGDVLSVPHINRVlREHAGLSIVNGYGPTENTT 6228
Cdd:cd05923   233 ALKL---IEQERVTSLFATPTHLDALAA--AAEFAGLKlsslrHVTFAGATMPDAVLERV-NQHLPGEKVNIYGTTEAMN 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6229 FstthtIVGEQKEAVPIGKPINNSTAYIV---DSKLSLLPVGVWGELIV--GGDGVARGYLNRPELTAEKFVEssflpge 6303
Cdd:cd05923   307 S-----LYMRDARTGTEMRPGFFSEVRIVrigGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQD------- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6304 RCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERE-LTIG 6382
Cdd:cd05923   375 GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGtLSAD 454
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 386647928 6383 ELRA-ALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05923   455 ELDQfCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
5959-6420 8.83e-44

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 168.93  E-value: 8.83e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5959 KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLV 6038
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6039 QGhlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKN-TNYVELNEQ-- 6115
Cdd:cd05907    84 ED---------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALAlAERLPATEGdr 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6116 -------THILqtgavvfdASTFEIWGALLNGGRLYVVRN-ETILDavslknAIQQYGINTMwLTAP-----LYNQLSQQ 6182
Cdd:cd05907   131 hlsflplAHVF--------ERRAGLYVPLLAGARIYFASSaETLLD------DLSEVRPTVF-LAVPrvwekVYAAIKVK 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6183 DSG-----MFA-----GLKTLIVGGDVLSvPHINRVLReHAGLSIVNGYGPTENTTFSTTHTivGEQKEAVPIGKPINNS 6252
Cdd:cd05907   196 AVPglkrkLFDlavggRLRFAASGGAPLP-AELLHFFR-ALGIPVYEGYGLTETSAVVTLNP--PGDNRIGTVGKPLPGV 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6253 TAYIVDSklsllpvgvwGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRI-DEQVK 6331
Cdd:cd05907   272 EVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWL------HTGDLGEIDEDGFLHITGRKkDLIIT 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6332 IRGYRIELGEIEEQLLKVASVKEATV-----------IVREDES--------GQKQLCAYFVAERELTIGELRAALSQ-- 6390
Cdd:cd05907   336 SGGKNISPEPIENALKASPLISQAVVigdgrpflvalIVPDPEAleawaeehGIAYTDVAELAANPAVRAEIEAAVEAan 415
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 6391 -ELPNYMIPSHFVPLERMP------LTPNGKIDRRAL 6420
Cdd:cd05907   416 aRLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRPVI 452
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
2336-2779 1.03e-43

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 172.21  E-value: 1.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2336 ATAADYEADKTIHQLFEEQAERIPDHPAVVF----EGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVG 2411
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2412 MFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQ--------RRLQERVSFAGTVVTVDDEQAYAGD--------- 2474
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdqeqldklLEVRDELPSLRHIVVLDPRGLRDDPrllsldell 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2475 --GSNLES---------AVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLS--FdASC 2541
Cdd:COG1022   162 alGREVADpaelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAhvF-ERT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2542 WEVFQtLFFGATLYIPTK-ETILD--------------------------------------YQWF-------ERYMSDN 2575
Cdd:COG1022   241 VSYYA-LAAGATVAFAESpDTLAEdlrevkptfmlavprvwekvyagiqakaeeagglkrklFRWAlavgrryARARLAG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2576 GITTATLPPTYAVY----LNP--DHM-PDFKRLIAAGSASSLELLqqwkdkvKYFNA--------YGPTEDSICTTIWTP 2640
Cdd:COG1022   320 KSPSLLLRLKHALAdklvFSKlrEALgGRLRFAVSGGAALGPELA-------RFFRAlgipvlegYGLTETSPVITVNRP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2641 STEDISqlkSV--PIGGpiVNHRIyivdahyqpvpvGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGD 2718
Cdd:COG1022   393 GDNRIG---TVgpPLPG--VEVKI------------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGD 449
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 2719 LAKWLPDGTIEYLGRIDHQVKIR-GYRIELGEIEEQLLKVASVQEAIVIAHddasGQKQLCA 2779
Cdd:COG1022   450 IGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGD----GRPFLAA 507
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
5962-6420 1.15e-43

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 168.01  E-value: 1.15e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5962 TYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQGH 6041
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6042 LLDRASFADklvNLNDDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVrlvknTNYVELNEQTHILQT 6121
Cdd:TIGR01923   81 LEEKDFQAD---SLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHY-----ASAVGSKENLGFTED 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6122 GAVVFDASTFEI------WGALLNGGRLYVVrnetilDAVS-LKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAgLKTLI 6194
Cdd:TIGR01923  153 DNWLLSLPLYHIsglsilFRWLIEGATLRIV------DKFNqLLEMIANERVTHISLVPTQLNRLLDEGGHNEN-LRKIL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6195 VGGDVLSVPHINRVLREhaGLSIVNGYGPTENTTFSTTHTIVGEqKEAVPIGKPINNstayiVDSKLSLLPVGVWGELIV 6274
Cdd:TIGR01923  226 LGGSAIPAPLIEEAQQY--GLPIYLSYGMTETCSQVTTATPEML-HARPDVGRPLAG-----REIKIKVDNKEGHGEIMV 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6275 GGDGVARGYLNRPELTaekfvESSFLPGerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKE 6354
Cdd:TIGR01923  298 KGANLMKGYLYQGELT-----PAFEQQG--WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQE 370
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  6355 ATVIVRED-ESGQKQLcAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:TIGR01923  371 AVVVPKPDaEWGQVPV-AYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
5927-6420 1.90e-43

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 168.66  E-value: 1.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5927 TEAKYPSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAIL 6006
Cdd:cd05920     7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6007 KAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQG--HLLDRASFADKLVNLNDDGAYhedgsnlepvngpehltyVIYTS 6084
Cdd:cd05920    87 RLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDrhAGFDHRALARELAESIPEVAL------------------FLLSG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6085 GTTGRPKGVMVEHRNVVRLVKNTNYV-ELNEQTHILqtgAVVFDASTFE-----IWGALLNGGRLYVVRNETILDAVSLk 6158
Cdd:cd05920   149 GTTGTPKLIPRTHNDYAYNVRASAEVcGLDQDTVYL---AVLPAAHNFPlacpgVLGTLLAGGRVVLAPDPSPDAAFPL- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6159 naIQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTLI---VGGDVLSVPHINRVlREHAGLSIVNGYGPTEN----TTFST 6231
Cdd:cd05920   225 --IEREGVTVTALVPALVSLWLDAAASRRADLSSLRllqVGGARLSPALARRV-PPVLGCTLQQVFGMAEGllnyTRLDD 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6232 TH-TIVGEQkeavpiGKPIN-NSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTG 6309
Cdd:cd05920   302 PDeVIIHTQ------GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6310 DLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVA-ERELTIGELRAAL 6388
Cdd:cd05920   370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLrDPPPSAAQLRRFL 449
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 6389 SQ-ELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05920   450 RErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1902-2309 1.97e-43

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 166.21  E-value: 1.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1902 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEP----------VQRV-- 1969
Cdd:cd19537     3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLrrsyssspprVQRVdt 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1970 ---YKEVNfavehyrtseaeagevvrgfvRTFDLAKPPLLRVglvELAEDlhILLLDMHHIVSDGMSTDVLTEEFGRLYN 2046
Cdd:cd19537    83 ldvWKEIN---------------------RPFDLEREDPIRV---FISPD--TLLVVMSHIICDLTTLQLLLREVSAAYN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2047 GESLATLRIQYKDYAVWQQ--SEEQLErvkrqeaYWLDMFRGeLPVLEMPtdyPRPAVRRFEGSTLSFRLDAGLNEALKR 2124
Cdd:cd19537   137 GKLLPPVRREYLDSTAWSRpaSPEDLD-------FWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQ 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2125 VAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHGDLQPLIGMFVNTLAIR-NYP-AGGKTFRSFLEEVKETT 2202
Cdd:cd19537   206 FSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRiRFPsSSDASAADFLRAVRRSS 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2203 LGAYEHqTYPFEELVEKLQVPRDLSRNPIFDAM--FVLQNTENEELQLDGLK-LAPYPSGntiARFDLTLDVTETGSG-L 2278
Cdd:cd19537   286 QAALAH-AIPWHQLLEHLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVEpLYTWAEG---AKFPLMFEFTALSDDsL 361
                         410       420       430
                  ....*....|....*....|....*....|.
gi 386647928 2279 ECNLEYATSLYARETIARMAKHLEQLLTAIA 2309
Cdd:cd19537   362 LLRLEYDTDCFSEEEIDRIESLILAALELLV 392
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
7442-7928 2.18e-43

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 169.93  E-value: 2.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7442 YAREQTIHGLFEEQAERMPEKAAVVFEN-TQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAG 7520
Cdd:PRK06087   19 YWGDASLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7521 GAYVPIDPEYPEDRIRYMLEDSGAQVLLTQ-------------------RHLQECVSFDgKVIAADDEQAYGEDGSNLEP 7581
Cdd:PRK06087   99 AVSVPLLPSWREAELVWVLNKCQAKMFFAPtlfkqtrpvdlilplqnqlPQLQQIVGVD-KLAPATSSLSLSQIIADYEP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7582 VVGP-----NHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDAscweifkALFFG--AT 7654
Cdd:PRK06087  178 LTTAitthgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHAT-------GFLHGvtAP 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7655 LYIPAKDTILDypLFES-----YMNENGITAAiLPPTYAIY-------LSPDRLPSLKKLITGGSAASVEFVQQ-WKDKV 7721
Cdd:PRK06087  251 FLIGARSVLLD--IFTPdaclaLLEQQRCTCM-LGATPFIYdllnlleKQPADLSALRFFLCGGTTIPKKVAREcQQRGI 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7722 RYFNAYGPTEASIVTSVWAASPdgLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAeK 7801
Cdd:PRK06087  328 KLLSVYGSTESSPHAVVNLDDP--LSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-R 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7802 FVDNpflagERMYRTGDLARWLPDGNIEYLGRiDHQVKIR-GYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAY 7880
Cdd:PRK06087  405 ALDE-----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAY 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7881 FV---ADRELTVSELRGTLS-QELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK06087  479 VVlkaPHHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
8035-8445 2.67e-43

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 165.82  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8035 PVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVqRVYSDvefavEYSK 8114
Cdd:cd19537     3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLR-RSYSS-----SPPR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8115 ADREEAVEIAQRFVRPFDLRKPPLLRVglievEPERHILMLDMHHIISDGASVGILQEEFSRLYAGEELPPLRIQYKDYA 8194
Cdd:cd19537    77 VQRVDTLDVWKEINRPFDLEREDPIRV-----FISPDTLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDST 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8195 AWQR--SEAYAKrvkqqegYWLQTLAGeLPVIELPTdyeRTSTRSFEGAELEFEADEALTQRLNELAARHESTLYMVLLS 8272
Cdd:cd19537   152 AWSRpaSPEDLD-------FWSEYLSG-LPLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALA 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8273 AYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIR-NYP-AGDKTFLSYLEEVKETTLGAFEHQdYPFEELV 8350
Cdd:cd19537   221 AVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRiRFPsSSDASAADFLRAVRRSSQAALAHA-IPWHQLL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8351 ERLNVKRDASRNPVFDTM--FvlqntEDRGIEADAFSLtPFVFDQTVAAQ-------FDLTlsvAEDDGAIRGSFQYAAK 8421
Cdd:cd19537   300 EHLGLPPDSPNHPLFDVMvtF-----HDDRGVSLALPI-PGVEPLYTWAEgakfplmFEFT---ALSDDSLLLRLEYDTD 370
                         410       420
                  ....*....|....*....|....
gi 386647928 8422 LFKATMIRKMSKDLLAVLEQICGN 8445
Cdd:cd19537   371 CFSEEEIDRIESLILAALELLVEG 394
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
7444-7925 3.18e-43

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 169.95  E-value: 3.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7444 REQTIHGLFEEQAERMPEKAAVVFENTQL--TYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGG 7521
Cdd:PRK12583   16 LTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7522 AYVPIDPEYPEDRIRYMLEDSGAQVLLT-----------------------QR---------HLQECVSFDGK----VIA 7565
Cdd:PRK12583   96 ILVNINPAYRASELEYALGQSGVRWVICadafktsdyhamlqellpglaegQPgalacerlpELRGVVSLAPApppgFLA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7566 ADDEQAYGE--DGSNLEPVVGPNHLAYVI---YTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQ-------F 7633
Cdd:PRK12583  176 WHELQARGEtvSREALAERQASLDRDDPIniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVpvplyhcF 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7634 ASLSFDASCweifkaLFFGATLYIPAKDtiLDYPLFESYMNENGITAAILPPTYAI--YLSPDR----LPSLKKLITGGS 7707
Cdd:PRK12583  256 GMVLANLGC------MTVGACLVYPNEA--FDPLATLQAVEEERCTALYGVPTMFIaeLDHPQRgnfdLSSLRTGIMAGA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7708 AASVEFVQQWKDKVRYFN---AYGPTEASIVTSVWAASpDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISG 7784
Cdd:PRK12583  328 PCPIEVMRRVMDEMHMAEvqiAYGMTETSPVSLQTTAA-DDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRG 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7785 AGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETI 7864
Cdd:PRK12583  407 YSVMKGYWNNPEATAESIDEDGWM------HTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQ 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 7865 VIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:PRK12583  481 VFGVPDEKYGEEIVAWVRlhPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
256-747 4.68e-43

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 167.50  E-value: 4.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  256 YPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGG 335
Cdd:cd05920    11 YWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  336 AYVPIDPEYPEERIRYMLEDSGTQVLLsqghlqervsFSGTWIRLDDEEAYHEDgsnLESVNGPehlTYVIYTSGTTGKP 415
Cdd:cd05920    91 VPVLALPSHRRSELSAFCAHAEAVAYI----------VPDRHAGFDHRALAREL---AESIPEV---ALFLLSGGTTGTP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  416 KGNLTTHRNIIRVVKNTNYIDVTGQDK--LLQLS-SYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLaglIEKQQIS 492
Cdd:cd05920   155 KLIPRTHNDYAYNVRASAEVCGLDQDTvyLAVLPaAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPL---IEREGVT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  493 VMFITTAFFNVLVD---MNPDCLRHARAILFGGERVSVSHVRKALGHLGPgKIKHVYGPTESTVFATSY-DVHEVEEGAV 568
Cdd:cd05920   232 VTALVPALVSLWLDaaaSRRADLSSLRLLQVGGARLSPALARRVPPVLGC-TLQQVFGMAEGLLNYTRLdDPDEVIIHTQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  569 sipiGGPIS-NTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTI 647
Cdd:cd05920   311 ----GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYL 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  648 EYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKqLCAYYVA-DRSLPANEVRSTLSQ-ELPAYML 724
Cdd:cd05920   381 VVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVaMPDELLGER-SCAFVVLrDPPPSAAQLRRFLRErGLAAYKL 459
                         490       500
                  ....*....|....*....|...
gi 386647928  725 PSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05920   460 PDRIEFVDSLPLTAVGKIDKKAL 482
PRK07798 PRK07798
acyl-CoA synthetase; Validated
4889-5381 4.71e-43

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 168.52  E-value: 4.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4889 FHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 4968
Cdd:PRK07798    5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4969 PDYPSDRIQFMLEDSAASVLLTQTHLQER-AQQWGQT--LQAALCLDDEAAYA--------EDAsnVANVNEPHDLA--- 5034
Cdd:PRK07798   85 YRYVEDELRYLLDDSDAVALVYEREFAPRvAEVLPRLpkLRTLVVVEDGSGNDllpgavdyEDA--LAAGSPERDFGers 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5035 ----YVIYTSGTTGRPKGVMIEH----RSLVNTAAGYRREYRLD---------------QFPVRLL-----QLASFSfdv 5086
Cdd:PRK07798  163 pddlYLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDeeelakraaagpgmrRFPAPPLmhgagQWAAFA--- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5087 fvgdiarTLYNGGTMVICPkDDRIDPARLHYWISEEKIT-IFESTPALIIPFMD-YVAEHGLDMSSMVLLITSSDSCSVT 5164
Cdd:PRK07798  240 -------ALFSGQTVVLLP-DVRFDADEVWRTIEREKVNvITIVGDAMARPLLDaLEARGPYDLSSLFAIASGGALFSPS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5165 DYRVLQERFgSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALnakfyIVDAHLNPVPVGvlgelcIGGIG- 5243
Cdd:PRK07798  312 VKEALLELL-PNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTV-----VLDEDGNPVEPG------SGEIGw 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5244 VAR------GYLNRPELTEEKFvdsPFVEGERLYRTGDLARWMPDGNVDFIGRiDNQAkirgyrIETG-------EIEtQ 5310
Cdd:PRK07798  380 IARrghiplGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR-GSVC------INTGgekvfpeEVE-E 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5311 LLKAEGvreavvvVREDAK---------GQKVlCA--HFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGK 5379
Cdd:PRK07798  449 ALKAHP-------DVADALvvgvpderwGQEV-VAvvQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520

                  ..
gi 386647928 5380 ID 5381
Cdd:PRK07798  521 AD 522
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1304-1795 4.76e-43

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 167.73  E-value: 4.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1304 EKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQ-GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 1382
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLEDSAASVLLTQTHLQERAQ--QWGQTLQAVLCLDDEAAyAEDASNVANVNEPHDLAYVI-YTSGTTGRPKGV 1459
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTFQNMALsmQKVSYVQRVISITSLKE-IEDRKIDNFVEKNESASFIIcYTSGTTGKPKGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 MIEH-----RSLVNTAAgyrREYRLDQFPVRLLQLasfsfdVFVGDIA----RTLYNGGTMVIcpkDDRIDPARLHYWIS 1530
Cdd:PRK06839  168 VLTQenmfwNALNNTFA---IDLTMHDRSIVLLPL------FHIGGIGlfafPTLFAGGVIIV---PRKFEPTKALSMIE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1531 EEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERfgsQFRIINAYGVTEAAIDSSLYDEPLA 1610
Cdd:PRK06839  236 KHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR---GFLFGQGFGMTETSPTVFMLSEEDA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1611 KlPEAGNvpIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWM 1690
Cdd:PRK06839  313 R-RKVGS--IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVD 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1691 PDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSE--LRSSLSQELP 1768
Cdd:PRK06839  383 EDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEkdVIEHCRLFLA 462
                         490       500
                  ....*....|....*....|....*..
gi 386647928 1769 GYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK06839  463 KYKIPKEIVFLKELPKNATGKIQKAQL 489
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
5961-6420 5.24e-43

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 165.97  E-value: 5.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVqg 6040
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 hlldrasfadklvNLNDdgayhedgsnlepvngpehLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVelneqtHILQ 6120
Cdd:cd05972    79 -------------DAED-------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYW------LGLR 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6121 TGAVVFDAS----TFEIWGAL---LNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQD--SGMFAGLK 6191
Cdd:cd05972   121 PDDIHWNIAdpgwAKGAWSSFfgpWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDlsSYKFSHLR 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6192 TLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTENT-TFSTTHTIvgeqkEAVP--IGKPINNSTAYIVDSKLSLLPVGV 6268
Cdd:cd05972   201 LVVSAGEPLN-PEVIEWWRAATGLPIRDGYGQTETGlTVGNFPDM-----PVKPgsMGRPTPGYDVAIIDDDGRELPPGE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6269 WGELIV--GGDGVARGYLNRPELTAEKFVESSflpgercYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQL 6346
Cdd:cd05972   275 EGDIAIklPPPGLFLGYVGDPEKTEASIRGDY-------YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6347 LKVASVKEATVIVREDESGQKQLCAYFVaereLTIGELRA-ALSQELPN--------YMIPS--HFVPleRMPLTPNGKI 6415
Cdd:cd05972   348 LEHPAVAEAAVVGSPDPVRGEVVKAFVV----LTSGYEPSeELAEELQGhvkkvlapYKYPReiEFVE--ELPKTISGKI 421

                  ....*
gi 386647928 6416 DRRAL 6420
Cdd:cd05972   422 RRVEL 426
PRK07798 PRK07798
acyl-CoA synthetase; Validated
7447-7924 5.47e-43

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 168.52  E-value: 5.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7447 TIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPI 7526
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7527 DPEYPEDRIRYMLEDSGAQVLLTQRhlqecvSFDGKV---------------IAADDEQAYGEDGSNLEPVV---GPNHL 7588
Cdd:PRK07798   84 NYRYVEDELRYLLDDSDAVALVYER------EFAPRVaevlprlpklrtlvvVEDGSGNDLLPGAVDYEDALaagSPERD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7589 A--------YVIYTSGTTGKPKGVMVEHH-----GLCSLKLMFAETLRiTEEDRVVQFAS-----------LSFDASCWE 7644
Cdd:PRK07798  158 FgerspddlYLLYTGGTTGMPKGVMWRQEdifrvLLGGRDFATGEPIE-DEEELAKRAAAgpgmrrfpappLMHGAGQWA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7645 IFKALFFGATLyipakdTILDYPLFE-----SYMNENGITA------AILPPTYAIYLSPDR--LPSLKKLITGGSAASV 7711
Cdd:PRK07798  237 AFAALFSGQTV------VLLPDVRFDadevwRTIEREKVNVitivgdAMARPLLDALEARGPydLSSLFAIASGGALFSP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7712 EFVQQWKD---KVRYFNAYGPTEASIVTSVWAASpdgldlRSVPIGRPI--ANHQIFIVDSQNHMLPVGvagelciSGAG 7786
Cdd:PRK07798  311 SVKEALLEllpNVVLTDSIGSSETGFGGSGTVAK------GAVHTGGPRftIGPRTVVLDEDGNPVEPG-------SGEI 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7787 --LAR------GYLNRPELTAEKFvdnPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIA 7858
Cdd:PRK07798  378 gwIARrghiplGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHP 454
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 7859 SVQETIVIARGDANGQQQLCAyFVADRE---LTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKID 7924
Cdd:PRK07798  455 DVADALVVGVPDERWGQEVVA-VVQLREgarPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
7438-7928 5.86e-43

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 167.12  E-value: 5.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7438 TAAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIM 7517
Cdd:cd05920     7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7518 KAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQEcvsFDGKVIAADDEQAYGEdgsnlepvvgpnhLAYVIYTSGT 7597
Cdd:cd05920    87 RLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAG---FDHRALARELAESIPE-------------VALFLLSGGT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7598 TGKPKGVMVEHHGLCSLKLMFAETLRITEEDR--VVQFASLSFDASCWEIFKALFFGATLYI---PAKDTILdyPLFEsy 7672
Cdd:cd05920   151 TGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVylAVLPAAHNFPLACPGVLGTLLAGGRVVLapdPSPDAAF--PLIE-- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 mnENGITA-AILPPTYAIYL-----SPDRLPSLKKLITGGS------AASVEFV-----QQWkdkvryfnaYGPTEAsIV 7735
Cdd:cd05920   227 --REGVTVtALVPALVSLWLdaaasRRADLSSLRLLQVGGArlspalARRVPPVlgctlQQV---------FGMAEG-LL 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7736 TSVWAASPDGLDLRSVpiGRPIANH-QIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermY 7814
Cdd:cd05920   295 NYTRLDDPDEVIIHTQ--GRPMSPDdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------Y 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7815 RTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA-DRELTVSELR 7893
Cdd:cd05920   367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLrDPPPSAAQLR 446
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 7894 GTLSQ-ELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05920   447 RFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
7469-7928 7.29e-43

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 167.10  E-value: 7.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7469 NTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLL 7548
Cdd:cd05926    12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7549 TQRH---------------LQECVSFDGKVIAADD--EQAYGEDG---SNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEH 7608
Cdd:cd05926    92 TPKGelgpasraasklglaILELALDVGVLIRAPSaeSLSNLLADkknAKSEGVPLPDDLALILHTSGTTGRPKGVPLTH 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7609 HGLCSLKLMFAETLRITEEDRVV----------QFASL--------------SFDASC-WEIFKAlfFGATLY--IPakd 7661
Cdd:cd05926   172 RNLAASATNITNTYKLTPDDRTLvvmplfhvhgLVASLlstlaaggsvvlppRFSASTfWPDVRD--YNATWYtaVP--- 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7662 TILDYPLfesyMNENGITAAILPPTYAIY-----LSPDRLPSLKKLItggsAASVefvqqwkdkvryFNAYGPTEAS-IV 7735
Cdd:cd05926   247 TIHQILL----NRPEPNPESPPPKLRFIRscsasLPPAVLEALEATF----GAPV------------LEAYGMTEAAhQM 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7736 TSvwaaSPdgldLRSVP-----IGRPIANhQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLag 7810
Cdd:cd05926   307 TS----NP----LPPGPrkpgsVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWF-- 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7811 ermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELT 7888
Cdd:cd05926   376 ----RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlrEGASVT 451
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 386647928 7889 VSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05926   452 EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
4443-4854 7.46e-43

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 165.31  E-value: 7.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4443 YPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELID-GEPVQRIYPEVDFAVET 4521
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4522 VQ---ASEQEAKA---IVRDFIRPFDLAKPPLLRVGLIELAP-ERCILMLDMHHIVSDGVSADVLVEEFARLYSG----- 4589
Cdd:cd19536    82 LDltpLEEQLDPLrayKEETKIRRFDLGRAPLVRAALVRKDErERFLLVISDHHSILDGWSLYLLVKEILAVYNQlleyk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4590 -EELPGlRIQYKDYAVWQQSEAQKEQLkrqEAYWLEAFRG-ELPVLEMPTDyarpAVQSYAGDTLDFRMNSEISEGLKRI 4667
Cdd:cd19536   162 pLSLPP-AQPYRDFVAHERASIQQAAS---ERYWREYLAGaTLATLPALSE----AVGGGPEQDSELLVSVPLPVRSRSL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4668 AAESGATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTH--ADLQSLIGMFVNTLAIRnYPAADKTFLSYLEDVKETTL 4745
Cdd:cd19536   234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLR-VTLSEETVEDLLKRAQEQEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4746 GAFEHQTYPFEELvdklqmARDLSRNPLFDTMFSLQN-------TENKEMHLPGLHLTPYPTeygmsKFDLSLDMMEDSE 4818
Cdd:cd19536   313 ESLSHEQVPLADI------QRCSEGEPLFDSIVNFRHfdldfglPEWGSDEGMRRGLLFSEF-----KSNYDVNLSVLPK 381
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 386647928 4819 G--LECSLEFATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19536   382 QdrLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1307-1790 7.50e-43

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 167.80  E-value: 7.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 1386
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QFMLEDSAASVLLTQTHLQERAQ---------------QWGQTLQAVLCLDDEAAYAEDASNVANVnEPH--DLAYVIYT 1449
Cdd:PRK08316  101 AYILDHSGARAFLVDPALAPTAEaalallpvdtlilslVLGGREAPGGWLDFADWAEAGSVAEPDV-ELAddDLAQILYT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1450 SGTTGRPKGVMIEHRSLVN-----TAAGyrrEYRLDQFPVRLLQL-ASFSFDVFVGDIartLYNGGTMVICpkdDRIDPA 1523
Cdd:PRK08316  180 SGTESLPKGAMLTHRALIAeyvscIVAG---DMSADDIPLHALPLyHCAQLDVFLGPY---LYVGATNVIL---DAPDPE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1524 RLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTE-AAIDS 1602
Cdd:PRK08316  251 LILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERL-PGLRFYNCYGQTEiAPLAT 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1603 SLY-DEPLAKLPEAgnvpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerly 1681
Cdd:PRK08316  330 VLGpEEHLRRPGSA-----GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF------- 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1682 RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYF--TAESELKLSEL 1759
Cdd:PRK08316  398 HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVvpKAGATVTEDEL 477
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 1760 RSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:PRK08316  478 IAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1322-1795 8.74e-43

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 165.34  E-value: 8.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 1401
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 THLQeraqqwgqtlqavlclddeaayaedasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 1481
Cdd:cd05935    81 SELD------------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 FPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLhywISEEKITIFESTPALIIPFMDYVAEHGLDMSSM 1561
Cdd:cd05935   125 SDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALEL---IEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1562 ELLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAidSSLYDEPLAKlPEAGNVPIGKAALNAKfyIVDAH-LNPVP 1640
Cdd:cd05935   202 KVLTGGGAPMPPAVAEKLLKLTG--LRFVEGYGLTETM--SQTHTNPPLR-PKLQCLGIP*FGVDAR--VIDIEtGRELP 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1641 VGVLGELCIGGIGVARGYLNRPELTEEKFVDspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQ 1720
Cdd:cd05935   275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 1721 LLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLS----ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05935   352 LYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKvteeDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1314-1795 9.88e-43

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 167.16  E-value: 9.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1314 AAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDS 1393
Cdd:cd05959    21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1394 AASVLLTQTHLQERAQQWGQTLQAVLC----------------LDDEAAYAEDASNVANVNePHDLAYVIYTSGTTGRPK 1457
Cdd:cd05959   101 RARVVVVSGELAPVLAAALTKSEHTLVvlivsggagpeagallLAELVAAEAEQLKPAATH-ADDPAFWLYSSGSTGRPK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1458 GVMIEHRSLVNTAAGYRRE---YRLDQfpvRLLQLASFSFDVFVGDiART--LYNGGTMVICPkdDRIDPARLHYWISEE 1532
Cdd:cd05959   180 GVVHLHADIYWTAELYARNvlgIREDD---VCFSAAKLFFAYGLGN-SLTfpLSVGATTVLMP--ERPTPAAVFKRIRRY 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1533 KITIFESTPALiipFMDYVAEHGL---DMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAaIDSSLYDEPL 1609
Cdd:cd05959   254 RPTVFFGVPTL---YAAMLAAPNLpsrDLSSLRLCVSAGEALPAEVGERWKARFGLD--ILDGIGSTEM-LHIFLSNRPG 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1610 AKLPEAGNVPIGKAALNakfyIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfvEGErLYRTGDLARW 1689
Cdd:cd05959   328 RVRYGTTGKPVPGYEVE----LRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------QGE-WTRTGDKYVR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1690 MPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYF-----TAESELKLSELRSSLS 1764
Cdd:cd05959   397 DDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVvlrpgYEDSEALEEELKEFVK 476
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 1765 QELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05959   477 DRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
PRK06188 PRK06188
acyl-CoA synthetase; Validated
4901-5388 1.34e-42

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 167.09  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:PRK06188   26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLT-QTHLQERAQQWGQ---TLQAALCLDD---------EAAYAEDASNVAnVNEPHDLAYVIYTSGTTGRPK 5047
Cdd:PRK06188  106 EDAGISTLIVdPAPFVERALALLArvpSLKHVLTLGPvpdgvdllaAAAKFGPAPLVA-AALPPDIAGLAYTGGTTGKPK 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5048 GVMIEHRSLVNTAAGYRREYRLDQFPvRLLQLASFSfDVFVGDIARTLYNGGTMVICPKddrIDPARLHYWISEEKITIF 5127
Cdd:PRK06188  185 GVMGTHRSIATMAQIQLAEWEWPADP-RFLMCTPLS-HAGGAFFLPTLLRGGTVIVLAK---FDPAEVLRAIEEQRITAT 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5128 ESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQFriINAYGVTEAAIdsslydePLAKLPEAGN 5207
Cdd:PRK06188  260 FLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIF--AQYYGQTEAPM-------VITYLRKRDH 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5208 VPI--------GKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARW 5279
Cdd:PRK06188  331 DPDdpkrltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-------WLHTGDVARE 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5280 MPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQK-----VLCAHFTAESElklsELRSSL 5353
Cdd:PRK06188  404 DEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEAvtavvVLRPGAAVDAA----ELQAHV 479
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 386647928 5354 SQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 5388
Cdd:PRK06188  480 KERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
287-747 1.39e-42

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 164.91  E-value: 1.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  287 TYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGh 366
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  367 lqervsfsgtwirlDDEEAYhedgsnlesvngpehltyVIYTSGTTGKPKGNLTTHRNII----------RVVKNTNYID 436
Cdd:cd05971    87 --------------SDDPAL------------------IIYTSGTTGPPKGALHAHRVLLghlpgvqfpfNLFPRDGDLY 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  437 VTGQDkllqlssYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFIT-TAFfnVLVDMNPDCLRHA 515
Cdd:cd05971   135 WTPAD-------WAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPpTAL--KMMRQQGEQLKHA 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  516 ----RAILFGGE---RVSVSHVRKALGhlgpGKIKHVYGPTEST-VFATSYDVHEVEEGAvsipIGGPISNTAIYIVNAQ 587
Cdd:cd05971   206 qvklRAIATGGEslgEELLGWAREQFG----VEVNEFYGQTECNlVIGNCSALFPIKPGS----MGKPIPGHRVAIVDDN 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  588 NKLQPIGVAGELCVA-GDGLAR-GYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIE 665
Cdd:cd05971   278 GTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  666 LGEIEAHLLK----LEA------------IEKATVVVRESANGEKQLcayyvadrslpANEVRSTLSQELPAYMLPSYFV 729
Cdd:cd05971   351 PAEIEECLLKhpavLMAavvgipdpirgeIVKAFVVLNPGETPSDAL-----------AREIQELVKTRLAAHEYPREIE 419
                         490
                  ....*....|....*...
gi 386647928  730 QLEQMPLTTNGKVDRRAL 747
Cdd:cd05971   420 FVNELPRTATGKIRRREL 437
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
5945-6420 1.62e-42

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 167.44  E-value: 1.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDR 6023
Cdd:PRK08314   20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6024 IRYMLEDSGAKLLLVQGHLLDR---------------ASFAD------------------KLVNLNDDGAYH-----EDG 6065
Cdd:PRK08314  100 LAHYVTDSGARVAIVGSELAPKvapavgnlrlrhvivAQYSDylpaepeiavpawlraepPLQALAPGGVVAwkealAAG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6066 SNLEPVN-GPEHLTYVIYTSGTTGRPKGVMVEHRNVvrlvkNTNYVelneqthilqtGAVVFDAST-----------FEI 6133
Cdd:PRK08314  180 LAPPPHTaGPDDLAVLPYTSGTTGVPKGCMHTHRTV-----MANAV-----------GSVLWSNSTpesvvlavlplFHV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6134 WG-------ALLNGGRLYVVrneTILDAVSLKNAIQQYGInTMWLTAP--LYNQLSQQDSGMFaGLKTLI-VGGDVLSVP 6203
Cdd:PRK08314  244 TGmvhsmnaPIYAGATVVLM---PRWDREAAARLIERYRV-THWTNIPtmVVDFLASPGLAER-DLSSLRyIGGGGAAMP 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6204 H-INRVLREHAGLSIVNGYGPTEntTFSTTHTIVGEQKEAVPIGKPINNSTAYIVD-SKLSLLPVGVWGELIVGGDGVAR 6281
Cdd:PRK08314  319 EaVAERLKELTGLDYVEGYGLTE--TMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFK 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6282 GYLNRPELTAEKFVEssfLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVRE 6361
Cdd:PRK08314  397 GYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6362 DESGQKQLCAYFV--AERELTIG--ELRAALSQELPNYMIPS--HFVplERMPLTPNGKIDRRAL 6420
Cdd:PRK08314  474 DPRRGETVKAVVVlrPEARGKTTeeEIIAWAREHMAAYKYPRivEFV--DSLPKSGSGKILWRQL 536
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
7472-7928 2.26e-42

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 164.05  E-value: 2.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAqvlltqr 7551
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 hlqecvsfdgKVIAADDEQaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVV 7631
Cdd:cd05972    74 ----------KAIVTDAED-----------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7632 QFASLSFDASCW-EIFKALFFGATLYI---PAKDTILDYPLFESYmnenGITAAILPPT-YAIYLSPD----RLPSLKKL 7702
Cdd:cd05972   127 NIADPGWAKGAWsSFFGPWLLGATVFVyegPRFDAERILELLERY----GVTSFCGPPTaYRMLIKQDlssyKFSHLRLV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7703 ITGGSAASVEFVQQWKDK----VRyfNAYGPTEASIVTSVWAaspdGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAG 7778
Cdd:cd05972   203 VSAGEPLNPEVIEWWRAAtglpIR--DGYGQTETGLTVGNFP----DMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEG 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7779 ELCI--SGAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLK 7856
Cdd:cd05972   277 DIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLE 349
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7857 IASVQETIVIARGDANGQQQLCAYFV------ADRELtVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05972   350 HPAVAEAAVVGSPDPVRGEVVKAFVVltsgyePSEEL-AEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
3854-4337 2.42e-42

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 165.76  E-value: 2.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3854 QTIHGLFEEQALRNPDAVAVVFEKSQ--LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAY 3931
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3932 IPIDPEYPEDRIRYMLEDSGAQALLTQ---------RHLRERVSFAGtfVAVDDEQAYHADGSNLEPVVGPNHLAYVIYT 4002
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAVIAvdaqvmdaiFQSGVRVLALS--DLVGLGEPESAGPLIEDPPREPEQPAFVFYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4003 SGTTGKPKGVMVEHHGLCSLKLMFANTLQMT--EQDRVVQFASLSFDASCWEIF-KALFFGATLYIPTSttiLDYPLFES 4079
Cdd:cd05923   159 SGTTGLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVVEE---FDPADALK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4080 YMNENGITATILPPTY------AAYLNPDRMPSLKKLITGGSA---ASVEFVQQWKdKVLYFNAYGPTEAsiVTSIWDEa 4150
Cdd:cd05923   236 LIEQERVTSLFATPTHldalaaAAEFAGLKLSSLRHVTFAGATmpdAVLERVNQHL-PGEKVNIYGTTEA--MNSLYMR- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4151 sdslgDRKSVPIGRPLANHRIYVV---DSHNRMLPVGVAGELCISGVGLA--RGYLNRPELTAEKFVDnpfepgeRMYRT 4225
Cdd:cd05923   312 -----DARTGTEMRPGFFSEVRIVrigGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRT 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4226 GDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRE-LTAAELRA- 4303
Cdd:cd05923   380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGtLSADELDQf 459
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 4304 TMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05923   460 CRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1323-1799 3.12e-42

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 163.83  E-value: 3.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 1402
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 HLQERAqqwgqtlqavlclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRreYRLDQF 1482
Cdd:cd05969    81 ELYERT------------------------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGK--YVLDLH 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1483 PVrllqlasfsfDVF--VGD---IARTLY-------NGGTMVIcpKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 1550
Cdd:cd05969   129 PD----------DIYwcTADpgwVTGTVYgiwapwlNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKE 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1551 VAE--HGLDMSSMELLitssdsCSVTDY------RVLQERFGsqFRIINAYGVTE-AAIDSSLYDEPLAKLPEAGN-VPI 1620
Cdd:cd05969   197 GDElaRKYDLSSLRFI------HSVGEPlnpeaiRWGMEVFG--VPIHDTWWQTEtGSIMIANYPCMPIKPGSMGKpLPG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1621 GKAAlnakfyIVDAHLNPVPVGVLGELCI--GGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFI 1698
Cdd:cd05969   269 VKAA------VVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFV 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1699 GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAY------FTAESELKlSELRSSLSQELPGYMI 1772
Cdd:cd05969   336 GRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFislkegFEPSDELK-EEIINFVRQKLGAHVA 414
                         490       500
                  ....*....|....*....|....*..
gi 386647928 1773 PSYFVQLEQLPLTANGKIDRKALPAPD 1799
Cdd:cd05969   415 PREIEFVDNLPKTRSGKIMRRVLKAKE 441
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
286-751 3.18e-42

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 163.83  E-value: 3.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQG 365
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  366 HLQERVSfsgtwirlddeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTNYI-DVTGQDKLL 444
Cdd:cd05969    81 ELYERTD--------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVlDLHPDDIYW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  445 QLSSYSF-DGSTFDIFGALLNGAKLVLVpkETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLR-----HARAI 518
Cdd:cd05969   135 CTADPGWvTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARkydlsSLRFI 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  519 LFGGERVSVSHVRKALGHLGPgKIKHVYGPTES-TVFATSYDVHEVEEGAVSIPIGGPisnTAIYIVNAQNKLQPiGVAG 597
Cdd:cd05969   213 HSVGEPLNPEAIRWGMEVFGV-PIHDTWWQTETgSIMIANYPCMPIKPGSMGKPLPGV---KAAVVDENGNELPP-GTKG 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  598 ELCVAGD--GLARGYLNRPdltaEKFaDNPFAPGerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLK 675
Cdd:cd05969   288 ILALKPGwpSMFRGIWNDE----ERY-KNSFIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALME 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  676 LEAIEKATVVVRESANGEKQLCAYYVADRSLPA-----NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAP 750
Cdd:cd05969   361 HPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPsdelkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440

                  .
gi 386647928  751 E 751
Cdd:cd05969   441 E 441
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
4912-5385 3.63e-42

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 163.42  E-value: 3.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 4991
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 THLQeraqqwgqtlqaalclddeaayaedasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 5071
Cdd:cd05935    81 SELD------------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5072 FPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLhywISEEKITIFESTPALIIPFMDYVAEHGLDMSSM 5151
Cdd:cd05935   125 SDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALEL---IEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5152 VLLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAidSSLYDEPLAKlPEAGNVPIGKAALNAKfyIVDAH-LNPVP 5230
Cdd:cd05935   202 KVLTGGGAPMPPAVAEKLLKLTG--LRFVEGYGLTETM--SQTHTNPPLR-PKLQCLGIP*FGVDAR--VIDIEtGRELP 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5231 VGVLGELCIGGIGVARGYLNRPELTEEKFVDspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQ 5310
Cdd:cd05935   275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5311 LLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLS----ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05935   352 LYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKvteeDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
4894-5385 4.44e-42

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 165.03  E-value: 4.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4894 EKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQ-GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 4972
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLEDSAASVLLTQTHLQERAQ--QWGQTLQAALCLDDEAAyAEDASNVANVNEPHDLAYVI-YTSGTTGRPKGV 5049
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTFQNMALsmQKVSYVQRVISITSLKE-IEDRKIDNFVEKNESASFIIcYTSGTTGKPKGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5050 MIEH-----RSLVNTAAgyrREYRLDQFPVRLLQLasfsfdVFVGDIA----RTLYNGGTMVIcpkDDRIDPARLHYWIS 5120
Cdd:PRK06839  168 VLTQenmfwNALNNTFA---IDLTMHDRSIVLLPL------FHIGGIGlfafPTLFAGGVIIV---PRKFEPTKALSMIE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5121 EEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERfgsQFRIINAYGVTEAAIDSSLYDEPLA 5200
Cdd:PRK06839  236 KHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR---GFLFGQGFGMTETSPTVFMLSEEDA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5201 KlPEAGNvpIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWM 5280
Cdd:PRK06839  313 R-RKVGS--IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVD 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5281 PDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSE--LRSSLSQELP 5358
Cdd:PRK06839  383 EDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEkdVIEHCRLFLA 462
                         490       500
                  ....*....|....*....|....*..
gi 386647928 5359 GYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK06839  463 KYKIPKEIVFLKELPKNATGKIQKAQL 489
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
3880-4337 6.57e-42

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 162.51  E-value: 6.57e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALltqr 3959
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 hlrervsfagtfvavddeqayhadgsnlepVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVV 4039
Cdd:cd05972    77 ------------------------------VTDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4040 QFASLSFDASCW-EIFKALFFGATlyiptsTTILDYPLFES-----YMNENGITATILPPT-YAAYLNPD----RMPSLK 4108
Cdd:cd05972   127 NIADPGWAKGAWsSFFGPWLLGAT------VFVYEGPRFDAerileLLERYGVTSFCGPPTaYRMLIKQDlssyKFSHLR 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4109 KLITGGSAASVEFVQQWKDKV-LYF-NAYGPTEASIVtsiwdeasdsLGDRKSVPI-----GRPLANHRIYVVDSHNRML 4181
Cdd:cd05972   201 LVVSAGEPLNPEVIEWWRAATgLPIrDGYGQTETGLT----------VGNFPDMPVkpgsmGRPTPGYDVAIIDDDGREL 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4182 PVGVAGELCI--SGVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEV 4259
Cdd:cd05972   271 PPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4260 ETQLAKIDAVQEAIVLAREDANGQQQLVAYFV------AQRELtAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:cd05972   344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVltsgyePSEEL-AEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422

                  ....
gi 386647928 4334 RKAL 4337
Cdd:cd05972   423 RVEL 426
PRK06188 PRK06188
acyl-CoA synthetase; Validated
2356-2831 7.12e-42

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 165.16  E-value: 7.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2356 ERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRIS 2435
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2436 YMLEDSSAQVLL------AQR--RLQERVSFAGTVVTVDD--------EQAYAGDGSNLESAVGPNDLAYIIYTSGTTGK 2499
Cdd:PRK06188  103 YVLEDAGISTLIvdpapfVERalALLARVPSLKHVLTLGPvpdgvdllAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2500 PKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSfDASCWEVFQTLFFGATLYIPTKetiLDYQWFERYMSDNGITT 2579
Cdd:PRK06188  183 PKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVLAK---FDPAEVLRAIEEQRITA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2580 ATLPPTyAVYLNPDHmPDfkrlIAAGSASSLEL------------LQQWKDKVK--YFNAYGPTEDSICTTIWTP---ST 2642
Cdd:PRK06188  259 TFLVPT-MIYALLDH-PD----LRTRDLSSLETvyygaspmspvrLAEAIERFGpiFAQYYGQTEAPMVITYLRKrdhDP 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2643 EDISQLKSVpiGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKW 2722
Cdd:PRK06188  333 DDPKRLTSC--GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-------WLHTGDVARE 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2723 LPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRgELSGEL 2800
Cdd:PRK06188  404 DEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVlrPGAAVDAAELQ-AHVKER 482
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 2801 PGYM-IPAHFVQLERMPLTPNGKIDRKALPAP 2831
Cdd:PRK06188  483 KGSVhAPKQVDFVDSLPLTALGKPDKKALRAR 514
PRK08316 PRK08316
acyl-CoA synthetase; Validated
4900-5380 7.96e-42

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 164.72  E-value: 7.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4900 TPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFM 4979
Cdd:PRK08316   24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4980 LEDSAASVLLTQTHLQERAQ---------------QWGQTLQAALCLDDEAAYAEDASNVANVnEPH--DLAYVIYTSGT 5042
Cdd:PRK08316  104 LDHSGARAFLVDPALAPTAEaalallpvdtlilslVLGGREAPGGWLDFADWAEAGSVAEPDV-ELAddDLAQILYTSGT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5043 TGRPKGVMIEHRSLVN-----TAAGyrrEYRLDQFPVRLLQL-ASFSFDVFVGDIartLYNGGTMVICpkdDRIDPARLH 5116
Cdd:PRK08316  183 ESLPKGAMLTHRALIAeyvscIVAG---DMSADDIPLHALPLyHCAQLDVFLGPY---LYVGATNVIL---DAPDPELIL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5117 YWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTE-AAIDSSLY 5195
Cdd:PRK08316  254 RTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERL-PGLRFYNCYGQTEiAPLATVLG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5196 -DEPLAKLPEAgnvpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTG 5274
Cdd:PRK08316  333 pEEHLRRPGSA-----GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF-------HSG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5275 DLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHF--TAESELKLSELRSS 5352
Cdd:PRK08316  401 DLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVvpKAGATVTEDELIAH 480
                         490       500
                  ....*....|....*....|....*...
gi 386647928 5353 LSQELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:PRK08316  481 CRARLAGFKVPKRVIFVDELPRNPSGKI 508
PRK08316 PRK08316
acyl-CoA synthetase; Validated
2346-2823 9.24e-42

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 164.72  E-value: 9.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI 2425
Cdd:PRK08316   12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2426 DPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVD--------------------DEQAYAGDGSNLESAVGPN 2485
Cdd:PRK08316   92 NFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDtlilslvlggreapggwldfADWAEAGSVAEPDVELADD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2486 DLAYIIYTSGTTGKPKGVMVEHHGLCS--LKQMFAntLQINAQDRVVQ----FASLSFDascweVF--QTLFFGATLYI- 2556
Cdd:PRK08316  172 DLAQILYTSGTESLPKGAMLTHRALIAeyVSCIVA--GDMSADDIPLHalplYHCAQLD-----VFlgPYLYVGATNVIl 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2557 --PTKETILDYqwFERYmsdnGITTATLPPTyaVYLNPDHMPDFKR-----LIAAGSASS------LELLQQWKDKVKYF 2623
Cdd:PRK08316  245 daPDPELILRT--IEAE----RITSFFAPPT--VWISLLRHPDFDTrdlssLRKGYYGASimpvevLKELRERLPGLRFY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2624 NAYGPTEDSICTTIWTPStEDISQLKSVpiGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFV 2703
Cdd:PRK08316  317 NCYGQTEIAPLATVLGPE-EHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2704 DNPFepgermyRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV- 2782
Cdd:PRK08316  394 GGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVp 466
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928 2783 -ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKI 2823
Cdd:PRK08316  467 kAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
6989-7411 9.28e-42

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 161.84  E-value: 9.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6989 IYTLTPMQKGMWFHTALDKEAGAY--FEQMRFTVQGSLDAeqFARSWNDLVARHAILRTNFFSGPRGEPLQIVYRDKRIg 7066
Cdd:cd19544     1 IYPLAPLQEGILFHHLLAEEGDPYllRSLLAFDSRARLDA--FLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAEL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7067 fvyeDLSHLPADERQASVERLEQEDIARGF--DLEQDALVRVAVIRTQET-SYRVLWSFHHILMDGWCLPLVVKELfety 7143
Cdd:cd19544    78 ----PVEELTLDPGDDALAQLRARFDPRRYrlDLRQAPLLRAHVAEDPANgRWLLLLLFHHLISDHTSLELLLEEI---- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7144 EAYVQGDRPEQKAAPAYSQYIEW-LENQDSAAASAYWSNYLAGYEgQTALPQEKAQKRSEGYVAEHVVCELDKELSERMN 7222
Cdd:cd19544   150 QAILAGRAAALPPPVPYRNFVAQaRLGASQAEHEAFFREMLGDVD-EPTAPFGLLDVQGDGSDITEARLALDAELAQRLR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7223 RAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVACQpEESFADVMGRMQEA 7302
Cdd:cd19544   229 AQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHAR 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7303 ALESGRYDFYPLYEIQTQS--AQKQELINHLLvfeNYPMDEQVEQAGGDDSGTlSITDVDVAEHTNYNFTVTV--FpGDE 7378
Cdd:cd19544   308 LAELLRHEHASLALAQRCSgvPAPTPLFSALL---NYRHSAAAAAAAALAAWE-GIELLGGEERTNYPLTLSVddL-GDG 382
                         410       420       430
                  ....*....|....*....|....*....|...
gi 386647928 7379 IVVRFDynsfVFERADMERLKGHLLHMLEQIVA 7411
Cdd:cd19544   383 FSLTAQ----VVAPIDAERVCAYMETALEQLVD 411
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1322-1790 9.52e-42

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 162.55  E-value: 9.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 1401
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 ThlqeraqQWGQTlqavlcldDEAAyaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 1481
Cdd:cd05903    81 E-------RFRQF--------DPAA------------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 FPVRLLQLASFSFDVFVGDIARTLYNGGTMVICpkdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSM 1561
Cdd:cd05903   134 GDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1562 ELLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTE--AAIDSSLYDEPLAKLPEAGNVpigkaALNAKFYIVDAHLNPV 1639
Cdd:cd05903   211 RTFVCGGATVPRSLARRAAELLGA--KVCSAYGSTEcpGAVTSITPAPEDRRLYTDGRP-----LPGVEIKVVDDTGATL 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1640 PVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVdfigRIDNQAK---IR-GYRIETG 1715
Cdd:cd05903   284 APGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYL----RITGRSKdiiIRgGENIPVL 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 1716 EIETQLLKAEGVREAVVVVREDAK-GQKVlCAYFTAES--ELKLSELRSSLS-QELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:cd05903   353 EVEDLLLGHPGVIEAAVVALPDERlGERA-CAVVVTKSgaLLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
7470-7869 9.54e-42

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 162.76  E-value: 9.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7470 TQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLT 7549
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7550 QrhlqecvsfdgkviaaddeqaygedgsnlepvvGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDR 7629
Cdd:cd05907    84 E---------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDR 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7630 VVQFASLS--FDASCWEIFkALFFGATLYIPAKDTIL--DYP------------LFE-SYmneNGITAAILPP-TYAIYL 7691
Cdd:cd05907   131 HLSFLPLAhvFERRAGLYV-PLLAGARIYFASSAETLldDLSevrptvflavprVWEkVY---AAIKVKAVPGlKRKLFD 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7692 SPdRLPSLKKLITGGSAASVEFVQQW-KDKVRYFNAYGPTEASIVTSVWaaSPDGLDLRSVpiGRPIANHQIFIVDSqnh 7770
Cdd:cd05907   207 LA-VGGRLRFAASGGAPLPAELLHFFrALGIPVYEGYGLTETSAVVTLN--PPGDNRIGTV--GKPLPGVEVRIADD--- 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7771 mlpvgvaGELCISGAGLARGYLNRPELTAEKFVDNPFLAgermyrTGDLARWLPDGNIEYLGRI-DHQVKIRGYRIELGE 7849
Cdd:cd05907   279 -------GEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEP 345
                         410       420
                  ....*....|....*....|
gi 386647928 7850 IEEQLLKIASVQETIVIARG 7869
Cdd:cd05907   346 IENALKASPLISQAVVIGDG 365
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
7471-7928 1.01e-41

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 162.26  E-value: 1.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7471 QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTq 7550
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7551 rhlqecvsfdgkviaaddeqaygedGSNLEpvvgpnHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRV 7630
Cdd:cd05935    80 -------------------------GSELD------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7631 VQ----FASLSFDAScweIFKALFFGATLYIPA---KDTILDypLFESYmnenGITAAILPPTYAIYL--SP---DR-LP 7697
Cdd:cd05935   129 LAclplFHVTGFVGS---LNTAVYVGGTYVLMArwdRETALE--LIEKY----KVTFWTNIPTMLVDLlaTPefkTRdLS 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7698 SLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEASIVTSVwaaSPDGlDLRSVPIGRPIANHQIFIVDSQN-HMLPV 7774
Cdd:cd05935   200 SLKVLTGGGAPMPPAVAEKLLKLtgLRFVEGYGLTETMSQTHT---NPPL-RPKLQCLGIP*FGVDARVIDIETgRELPP 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7775 GVAGELCISGAGLARGYLNRPELTAEKFVDnpfLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQL 7854
Cdd:cd05935   276 NEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7855 LKIASVQETIVIARGDANGQQQLCAYFVADreltvSELRGTLSQE---------LPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd05935   353 YKHPAI*EVCVISVPDERVGEEVKAFIVLR-----PEYRGKVTEEdiiewareqMAAYKYPREVEFVDELPRSASGKILW 427

                  ...
gi 386647928 7926 NAL 7928
Cdd:cd05935   428 RLL 430
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
256-747 1.03e-41

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 164.55  E-value: 1.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  256 YPRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGG 335
Cdd:COG1021    21 YWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  336 ayVPIDPeYPEER---IRYMLEDSG-------------------TQVLLSQGHLQERVSF--SGTWIRLDDeeAYHEDGS 391
Cdd:COG1021   101 --IPVFA-LPAHRraeISHFAEQSEavayiipdrhrgfdyralaRELQAEVPSLRHVLVVgdAGEFTSLDA--LLAAPAD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  392 NLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTNYI-DVTGQDKLLQLS--SYSFDGSTFDIFGALLNGAKL 468
Cdd:COG1021   176 LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEIcGLDADTVYLAALpaAHNFPLSSPGVLGVLYAGGTV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  469 VLVPK---ETVLDvaklagLIEKQQISVmfitTAffnvLV-----------DMNPDCLRHARAILFGGERVSVSH---VR 531
Cdd:COG1021   256 VLAPDpspDTAFP------LIERERVTV----TA----LVpplallwldaaERSRYDLSSLRVLQVGGAKLSPELarrVR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  532 KALGHlgpgKIKHVYGPTESTVFATSYD------VHEVeegavsipiGGPIS-NTAIYIVNAQNKLQPIGVAGELCVAGD 604
Cdd:COG1021   322 PALGC----TLQQVFGMAEGLVNYTRLDdpeeviLTTQ---------GRPISpDDEVRIVDEDGNPVPPGEVGELLTRGP 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  605 GLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVkIRGfrielGE------IEAHLLKLEA 678
Cdd:COG1021   389 YTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPA 456
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  679 IEKATVV-VRESANGEKqLCAYYVA-DRSLPANEVRSTL-SQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:COG1021   457 VHDAAVVaMPDEYLGER-SCAFVVPrGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
3861-4337 1.27e-41

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 163.49  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3861 EEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLR-DAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYP 3939
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3940 EDRIRYMLEDSGAQALLTQRH-------LRERVSFAGTFVAVDDEQAYHADGSNLEPvvGPNHLAYVI-YTSGTTGKPKG 4011
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTfqnmalsMQKVSYVQRVISITSLKEIEDRKIDNFVE--KNESASFIIcYTSGTTGKPKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4012 VMVEHHGlcslklMFAN------TLQMTEQDRVVQFASLsFDASCWEIFK--ALFFGATLYIPTSttiLDYPLFESYMNE 4083
Cdd:PRK06839  167 AVLTQEN------MFWNalnntfAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIVPRK---FEPTKALSMIEK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4084 NGITATI-LPPTYAAYLN-PDR----MPSLKKLITGGSAASVEFVQQWKDKVLYF-NAYGPTEASIVTSIWDEASDSlgd 4156
Cdd:PRK06839  237 HKVTVVMgVPTIHQALINcSKFettnLQSVRWFYNGGAPCPEELMREFIDRGFLFgQGFGMTETSPTVFMLSEEDAR--- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4157 RKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermyRTGDLVRWLPDGN 4236
Cdd:PRK06839  314 RKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDEDGF 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4237 LEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRE--LTAAELRATMSQELPNYMI 4314
Cdd:PRK06839  387 VYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSsvLIEKDVIEHCRLFLAKYKI 466
                         490       500
                  ....*....|....*....|...
gi 386647928 4315 PSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK06839  467 PKEIVFLKELPKNATGKIQKAQL 489
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
2341-2828 1.73e-41

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 164.54  E-value: 1.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2341 YEADKTIHQLFEEQAERIPDHPAVVFE-GQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAG 2419
Cdd:PRK06087   19 YWGDASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2420 GAYVPIDPEYPEDRISYMLEDSSAQVLLA-----QRR-------LQERVSFAGTVVTVDDEQ------AYA---GDGSNL 2478
Cdd:PRK06087   99 AVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkQTRpvdlilpLQNQLPQLQQIVGVDKLApatsslSLSqiiADYEPL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2479 ESA--VGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSfdascwevFQTLFFG---AT 2553
Cdd:PRK06087  179 TTAitTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLG--------HATGFLHgvtAP 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2554 LYIPTKETILDyqwfeRYMSDNGIT-------TATLPPTYAVY--LN-----PDHMPDFKRLIAAGSASSLELLQQ-WKD 2618
Cdd:PRK06087  251 FLIGARSVLLD-----IFTPDACLAlleqqrcTCMLGATPFIYdlLNllekqPADLSALRFFLCGGTTIPKKVAREcQQR 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2619 KVKYFNAYGPTEDsiCTTIWTPSTEDISQLKSVPiGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLT 2698
Cdd:PRK06087  326 GIKLLSVYGSTES--SPHAVVNLDDPLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2699 AeKFVDNpfepgERMYRTGDLAKWLPDGTIEYLGRiDHQVKIR-GYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQL 2777
Cdd:PRK06087  403 A-RALDE-----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERS 475
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 2778 CAYFV---ADRTMTVGELRGELSGE-LPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK06087  476 CAYVVlkaPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1299-1791 1.79e-41

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 163.90  E-value: 1.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1299 FHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 1378
Cdd:PRK07798    5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1379 PDYPSDRIQFMLEDSAASVLLTQTHLQER-AQQWGQT--LQAVLCLDDEAAYA--------EDAsnVANVNEPHDLA--- 1444
Cdd:PRK07798   85 YRYVEDELRYLLDDSDAVALVYEREFAPRvAEVLPRLpkLRTLVVVEDGSGNDllpgavdyEDA--LAAGSPERDFGers 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1445 ----YVIYTSGTTGRPKGVMIEH----RSLVNTAAGYRREYRLD---------------QFPVRLL-----QLASFSfdv 1496
Cdd:PRK07798  163 pddlYLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDeeelakraaagpgmrRFPAPPLmhgagQWAAFA--- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1497 fvgdiarTLYNGGTMVICPkDDRIDPARLHYWISEEKIT-IFESTPALIIPFMD-YVAEHGLDMSSMELLITSSDSCSVT 1574
Cdd:PRK07798  240 -------ALFSGQTVVLLP-DVRFDADEVWRTIEREKVNvITIVGDAMARPLLDaLEARGPYDLSSLFAIASGGALFSPS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1575 DYRVLQERFgSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGKAALnakfyIVDAHLNPVPVGvlgelcIGGIG- 1653
Cdd:PRK07798  312 VKEALLELL-PNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTV-----VLDEDGNPVEPG------SGEIGw 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1654 VAR------GYLNRPELTEEKFvdsPFVEGERLYRTGDLARWMPDGNVDFIGRiDNQAkirgyrIETG-------EIEtQ 1720
Cdd:PRK07798  380 IARrghiplGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR-GSVC------INTGgekvfpeEVE-E 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1721 LLKAEGvreavvvVREDAK---------GQKVLCAYFTAE-SELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:PRK07798  449 ALKAHP-------DVADALvvgvpderwGQEVVAVVQLREgARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKA 521

                  .
gi 386647928 1791 D 1791
Cdd:PRK07798  522 D 522
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1306-1804 2.04e-41

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 162.67  E-value: 2.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1306 QAERTPE-VAAVVYENDR-LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 1383
Cdd:PRK09088    4 HARLQPQrLAAVDLALGRrWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1384 DRIQFMLEDSAASVLLTQTHLQERAQQwgqtlqaVLCLDDEAAYAEDASNVANVNEPHD-LAYVIYTSGTTGRPKGVMIE 1462
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVAAGRTD-------VEDLAAFIASADALEPADTPSIPPErVSLILFTSGTSGQPKGVMLS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1463 HRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpkDDRIDPARLHYWISEEK--ITIFEST 1540
Cdd:PRK09088  157 ERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILV---SNGFEPKRTLGRLGDPAlgITHYFCV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1541 PALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQErfgSQFRIINAYGVTEA------AIDSSLYDeplAKLPE 1614
Cdd:PRK09088  234 PQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLD---DGIPMVDGFGMSEAgtvfgmSVDCDVIR---AKAGA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1615 AgnvpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfvEGERLYRTGDLARWMPDGN 1694
Cdd:PRK09088  308 A-----GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGF 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1695 VDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKV--LCAYFTAESELKLSELRSSLSQELPGYMI 1772
Cdd:PRK09088  377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVgyLAIVPADGAPLDLERIRSHLSTRLAKYKV 456
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 1773 PSYFVQLEQLPLTANGKIDRKALPAPDASMQT 1804
Cdd:PRK09088  457 PKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
PRK06188 PRK06188
acyl-CoA synthetase; Validated
3866-4340 2.05e-41

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 163.62  E-value: 2.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3866 RNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRY 3945
Cdd:PRK06188   24 RYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3946 MLEDSGAQALL------TQR--HLRERV-------SFAGTFVAVD-DEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKP 4009
Cdd:PRK06188  104 VLEDAGISTLIvdpapfVERalALLARVpslkhvlTLGPVPDGVDlLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4010 KGVMVEHHGLCSLklmfaNTLQMTEqdrvvqfaslsfdascWEIFKALFF---------GATLYIPT----STTIL---- 4072
Cdd:PRK06188  184 KGVMGTHRSIATM-----AQIQLAE----------------WEWPADPRFlmctplshaGGAFFLPTllrgGTVIVlakf 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4073 DYPLFESYMNENGITATILPPT--YAAYLNPD----RMPSLKKLITGGSAASVEFVQQWKDKV--LYFNAYGPTEASIVT 4144
Cdd:PRK06188  243 DPAEVLRAIEEQRITATFLVPTmiYALLDHPDlrtrDLSSLETVYYGASPMSPVRLAEAIERFgpIFAQYYGQTEAPMVI 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4145 SIWDEASDSLGD-RKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNpfepgerMY 4223
Cdd:PRK06188  323 TYLRKRDHDPDDpKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-------WL 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4224 RTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRE--LTAAEL 4301
Cdd:PRK06188  396 HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGaaVDAAEL 475
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 386647928 4302 RATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAP 4340
Cdd:PRK06188  476 QAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3398-3821 2.28e-41

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 160.94  E-value: 2.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3398 YALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYKPVEFAY 3477
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEE-DGVPFQKIEPSKPLSFQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3478 EDLRHLAEAEWSAYLDQLVNDDktrgFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYL-- 3555
Cdd:cd20484    81 EDISSLKESEIIAYLREKAKEP----FVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLqg 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3556 RNDLSErPAAPSYSHYIEWleKQDMEAAAR------YWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERM 3629
Cdd:cd20484   157 KQPTLA-SSPASYYDFVAW--EQDMLAGAEgeehraYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3630 SRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEiaGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQE 3709
Cdd:cd20484   234 KSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3710 AALEsgGYDY--YPlYEIQAQSAQKQDLITHIMAFENFPMDEQIEQAGSYED------GKLAITDVD-IAEQTNYDFTLV 3780
Cdd:cd20484   312 TVLD--GLDHaaYP-FPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTSLQQflaeyqDVLSIEFVEgIHQEGEYELVLE 388
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 386647928 3781 VMPGEE-LAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd20484   389 VYEQEDrFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
267-747 2.29e-41

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 162.72  E-value: 2.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  267 EEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYP 345
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  346 EERIRYMLEDSGTQVLLSQGHLQ------ERVSFSGTWIRLDDeEAYHEDGSNLESVNGPEHLTYVI-YTSGTTGKPKGN 418
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTFQnmalsmQKVSYVQRVISITS-LKEIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  419 LTTHRNII-RVVKNTNYIDVTGQDK-LLQLSSYSFDGSTFDIFGALLNGAKlVLVPKEtvLDVAKLAGLIEKQQISVMF- 495
Cdd:PRK06839  168 VLTQENMFwNALNNTFAIDLTMHDRsIVLLPLFHIGGIGLFAFPTLFAGGV-IIVPRK--FEPTKALSMIEKHKVTVVMg 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  496 ---ITTAFFNVLVDMNPDcLRHARAILFGGERVSVSHVRKALGH---LGPGkikhvYGPTES--TVFATSYDVHEVEEGA 567
Cdd:PRK06839  245 vptIHQALINCSKFETTN-LQSVRWFYNGGAPCPEELMREFIDRgflFGQG-----FGMTETspTVFMLSEEDARRKVGS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  568 vsipIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFApgermyrTGDLARWLPDGTI 647
Cdd:PRK06839  319 ----IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC-------TGDLARVDEDGFV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  648 EYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYV--ADRSLPANEVRSTLSQELPAYMLP 725
Cdd:PRK06839  388 YIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVkkSSSVLIEKDVIEHCRLFLAKYKIP 467
                         490       500
                  ....*....|....*....|..
gi 386647928  726 SYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK06839  468 KEIVFLKELPKNATGKIQKAQL 489
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
4904-5385 2.39e-41

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 162.92  E-value: 2.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4904 AAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDS 4983
Cdd:cd05959    21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4984 AASVLLTQTHLQERAQQWGQTLQAALC----------------LDDEAAYAEDASNVANVNePHDLAYVIYTSGTTGRPK 5047
Cdd:cd05959   101 RARVVVVSGELAPVLAAALTKSEHTLVvlivsggagpeagallLAELVAAEAEQLKPAATH-ADDPAFWLYSSGSTGRPK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5048 GVMIEHRSLVNTAAGYRRE---YRLDQfpvRLLQLASFSFDVFVGDiART--LYNGGTMVICPkdDRIDPARLHYWISEE 5122
Cdd:cd05959   180 GVVHLHADIYWTAELYARNvlgIREDD---VCFSAAKLFFAYGLGN-SLTfpLSVGATTVLMP--ERPTPAAVFKRIRRY 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5123 KITIFESTPALiipFMDYVAEHGL---DMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAaIDSSLYDEPL 5199
Cdd:cd05959   254 RPTVFFGVPTL---YAAMLAAPNLpsrDLSSLRLCVSAGEALPAEVGERWKARFGLD--ILDGIGSTEM-LHIFLSNRPG 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5200 AKLPEAGNVPIGKAALNakfyIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfvEGErLYRTGDLARW 5279
Cdd:cd05959   328 RVRYGTTGKPVPGYEVE----LRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------QGE-WTRTGDKYVR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5280 MPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQK------VLCAHFTAESELKlSELRSSL 5353
Cdd:cd05959   397 DDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTkpkafvVLRPGYEDSEALE-EELKEFV 475
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 5354 SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05959   476 KDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
2371-2828 2.47e-41

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 160.59  E-value: 2.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVllaqr 2450
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2451 rlqervsfagtvvtvddeqayagdgsnlesavgpNDLAYIIYTSGTTGKPKGVMvehhglcslkQMFAN----------T 2520
Cdd:cd05912    77 ----------------------------------DDIATIMYTSGTTGKPKGVQ----------QTFGNhwwsaigsalN 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2521 LQINAQDR------VVQFASLSFdascweVFQTLFFGATLYIPTKetiLDYQWFERYMSDNGITTATLPPTY-----AVY 2589
Cdd:cd05912   113 LGLTEDDNwlcalpLFHISGLSI------LMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMlqrllEIL 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2590 LNPDHmPDFKRLIAAGSASSLELLQQWKDK-VKYFNAYGPTEdsICTTIWTPSTEDiSQLKSVPIGGPIVNHRIYIVDAH 2668
Cdd:cd05912   184 GEGYP-NNLRCILLGGGPAPKPLLEQCKEKgIPVYQSYGMTE--TCSQIVTLSPED-ALNKIGSAGKPLFPVELKIEDDG 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2669 YQPVPVGvagELCIAGVGLARGYLNRPDLTAEKFVDNPFEpgermyrTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELG 2748
Cdd:cd05912   260 QPPYEVG---EILLKGPNVTKGYLNRPDATEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2749 EIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05912   330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1295-1795 2.51e-41

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 163.39  E-value: 2.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1295 ENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPnqlvgilADR-------SADLLVGALAV 1367
Cdd:COG1021    23 RGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRP-------GDRvvvqlpnVAEFVIVFFAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1368 WKAGGAYVPLdpdYPSDR---IQFMLEDSAASVLLTQTH--------LQERAQQWGQTLQAVLCLDD-------EAAYAE 1429
Cdd:COG1021    96 FRAGAIPVFA---LPAHRraeISHFAEQSEAVAYIIPDRhrgfdyraLARELQAEVPSLRHVLVVGDageftslDALLAA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1430 DASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQL-----ASFSFDVFVGdiarT 1504
Cdd:COG1021   173 PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALpaahnFPLSSPGVLG----V 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1505 LYNGGTMVICPkddRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFG 1584
Cdd:COG1021   249 LYAGGTVVLAP---DPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1585 SQfrIINAYGVTEAAI------DS------------SLYDEPLaklpeagnvpigkaalnakfyIVDAHLNPVPVGVLGE 1646
Cdd:COG1021   326 CT--LQQVFGMAEGLVnytrldDPeevilttqgrpiSPDDEVR---------------------IVDEDGNPVPPGEVGE 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1647 LCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRIDNQAkIR-GYRIETGEIETQLLKAE 1725
Cdd:COG1021   383 LLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHP 455
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 1726 GVREAVVVVREDAK-GQKVlCAYFTA-ESELKLSELRSSL-SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:COG1021   456 AVHDAAVVAMPDEYlGERS-CAFVVPrGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
5492-5900 2.86e-41

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 159.66  E-value: 2.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5492 PVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVNGEP----------VQRV-- 5559
Cdd:cd19537     3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLrrsyssspprVQRVdt 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5560 ---YKEVNfavehyrtseaeagevvrgfvRTFDLAKPPLLRVglvELAEDlhILLLDMHHIVSDGVSTDVLTEEFGRMYN 5636
Cdd:cd19537    83 ldvWKEIN---------------------RPFDLEREDPIRV---FISPD--TLLVVMSHIICDLTTLQLLLREVSAAYN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5637 GESLAPLRIQYKDYATWQQSEAQQEQmkrqeAYWLDMFRGeLPVLELPtdyPRPAVRKFEGSLLQRQLEPKLGEGLQRIA 5716
Cdd:cd19537   137 GKLLPPVRREYLDSTAWSRPASPEDL-----DFWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFS 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5717 AESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTHSDLQPIIGMFVNTLAIR-SYPD-DKKTFRSFLDEVKETMLG 5794
Cdd:cd19537   208 TSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRiRFPSsSDASAADFLRAVRRSSQA 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5795 AYEHqSYPFEELVEKAQPARDLSRNPLFDTL--FALQNKETGELQLDGLRLTPYPAEHtvAKFDLSVDVTE-GSEGLELS 5871
Cdd:cd19537   288 ALAH-AIPWHQLLEHLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVEPLYTWAEG--AKFPLMFEFTAlSDDSLLLR 364
                         410       420
                  ....*....|....*....|....*....
gi 386647928 5872 MEYSTALYTRETIERMAKHFEQLLTAIVQ 5900
Cdd:cd19537   365 LEYDTDCFSEEEIDRIESLILAALELLVE 393
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
7453-7928 4.24e-41

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 161.95  E-value: 4.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7453 EEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYP 7531
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7532 EDRIRYMLEDSGAQVLLTQR-------------HLQECVSFDGKVIAADDEQAYGEDGSNLEPVVgpnhlayVIYTSGTT 7598
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKtfqnmalsmqkvsYVQRVISITSLKEIEDRKIDNFVEKNESASFI-------ICYTSGTT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7599 GKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLsFDASCWEIFK--ALFFGATLYIPAKdtiLDYPLFESYMNEN 7676
Cdd:PRK06839  162 GKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIVPRK---FEPTKALSMIEKH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7677 GITAAILPPTY--AIYLSPDR----LPSLKKLITGGSAASVEFVQQWKDK-VRYFNAYGPTEASivTSVWAASPDGLDLR 7749
Cdd:PRK06839  238 KVTVVMGVPTIhqALINCSKFettnLQSVRWFYNGGAPCPEELMREFIDRgFLFGQGFGMTETS--PTVFMLSEEDARRK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7750 SVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWLPDGNIE 7829
Cdd:PRK06839  316 VGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDEDGFVY 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7830 YLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPS 7907
Cdd:PRK06839  389 IVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVkkSSSVLIEKDVIEHCRLFLAKYKIPK 468
                         490       500
                  ....*....|....*....|.
gi 386647928 7908 YFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK06839  469 EIVFLKELPKNATGKIQKAQL 489
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
5491-5902 5.17e-41

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 159.92  E-value: 5.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5491 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN-GEPVQRVYKEVNFAV-E 5568
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVtE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5569 HYRTSEAEAGEVVRGFV-----RTFDLAKPPLLRVGLVELAEDLHILL-LDMHHIVSDGVSTDVLTEEFGRMYNG----- 5637
Cdd:cd19536    82 LDLTPLEEQLDPLRAYKeetkiRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQlleyk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5638 -ESLAPlRIQYKDYATWQQSEAQQEQMkrqEAYWLDMFRG-ELPVLElptdYPRPAVRKFEGSLLQRQLEPKLGEGLQRI 5715
Cdd:cd19536   162 pLSLPP-AQPYRDFVAHERASIQQAAS---ERYWREYLAGaTLATLP----ALSEAVGGGPEQDSELLVSVPLPVRSRSL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5716 AAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTH--SDLQPIIGMFVNTLAIR-SYPDDkkTFRSFLDEVKETM 5792
Cdd:cd19536   234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRvTLSEE--TVEDLLKRAQEQE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5793 LGAYEHQSYPFEELvekaqpARDLSRNPLFDTLFALQN-------KETGELQLDGLRLTPYpAEHTVAKFDLSVDVTEGS 5865
Cdd:cd19536   312 LESLSHEQVPLADI------QRCSEGEPLFDSIVNFRHfdldfglPEWGSDEGMRRGLLFS-EFKSNYDVNLSVLPKQDR 384
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 386647928 5866 egLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19536   385 --LELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK12467 PRK12467
peptide synthase; Provisional
8016-8459 5.68e-41

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 169.96  E-value: 5.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8016 GLEQEEHSAIPV-IGERE-YYPVSSAQKRLfILHQLEGAQQSYNIPGFAT-IEGpLDRDRFEAVFRQLIERHETLRTGFE 8092
Cdd:PRK12467 2627 GLSQEQLDRLPVaVGDIEdIYPLSPMQQGM-LFHTLYEGGAGDYINQMRVdVEG-LDVERFRTAWQAVIDRHEILRSGFL 2704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8093 MANG--EPVQRVYSDVEFAVEY----SKADREEAVE---IAQRfVRPFDLRKPPLLRVGLIEVEPERHILMLDMHHIISD 8163
Cdd:PRK12467 2705 WDGEleEPLQVVYKQARLPFSRldwrDRADLEQALDalaAADR-QQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMD 2783
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8164 GASVGILQEEFSRLYAGEELPPLRIQYKDYAAW-QRSEAYAkrvkqQEGYWLQTLAGelpvIELPTDYERT----STRSF 8238
Cdd:PRK12467 2784 GWSGSQLLGEVLQRYFGQPPPAREGRYRDYIAWlQAQDAEA-----SEAFWKEQLAA----LEEPTRLARAlypaPAEAV 2854
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8239 EG-AELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTH--ADVEPIIGMFVNTLAIR 8315
Cdd:PRK12467 2855 AGhGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAqlRGAEQQLGLFINTLPVI 2934
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8316 NYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEElverlnVKRDASR--NPVFDTMFV---------LQNTEDRGIEADAF 8384
Cdd:PRK12467 2935 ASPRAEQTVSDWLQQVQAQNLALREFEHTPLAD------IQRWAGQggEALFDSILVfenypiseaLKQGAPSGLRFGAV 3008
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 8385 SltpfVFDQTvaaQFDLTLSVAEDDgAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQLNEPE 8459
Cdd:PRK12467 3009 S----SREQT---NYPLTLAVGLGD-TLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAH 3075
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
3845-4243 6.21e-41

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 163.73  E-value: 6.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3845 NTAAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQ----LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVG 3920
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDGiwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3921 IMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALL--TQRHL------RERVSFAGTFVAVDDEQAYH----------- 3981
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLdkllevRDELPSLRHIVVLDPRGLRDdprllsldell 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3982 ADGSNLEPV---------VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLS--FdASC 4050
Cdd:COG1022   162 ALGREVADPaelearraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAhvF-ERT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4051 WEIFkALFFGATLYIPTST-TILDY-----P--------LFESYMneNGITATI--LPPT--------------YAAYLN 4100
Cdd:COG1022   241 VSYY-ALAAGATVAFAESPdTLAEDlrevkPtfmlavprVWEKVY--AGIQAKAeeAGGLkrklfrwalavgrrYARARL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4101 PDRMPSL--------------KKL-----------ITGGSAASVEfVQQWkdkvlyFNA--------YGPTEASIVTSIW 4147
Cdd:COG1022   318 AGKSPSLllrlkhaladklvfSKLrealggrlrfaVSGGAALGPE-LARF------FRAlgipvlegYGLTETSPVITVN 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4148 deasdSLGDRK--SVpiGRPLAN--HRIyvvdshnrmlpvGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermY 4223
Cdd:COG1022   391 -----RPGDNRigTV--GPPLPGveVKI------------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------L 445
                         490       500
                  ....*....|....*....|
gi 386647928 4224 RTGDLVRWLPDGNLEYLGRI 4243
Cdd:COG1022   446 HTGDIGELDEDGFLRITGRK 465
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
278-747 7.46e-41

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 159.93  E-value: 7.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  278 AVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSG 357
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  358 TQVLLSQGhlqervsfsgtwirlDDeeayhedgsnlesvngpehLTYVIYTSGTTGKPKGNLTTHRNIIRVVK--NTNYI 435
Cdd:cd05919    83 ARLVVTSA---------------DD-------------------IAYLLYSSGTTGPPKGVMHAHRDPLLFADamAREAL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  436 DVTGQDKLLQLS----SYSFDGStfdIFGALLNGAKLVLVPkeTVLDVAKLAGLIEKQQISVMFITTAFF-NVLV--DMN 508
Cdd:cd05919   129 GLTPGDRVFSSAkmffGYGLGNS---LWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYaNLLDscAGS 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  509 PDCLRHARAILFGGERVSVSHVRKALGHLGpGKIKHVYGPTESTVFATSYDVHEVEEGAVsipiGGPISNTAIYIVNAQN 588
Cdd:cd05919   204 PDALRSLRLCVSAGEALPRGLGERWMEHFG-GPILDGIGATEVGHIFLSNRPGAWRLGST----GRPVPGYEIRLVDEEG 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  589 KLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGE 668
Cdd:cd05919   279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  669 IEAHLLKLEAIEKATVV-VRESANGEKqLCAYYVADRSLP-----ANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKV 742
Cdd:cd05919   352 VESLIIQHPAVAEAAVVaVPESTGLSR-LTAFVVLKSPAApqeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430

                  ....*
gi 386647928  743 DRRAL 747
Cdd:cd05919   431 QRFKL 435
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
4912-5380 7.48e-41

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 159.85  E-value: 7.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 4991
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 ThlqeraqQWGQTLQAAlclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 5071
Cdd:cd05903    81 E-------RFRQFDPAA--------------------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5072 FPVRLLQLASFSFDVFVGDIARTLYNGGTMVICpkdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSM 5151
Cdd:cd05903   134 GDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5152 VLLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTE--AAIDSSLYDEPLAKLPEAGNVpigkaALNAKFYIVDAHLNPV 5229
Cdd:cd05903   211 RTFVCGGATVPRSLARRAAELLGA--KVCSAYGSTEcpGAVTSITPAPEDRRLYTDGRP-----LPGVEIKVVDDTGATL 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5230 PVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVdfigRIDNQAK---IR-GYRIETG 5305
Cdd:cd05903   284 APGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYL----RITGRSKdiiIRgGENIPVL 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5306 EIETQLLKAEGVREAVVVVREDAK-GQKVlCAHFTAES--ELKLSELRSSLS-QELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:cd05903   353 EVEDLLLGHPGVIEAAVVALPDERlGERA-CAVVVTKSgaLLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
PRK09088 PRK09088
acyl-CoA synthetase; Validated
4896-5394 8.53e-41

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 161.13  E-value: 8.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4896 QAECTPEAAAVV--YENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 4973
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4974 DRIQFMLEDSAASVLLTQTHLQEraqqwGQTLQAALCLDDEAAYAEDASNVANVnEPHDLAYVIYTSGTTGRPKGVMIEH 5053
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVAA-----GRTDVEDLAAFIASADALEPADTPSI-PPERVSLILFTSGTSGQPKGVMLSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5054 RSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpkDDRIDPARLHYWISEEK--ITIFESTP 5131
Cdd:PRK09088  158 RNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILV---SNGFEPKRTLGRLGDPAlgITHYFCVP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 ALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQErfgSQFRIINAYGVTEA------AIDSSLYDeplAKLPEA 5205
Cdd:PRK09088  235 QMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLD---DGIPMVDGFGMSEAgtvfgmSVDCDVIR---AKAGAA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5206 gnvpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfvEGERLYRTGDLARWMPDGNV 5285
Cdd:PRK09088  309 -----GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGFF 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5286 DFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKV--LCAHFTAESELKLSELRSSLSQELPGYMIP 5363
Cdd:PRK09088  378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVgyLAIVPADGAPLDLERIRSHLSTRLAKYKVP 457
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 5364 SYFVQLEQLPLTANGKIDRKALPAPDASMQT 5394
Cdd:PRK09088  458 KHLRLVDALPRTASGKLQKARLRDALAAGRK 488
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1317-1795 9.53e-41

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 159.55  E-value: 9.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1317 VYENDR-LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAA 1395
Cdd:cd05919     4 FYAADRsVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1396 SVLltqthlqeraqqwgqtlqavlclddeaaYAEDAsnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR 1475
Cdd:cd05919    84 RLV----------------------------VTSAD----------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1476 EYRLDQFPVRLLQLASFSFDVFVGD-IARTLYNGGTMVICPkdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEH 1554
Cdd:cd05919   126 EALGLTPGDRVFSSAKMFFGYGLGNsLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1555 GLDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAidsSLYdepLAKLPeaGNVPIGKAALNAKFY---I 1631
Cdd:cd05919   204 PDALRSLRLCVSAGEALPRGLGERWMEHFGGP--ILDGIGATEVG---HIF---LSNRP--GAWRLGSTGRPVPGYeirL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1632 VDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYR 1711
Cdd:cd05919   274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1712 IETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSE-----LRSSLSQELPGYMIPSYFVQLEQLPLTA 1786
Cdd:cd05919   347 VSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslardIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                  ....*....
gi 386647928 1787 NGKIDRKAL 1795
Cdd:cd05919   427 TGKLQRFKL 435
PRK06145 PRK06145
acyl-CoA synthetase; Validated
7456-7928 1.09e-40

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 160.82  E-value: 1.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLLTQRHLQECVSFDGKVIAAD-----DEQAYGEDGSNLEP--VVGPNHLAYVIYTSGTTGKPKGVMVEH 7608
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDaaaqaDSRRLAQGGLEIPPqaAVAPTDLVRLMYTSGTTDRPKGVMHSY 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7609 HGLCSLKLMFAETLRITEEDRVVQFASLSFDASC-WEIFKALFFGATLYIPAKdtiLDYPLFESYMNENGITAAILPP-- 7685
Cdd:PRK06145  172 GNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFdLPGIAVLWVGGTLRIHRE---FDPEAVLAAIERHRLTCAWMAPvm 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7686 TYAIYLSPDR----LPSLKKLITGGSAASVEFVQQWKD---KVRYFNAYGPTEASIVTSVWAAspdGLDLRSV-PIGRPI 7757
Cdd:PRK06145  249 LSRVLTVPDRdrfdLDSLAWCIGGGEKTPESRIRDFTRvftRARYIDAYGLTETCSGDTLMEA---GREIEKIgSTGRAL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7758 ANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWLPDGNIEYLGRIDHQ 7837
Cdd:PRK06145  326 AHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLTDRKKDM 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7838 VKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPSYFVQLEQM 7915
Cdd:PRK06145  399 IISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlnPGATLTLEALDRHCRQRLASFKVPRQLKVRDEL 478
                         490
                  ....*....|...
gi 386647928 7916 PLTPNGKIDRNAL 7928
Cdd:PRK06145  479 PRNPSGKVLKRVL 491
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
4913-5389 1.10e-40

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 159.59  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 4992
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 HLQERAqqwgqtlqaalclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRreYRLDQF 5072
Cdd:cd05969    81 ELYERT------------------------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGK--YVLDLH 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5073 PVrllqlasfsfDVF--VGD---IARTLY-------NGGTMVIcpKDDRIDPARLHYWISEEKITIFESTPALIIPFMDY 5140
Cdd:cd05969   129 PD----------DIYwcTADpgwVTGTVYgiwapwlNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKE 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5141 VAE--HGLDMSSMVLLitssdsCSVTDY------RVLQERFGsqFRIINAYGVTE-AAIDSSLYDEPLAKLPEAGN-VPI 5210
Cdd:cd05969   197 GDElaRKYDLSSLRFI------HSVGEPlnpeaiRWGMEVFG--VPIHDTWWQTEtGSIMIANYPCMPIKPGSMGKpLPG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5211 GKAAlnakfyIVDAHLNPVPVGVLGELCI--GGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFI 5288
Cdd:cd05969   269 VKAA------VVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFV 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5289 GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA-KGQKV-----LCAHFTAESELKlSELRSSLSQELPGYMI 5362
Cdd:cd05969   336 GRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPlRGEIIkafisLKEGFEPSDELK-EEIINFVRQKLGAHVA 414
                         490       500
                  ....*....|....*....|....*..
gi 386647928 5363 PSYFVQLEQLPLTANGKIDRKALPAPD 5389
Cdd:cd05969   415 PREIEFVDNLPKTRSGKIMRRVLKAKE 441
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
270-747 1.87e-40

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 160.23  E-value: 1.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERI 349
Cdd:cd05959    14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  350 RYMLEDSGTQVLLSQGHLQERVSFSG--------TWIRLDDEEAY-----------HEDGSNLESVNGPEHLTYVIYTSG 410
Cdd:cd05959    94 AYYLEDSRARVVVVSGELAPVLAAALtksehtlvVLIVSGGAGPEagalllaelvaAEAEQLKPAATHADDPAFWLYSSG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  411 TTGKPKGNLTTHRNiIRVVKNT---NYIDVTGQDKLLQLSSYSF-----DGSTFdifgALLNGAKLVLVPK----ETVLD 478
Cdd:cd05959   174 STGRPKGVVHLHAD-IYWTAELyarNVLGIREDDVCFSAAKLFFayglgNSLTF----PLSVGATTVLMPErptpAAVFK 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  479 vaklagLIEKQQISVMFITTAFFNVLVDmNPDC----LRHARAILFGGERVSvSHV----RKALGHlgpgKIKHVYGPTE 550
Cdd:cd05959   249 ------RIRRYRPTVFFGVPTLYAAMLA-APNLpsrdLSSLRLCVSAGEALP-AEVgerwKARFGL----DILDGIGSTE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  551 STVFATSYDVHEVEEGAVSIPIGGpisnTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFAdnpfapGE 630
Cdd:cd05959   317 MLHIFLSNRPGRVRYGTTGKPVPG----YEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  631 rMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYV-----ADRS 705
Cdd:cd05959   387 -WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSE 465
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928  706 LPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05959   466 ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
7446-7928 2.00e-40

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 159.98  E-value: 2.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7446 QTIHGLFEEQAERMPEKAAVVF--ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAY 7523
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7524 VPIDPEYPEDRIRYMLE-DSGAQVLLT--QRHLQECVSFDGKVIAADDEQAYGE---DGSNLE-PVVGPNHLAYVIYTSG 7596
Cdd:cd05923    81 ALINPRLKAAELAELIErGEMTAAVIAvdAQVMDAIFQSGVRVLALSDLVGLGEpesAGPLIEdPPREPEQPAFVFYTSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7597 TTGKPKGVMVEHHGLCSLKLMFAET--LRITEEDRVVQFASLSFDASCWEIF-KALFFGATLYIPAKDTILD-YPLFEsy 7672
Cdd:cd05923   161 TTGLPKGAVIPQRAAESRVLFMSTQagLRHGRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVVEEFDPADaLKLIE-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 mnENGITAAILPPTY------AIYLSPDRLPSLKKLITGGSA---ASVEFVQQWKdKVRYFNAYGPTEAsiVTSVWAASP 7743
Cdd:cd05923   239 --QERVTSLFATPTHldalaaAAEFAGLKLSSLRHVTFAGATmpdAVLERVNQHL-PGEKVNIYGTTEA--MNSLYMRDA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7744 dgldlRSVPIGRPIANHQIFIV---DSQNHMLPVGVAGELCISGAGLA--RGYLNRPELTAEKFVDnpflageRMYRTGD 7818
Cdd:cd05923   314 -----RTGTEMRPGFFSEVRIVrigGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRTGD 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7819 LARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRE-LTVSELRG-TL 7896
Cdd:cd05923   382 VGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGtLSADELDQfCR 461
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 7897 SQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05923   462 ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1300-1795 2.02e-40

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 159.98  E-value: 2.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1300 HALFEKQAERTPE-VAAVVYEND-RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPL 1377
Cdd:cd05923     4 FEMLRRAASRAPDaCAIADPARGlRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1378 DPDYPSDRIQFMLE-DSAASVLLTQTHL--QERAQQWGQTLQAVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTG 1454
Cdd:cd05923    84 NPRLKAAELAELIErGEMTAAVIAVDAQvmDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1455 RPKGVMIEHRS------LVNTAAGYR---REYRLDQFPvrLLQLASFsFDVFVGDIArtlynGGTMVICPKDDriDPARL 1525
Cdd:cd05923   164 LPKGAVIPQRAaesrvlFMSTQAGLRhgrHNVVLGLMP--LYHVIGF-FAVLVAALA-----LDGTYVVVEEF--DPADA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1526 HYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFgsQFRIINAYGVTEAAidSSLY 1605
Cdd:cd05923   234 LKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHL--PGEKVNIYGTTEAM--NSLY 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1606 DEPlaklPEAGNVpiGKAALNAKFYIVDAHLNPV---PVGVLGELCIGGIGVA--RGYLNRPELTEEKFVDspfvegeRL 1680
Cdd:cd05923   310 MRD----ARTGTE--MRPGFFSEVRIVRIGGSPDealANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GW 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1681 YRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAYFTAESELKLSEL 1759
Cdd:cd05923   377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSVTACVVPREGTLSADEL 456
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 1760 RS-SLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05923   457 DQfCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1294-1795 2.46e-40

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 159.42  E-value: 2.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1294 PENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGga 1373
Cdd:cd05920    12 WQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1374 yvpldpdypsdriqfmledsAASVLLTQTHLQERAQQWGQTLQAVLCLDDEAAYAEDASNVA-NVNEPH-DLAYVIYTSG 1451
Cdd:cd05920    90 --------------------AVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALArELAESIpEVALFLLSGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1452 TTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQL-ASFSFDVFVGDIARTLYNGGTMVICPkddriDPARLHYW-- 1528
Cdd:cd05920   150 TTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLpAAHNFPLACPGVLGTLLAGGRVVLAP-----DPSPDAAFpl 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1529 ISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDSSLYDEP 1608
Cdd:cd05920   225 IEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT--LQQVFGMAEGLLNYTRLDDP 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1609 LAKLPEAGNVPIGKaalNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLAR 1688
Cdd:cd05920   303 DEVIIHTQGRPMSP---DDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVR 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1689 WMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVlCAYFTA-ESELKLSELRSSLSQ- 1765
Cdd:cd05920   374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGERS-CAFVVLrDPPPSAAQLRRFLREr 452
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 1766 ELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05920   453 GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK06178 PRK06178
acyl-CoA synthetase; Validated
270-747 2.65e-40

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 161.36  E-value: 2.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERI 349
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  350 RYMLEDSGTQVLLSQGHLQ---ERVSfSGTWIR----------------------LDDEEAYHEDGSNL------ESVNG 398
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLApvvEQVR-AETSLRhvivtsladvlpaeptlplpdsLRAPRLAAAGAIDLlpalraCTAPV 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  399 PEHLTY------VIYTSGTTGKPKGNLTTHRNIIRVVKNTNYIDVTGQDKLLQLSSYS---FDGSTFDIFGALLNGAKLV 469
Cdd:PRK06178  202 PLPPPAldalaaLNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPefwIAGENFGLLFPLFSGATLV 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  470 LVPK---ETVLDvaklagLIEKQQISVMFITTAFFNVLVDmNPD-------CLRHARAilfggervsVSHVRKalghLGP 539
Cdd:PRK06178  282 LLARwdaVAFMA------AVERYRVTRTVMLVDNAVELMD-HPRfaeydlsSLRQVRV---------VSFVKK----LNP 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  540 GKIKHVYGPTESTVFATSYDVHEV-------------EEGAVSIPI--GGPISNTAIYIVNAQN-KLQPIGVAGELCVAG 603
Cdd:PRK06178  342 DYRQRWRALTGSVLAEAAWGMTEThtcdtftagfqddDFDLLSQPVfvGLPVPGTEFKICDFETgELLPLGAEGEIVVRT 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  604 DGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKAT 683
Cdd:PRK06178  422 PSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSA 494
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  684 VVVRESANGEKQLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVqLEQMPLTTNGKVDRRAL 747
Cdd:PRK06178  495 VVGRPDPDKGQVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
PRK06178 PRK06178
acyl-CoA synthetase; Validated
5945-6420 3.49e-40

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 160.98  E-value: 3.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHLLDRA---------------SFADKL---------VNLNDDGAYHEDGSNL------EPVNGP 6074
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAPVVeqvraetslrhvivtSLADVLpaeptlplpDSLRAPRLAAAGAIDLlpalraCTAPVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6075 EHLTY------VIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVELNEQTHilqtgaVVFDASTFEIWGALLNGGRLYVVRN 6148
Cdd:PRK06178  203 LPPPAldalaaLNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGED------SVFLSFLPEFWIAGENFGLLFPLFS 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6149 ETIL------DAVSLKNAIQQYGINTMWLTAPLYNQL------SQQDsgmFAGLKTLIVGGDVLSV-PHINRVLREHAGL 6215
Cdd:PRK06178  277 GATLvllarwDAVAFMAAVERYRVTRTVMLVDNAVELmdhprfAEYD---LSSLRQVRVVSFVKKLnPDYRQRWRALTGS 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6216 SIVNG-YGPTENTTfSTTHTiVGEQK-------EAVPIGKPINNSTAYIVDSKL-SLLPVGVWGELIVGGDGVARGYLNR 6286
Cdd:PRK06178  354 VLAEAaWGMTETHT-CDTFT-AGFQDddfdllsQPVFVGLPVPGTEFKICDFETgELLPLGAEGEIVVRTPSLLKGYWNK 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6287 PELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDEsGQ 6366
Cdd:PRK06178  432 PEATAEALRDGWL-------HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDP-DK 503
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 6367 KQLCAYFV---AERELTIGELRAALSQELPNYMIPSHFVpLERMPLTPNGKIDRRAL 6420
Cdd:PRK06178  504 GQVPVAFVqlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
2371-2828 3.56e-40

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 157.50  E-value: 3.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLaqr 2450
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2451 rlqervsfagtvvtvddeqayagdgsnlesaVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVV 2530
Cdd:cd05972    78 -------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2531 QFASLSFDASCW-EVFQTLFFGATLYIPTKETILDYQWFERyMSDNGITTATLPPT-YAVYLNPD-HMPDFKRL---IAA 2604
Cdd:cd05972   127 NIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAERILEL-LERYGVTSFCGPPTaYRMLIKQDlSSYKFSHLrlvVSA 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2605 GSASSLELLQQWKDK--VKYFNAYGPTEdsicTTIWTPSTEDIsQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCI 2682
Cdd:cd05972   206 GEPLNPEVIEWWRAAtgLPIRDGYGQTE----TGLTVGNFPDM-PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAI 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2683 --AGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASV 2760
Cdd:cd05972   281 klPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAV 353
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2761 QEAIVIAH-DDASGQ--KqlcAYFV------ADRTMtVGELRGELSGELPGYMIP--AHFVqlERMPLTPNGKIDRKAL 2828
Cdd:cd05972   354 AEAAVVGSpDPVRGEvvK---AFVVltsgyePSEEL-AEELQGHVKKVLAPYKYPreIEFV--EELPKTISGKIRRVEL 426
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
4907-5385 7.76e-40

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 156.85  E-value: 7.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4907 VYENDR-LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAA 4985
Cdd:cd05919     4 FYAADRsVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4986 SVLltqthlqeraqqwgqtlqaalclddeaaYAEDAsnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR 5065
Cdd:cd05919    84 RLV----------------------------VTSAD----------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5066 EYRLDQFPVRLLQLASFSFDVFVGD-IARTLYNGGTMVICPkdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEH 5144
Cdd:cd05919   126 EALGLTPGDRVFSSAKMFFGYGLGNsLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5145 GLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAidsSLYdepLAKLPeaGNVPIGKAALNAKFY---I 5221
Cdd:cd05919   204 PDALRSLRLCVSAGEALPRGLGERWMEHFGGP--ILDGIGATEVG---HIF---LSNRP--GAWRLGSTGRPVPGYeirL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5222 VDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYR 5301
Cdd:cd05919   274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5302 IETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSE-----LRSSLSQELPGYMIPSYFVQLEQLPLTA 5376
Cdd:cd05919   347 VSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslardIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                  ....*....
gi 386647928 5377 NGKIDRKAL 5385
Cdd:cd05919   427 TGKLQRFKL 435
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
251-698 1.16e-39

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 159.88  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  251 KTGTDYPRDTTIHRLFEEQAERRPDAVAVTFED----RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVG 326
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  327 IMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLL--SQGHLQ------ERVSFSGTWIRLDDEEAYH----------- 387
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDkllevrDELPSLRHIVVLDPRGLRDdprllsldell 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  388 EDGSNLESVN---------GPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN-YIDVTGQDKLLqlsSY-----SFD 452
Cdd:COG1022   162 ALGREVADPAelearraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLeRLPLGPGDRTL---SFlplahVFE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  453 gSTFDIFgALLNGAKLVLVPK-ETVLDVAKLAG---------LIEKQQISVM-------FITTAFFNVLVDMnpdCLRHA 515
Cdd:COG1022   239 -RTVSYY-ALAAGATVAFAESpDTLAEDLREVKptfmlavprVWEKVYAGIQakaeeagGLKRKLFRWALAV---GRRYA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  516 RAILfGGERVSV--------------SHVRKALGH-----------LGP---------G-KIKHVYGPTESTVFATSYDV 560
Cdd:COG1022   314 RARL-AGKSPSLllrlkhaladklvfSKLREALGGrlrfavsggaaLGPelarffralGiPVLEGYGLTETSPVITVNRP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  561 HEVEEGAVsipiGGPISNTAIYIvnAQNklqpigvaGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLAR 640
Cdd:COG1022   393 GDNRIGTV----GPPLPGVEVKI--AED--------GEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGE 452
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928  641 WLPDGTIEYVGRIDDQVKIR-GFRIELGEIEAHLLKLEAIEKATVVvresANGEKQLCA 698
Cdd:COG1022   453 LDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV----GDGRPFLAA 507
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
7456-7923 1.17e-39

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 158.97  E-value: 1.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDR 7534
Cdd:PRK08314   20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7535 IRYMLEDSGAQVLLT-QRHLQECVSFDGK-----VIAA------DDE---------------QAYGEDG---------SN 7578
Cdd:PRK08314  100 LAHYVTDSGARVAIVgSELAPKVAPAVGNlrlrhVIVAqysdylPAEpeiavpawlraepplQALAPGGvvawkealaAG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7579 LEP---VVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASL--------SFDAscweifk 7647
Cdd:PRK08314  180 LAPpphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLfhvtgmvhSMNA------- 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7648 ALFFGATLYIPA---KDTILDypLFESYmnenGITAAILPPTYAIYL--SPD----RLPSLkKLITGGSAASVEFV-QQW 7717
Cdd:PRK08314  253 PIYAGATVVLMPrwdREAAAR--LIERY----RVTHWTNIPTMVVDFlaSPGlaerDLSSL-RYIGGGGAAMPEAVaERL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7718 KDK--VRYFNAYGPTEasivtsvwAASPDGLDLRSVP----IGRPIANHQIFIVDSQN-HMLPVGVAGELCISGAGLARG 7790
Cdd:PRK08314  326 KELtgLDYVEGYGLTE--------TMAQTHSNPPDRPklqcLGIPTFGVDARVIDPETlEELPPGEVGEIVVHGPQVFKG 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7791 YLNRPELTAEKFVDnpfLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGD 7870
Cdd:PRK08314  398 YWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPD 474
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7871 ANGQQQLCAYFVADreltvSELRGTLSQE---------LPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:PRK08314  475 PRRGETVKAVVVLR-----PEARGKTTEEeiiawarehMAAYKYPRIVEFVDSLPKSGSGKI 531
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
4901-5385 1.61e-39

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 157.29  E-value: 1.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:cd05923    17 ACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 E-DSAASVLLTQTHL--QERAQQWGQTLQAALCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRS-- 5055
Cdd:cd05923    97 ErGEMTAAVIAVDAQvmDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAae 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5056 ----LVNTAAGYR---REYRLDQFPvrLLQLASFsFDVFVGDIArtlynGGTMVICPKDDriDPARLHYWISEEKITIFE 5128
Cdd:cd05923   177 srvlFMSTQAGLRhgrHNVVLGLMP--LYHVIGF-FAVLVAALA-----LDGTYVVVEEF--DPADALKLIEQERVTSLF 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5129 STPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFgsQFRIINAYGVTEAAidSSLYDEPlaklPEAGNV 5208
Cdd:cd05923   247 ATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHL--PGEKVNIYGTTEAM--NSLYMRD----ARTGTE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5209 piGKAALNAKFYIVDAHLNPV---PVGVLGELCIGGIGVA--RGYLNRPELTEEKFVDspfvegeRLYRTGDLARWMPDG 5283
Cdd:cd05923   319 --MRPGFFSEVRIVRIGGSPDealANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRTGDVGYVDPSG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5284 NVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAHFTAESELKLSELRS-SLSQELPGYM 5361
Cdd:cd05923   390 DVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSVTACVVPREGTLSADELDQfCRASELADFK 469
                         490       500
                  ....*....|....*....|....
gi 386647928 5362 IPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05923   470 RPRRYFFLDELPKNAMNKVLRRQL 493
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
7472-7928 1.66e-39

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 155.20  E-value: 1.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVlltqr 7551
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 hlqecvsfdgkviaaDDeqaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMV---EH--HGLCSlklmfAETLRITE 7626
Cdd:cd05912    77 ---------------DD-------------------IATIMYTSGTTGKPKGVQQtfgNHwwSAIGS-----ALNLGLTE 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7627 EDR------VVQFASLSFdascweIFKALFFGATLYIPAKdtiLDYPLFESYMNENGIT------------AAILPPTYA 7688
Cdd:cd05912   118 DDNwlcalpLFHISGLSI------LMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTiisvvptmlqrlLEILGEGYP 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7689 iylspdrlPSLKKLITGGSAASVEFVQQWKDK-VRYFNAYGPTEAS--IVTsvwaASPDGLDLRSVPIGRPIANHQIFIV 7765
Cdd:cd05912   189 --------NNLRCILLGGGPAPKPLLEQCKEKgIPVYQSYGMTETCsqIVT----LSPEDALNKIGSAGKPLFPVELKIE 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7766 DSQNhmlPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRI 7845
Cdd:cd05912   257 DDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENI 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7846 ELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd05912   327 YPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406

                  ...
gi 386647928 7926 NAL 7928
Cdd:cd05912   407 HEL 409
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
6996-7413 2.02e-39

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 155.50  E-value: 2.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6996 QKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSgPRGEPLQIVyrdkrigfVYEDLSHL 7075
Cdd:cd19538     8 QRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPE-EDGVPYQLI--------LEEDEATP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7076 PADERQASVERLEQ---EDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDRP 7152
Cdd:cd19538    79 KLEIKEVDEEELESeinEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7153 EQKAAPA-YSQYIEW-------LENQDSAAAS--AYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMN 7222
Cdd:cd19538   159 ELAPLPVqYADYALWqqellgdESDPDSLIARqlAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7223 RAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEipGIEEMIGLFINTIPVRVACQPEESFADVMGRMQEA 7302
Cdd:cd19538   239 QLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKET 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7303 ALESgrYD-----FYPLYEI--QTQSAQKQELINHLLVFENYPmDEQVEQAGGDdsGTLSITDVDVAEHT-NYNFTVTVF 7374
Cdd:cd19538   317 NLEA--YEhqdipFERLVEAlnPTRSRSRHPLFQIMLALQNTP-QPSLDLPGLE--AKLELRTVGSAKFDlTFELREQYN 391
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 386647928 7375 PGDE--IVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19538   392 DGTPngIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
5931-6420 2.03e-39

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 157.99  E-value: 2.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5931 YPSDKTIHQLFEEQAERIPDHLAVTfeDKQ---LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILK 6007
Cdd:PRK06087   19 YWGDASLADYWQQTARAMPDKIAVV--DNHgasYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6008 AGGAYVPIDPDYPEDRIRYMLEDSGAKLLLV------------------QGHLLDRASFADKLVNLNDDGAYHEDGSNLE 6069
Cdd:PRK06087   97 VGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkqtrpvdlilplqnQLPQLQQIVGVDKLAPATSSLSLSQIIADYE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6070 PVNGP-----EHLTYVIYTSGTTGRPKGVMVEHRNVvrLVKNTNYV---ELNEQTHILQTgAVVFDASTF--EIWGALLN 6139
Cdd:PRK06087  177 PLTTAitthgDELAAVLFTSGTEGLPKGVMLTHNNI--LASERAYCarlNLTWQDVFMMP-APLGHATGFlhGVTAPFLI 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6140 GGRLYVVRNETILDAVSLKNaiQQYGINTMWLTAPLYNQLS--QQDSGMFAGLKTLIVGGDVlsVPhiNRVLRE--HAGL 6215
Cdd:PRK06087  254 GARSVLLDIFTPDACLALLE--QQRCTCMLGATPFIYDLLNllEKQPADLSALRFFLCGGTT--IP--KKVAREcqQRGI 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6216 SIVNGYGPTEnttfSTTHTIVgeqkeavPIGKPIN-----NSTAY------IVDSKLSLLPVGVWGELIVGGDGVARGYL 6284
Cdd:PRK06087  328 KLLSVYGSTE----SSPHAVV-------NLDDPLSrfmhtDGYAAagveikVVDEARKTLPPGCEGEEASRGPNVFMGYL 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6285 NRPELTAEKfvessfLPGERCYRTGDLARWLPDGTLEYKGRIDEqVKIRG-YRIELGEIEEQLLKVASVKEATVIVREDE 6363
Cdd:PRK06087  397 DEPELTARA------LDEEGWYYSGDLCRMDEAGYIKITGRKKD-IIVRGgENISSREVEDILLQHPKIHDACVVAMPDE 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 6364 SGQKQLCAYFV---AERELTIGELRAALS-QELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK06087  470 RLGERSCAYVVlkaPHHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
2370-2828 2.45e-39

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 157.41  E-value: 2.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2370 QLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQ 2449
Cdd:cd12119    25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2450 RRLQERV-SFAGTVVTVDDEQAYAGDGSNLESAvGPNDLAY-----------------------IIYTSGTTGKPKGVMV 2505
Cdd:cd12119   105 RDFLPLLeAIAPRLPTVEHVVVMTDDAAMPEPA-GVGVLAYeellaaespeydwpdfdentaaaICYTSGTTGNPKGVVY 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2506 EH-----HGLCSLKqmfANTLQINAQDRVVQFASLsFDASCWEV-FQTLFFGATLYIPTKEtiLDYQWFERYMSDNGITT 2579
Cdd:cd12119   184 SHrslvlHAMAALL---TDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLPGPY--LDPASLAELIEREGVTF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2580 ATLPPT----YAVYL--NPDHMPDFKRLIAAGSASSLELLQQWKDK-VKYFNAYGPTEDS-ICTTIWTPS-------TED 2644
Cdd:cd12119   258 AAGVPTvwqgLLDHLeaNGRDLSSLRRVVIGGSAVPRSLIEAFEERgVRVIHAWGMTETSpLGTVARPPSehsnlseDEQ 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2645 ISQLKSvpIGGPIVNHRIYIVDAHYQPVPV-GVA-GELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermyRTGDLAKW 2722
Cdd:cd12119   338 LALRAK--QGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RTGDVATI 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2723 LPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVA--DRTMTVGELRGELSGEL 2800
Cdd:cd12119   409 DEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLkeGATVTAEELLEFLADKV 488
                         490       500
                  ....*....|....*....|....*...
gi 386647928 2801 PGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd12119   489 AKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK07798 PRK07798
acyl-CoA synthetase; Validated
261-745 3.45e-39

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 156.97  E-value: 3.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPI 340
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  341 DPEYPEERIRYMLEDSGTQVLLSQGHLQERV-----SFSG--TWIRLDDE--EAYHEDGSNLESV---NGPEHL------ 402
Cdd:PRK07798   84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVaevlpRLPKlrTLVVVEDGsgNDLLPGAVDYEDAlaaGSPERDfgersp 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  403 --TYVIYTSGTTGKPKGNLTTHRNIIRV----VKNTNYIDVTGQDKLLQLSSYSFDGSTFDI------------FGALLN 464
Cdd:PRK07798  164 ddLYLLYTGGTTGMPKGVMWRQEDIFRVllggRDFATGEPIEDEEELAKRAAAGPGMRRFPApplmhgagqwaaFAALFS 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  465 GAKLVLVPKETvLDVAKLAGLIEKQQISVMFIT-TAFFNVLVdmnpDCLRHAR--------AILFGGERVSVSHVRKALG 535
Cdd:PRK07798  244 GQTVVLLPDVR-FDADEVWRTIEREKVNVITIVgDAMARPLL----DALEARGpydlsslfAIASGGALFSPSVKEALLE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  536 HLGPGKIKHVYGPTESTVFATSYdvheVEEGAVSipiggpisnTAIYIVNAQNKLQPIGVAGELCVAGDG----LAR--- 608
Cdd:PRK07798  319 LLPNVVLTDSIGSSETGFGGSGT----VAKGAVH---------TGGPRFTIGPRTVVLDEDGNPVEPGSGeigwIARrgh 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  609 ---GYLNRPDLTAEKFadnPFAPGERMYRTGDLARWLPDGTIEYVGRidDQVKIR--GFRIELGEIEAHLLKLEAIEKAT 683
Cdd:PRK07798  386 iplGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADAL 460
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  684 VVVRESangEK--QLCAYYVADR---SLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRR 745
Cdd:PRK07798  461 VVGVPD---ERwgQEVVAVVQLRegaRPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
4884-5385 3.79e-39

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 155.95  E-value: 3.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4884 PENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGA 4963
Cdd:cd05920    12 WQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4964 YVPLDPDYPSDRIqfmledsaasvlltqTHLQERAQQwgqtlqAALCLDDEAA---YAEDASNVANvnEPHDLAYVIYTS 5040
Cdd:cd05920    92 PVLALPSHRRSEL---------------SAFCAHAEA------VAYIVPDRHAgfdHRALARELAE--SIPEVALFLLSG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5041 GTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQL-ASFSFDVFVGDIARTLYNGGTMVICPkddriDPARLHYW- 5118
Cdd:cd05920   149 GTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLpAAHNFPLACPGVLGTLLAGGRVVLAP-----DPSPDAAFp 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5119 -ISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDSSLYDE 5197
Cdd:cd05920   224 lIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT--LQQVFGMAEGLLNYTRLDD 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5198 PLAKLPEAGNVPIGKaalNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLA 5277
Cdd:cd05920   302 PDEVIIHTQGRPMSP---DDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLV 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5278 RWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVlCAHFTA-ESELKLSELRSSLSQ 5355
Cdd:cd05920   373 RRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGERS-CAFVVLrDPPPSAAQLRRFLRE 451
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 5356 -ELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05920   452 rGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
3863-4337 6.05e-39

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 155.12  E-value: 6.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3863 QALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDR 3942
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3943 IRYMLEDSGAQALLTQRHLRERVsFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMvehhglcsl 4022
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKL-IPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI--------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4023 kLMFAN----------TLQMTEQDR---VVQFaslsFDASCWEI-FKALFFGATLYIptsttildYPLFES-----YMNE 4083
Cdd:PRK03640  161 -QTYGNhwwsavgsalNLGLTEDDCwlaAVPI----FHISGLSIlMRSVIYGMRVVL--------VEKFDAekinkLLQT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4084 NGIT-----ATILPPTYAAYLNPDRMPSLKKLITGGSAASVEFVQQWKDKVL-YFNAYGPTE-AS-IVTSIWDEASDSLG 4155
Cdd:PRK03640  228 GGVTiisvvSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIpVYQSYGMTEtASqIVTLSPEDALTKLG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4156 drkSVpiGRPLANHRIYVVDsHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermyRTGDLVRWLPDG 4235
Cdd:PRK03640  308 ---SA--GKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEG 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4236 NLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIP 4315
Cdd:PRK03640  375 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVP 454
                         490       500
                  ....*....|....*....|..
gi 386647928 4316 SYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK03640  455 KRFYFVEELPRNASGKLLRHEL 476
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
5954-6417 6.34e-39

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 154.91  E-value: 6.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5954 VTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGA 6033
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6034 KLLLVqghlldrasfadklvnlnddgayhedgSNlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVELN 6113
Cdd:cd05914    81 KAIFV---------------------------SD------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6114 EQT----------HI----------LQTGA-VVF---------DASTFEIWGALLNGGRLYVVRNETILDAVSLKN-AIQ 6162
Cdd:cd05914   128 GKGdkilsilplhHIypltftlllpLLNGAhVVFldkipsakiIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTlKKF 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6163 QYGINTMWLTAPLYNQLSQQDSGMFAG-LKTLIVGGDVLSvPHINRVLREhAGLSIVNGYGPTENT---TFSTTHTIVGE 6238
Cdd:cd05914   208 KFKLAKKINNRKIRKLAFKKVHEAFGGnIKEFVIGGAKIN-PDVEEFLRT-IGFPYTIGYGMTETApiiSYSPPNRIRLG 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6239 QkeavpIGKPINNSTAYIVDSKlsllPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDG 6318
Cdd:cd05914   286 S-----AGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWF------HTGDLGKIDAEG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6319 TLEYKGRIDEQ-VKIRGYRIELGEIEEQLLKVASVKEATVIVREDESgqkQLCAYFVAERELTIG------------ELR 6385
Cdd:cd05914   351 YLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL---VALAYIDPDFLDVKAlkqrniidaikwEVR 427
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 6386 AALSQELPNYM----IPSHFVPLERmplTPNGKIDR 6417
Cdd:cd05914   428 DKVNQKVPNYKkiskVKIVKEEFEK---TPKGKIKR 460
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
5961-6420 8.10e-39

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 153.27  E-value: 8.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLllvqg 6040
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 hlldrasfadklvnlnddgayhedgsnlepvngpEHLTYVIYTSGTTGRPKGVMVEHRN----VVRLVKNtnyVELNEQT 6116
Cdd:cd05912    77 ----------------------------------DDIATIMYTSGTTGKPKGVQQTFGNhwwsAIGSALN---LGLTEDD 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6117 HILqtgAVVfdaSTFEIWG------ALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMF-AG 6189
Cdd:cd05912   120 NWL---CAL---PLFHISGlsilmrSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYpNN 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6190 LKTLIVGGDVLSVPHINRVLREhaGLSIVNGYGPTEntTFSTTHTIVGEQKEAVP--IGKPINNSTAYIVDSklSLLPVG 6267
Cdd:cd05912   191 LRCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTE--TCSQIVTLSPEDALNKIgsAGKPLFPVELKIEDD--GQPPYE 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6268 VwGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLL 6347
Cdd:cd05912   265 V-GEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 6348 KVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05912   337 SHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
7455-7928 9.83e-39

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 154.73  E-value: 9.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7455 QAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDR 7534
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7535 IRYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVvgpnHL---AYVIYTSGTTGKPKGVMVEHHGL 7611
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEF----DLdevATIMYTSGTTGKPKGVIQTYGNH 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7612 CSLKLMFAETLRITEEDrvvqfaslsfdasCWEIFKALFFGATLYIPAKDTILDYP--LFESYmNENGITAAILPPTYAI 7689
Cdd:PRK03640  167 WWSAVGSALNLGLTEDD-------------CWLAAVPIFHISGLSILMRSVIYGMRvvLVEKF-DAEKINKLLQTGGVTI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7690 Y-------------LSPDRLP-SLKKLITGGSAASVEFVQQWKDK-VRYFNAYGPTE-AS-IVTsvwAASPDGLD-LRSV 7751
Cdd:PRK03640  233 IsvvstmlqrllerLGEGTYPsSFRCMLLGGGPAPKPLLEQCKEKgIPVYQSYGMTEtASqIVT---LSPEDALTkLGSA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7752 piGRPIANHQIFIVDsQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWLPDGNIEYL 7831
Cdd:PRK03640  310 --GKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7832 GRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQ 7911
Cdd:PRK03640  380 DRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYF 459
                         490
                  ....*....|....*..
gi 386647928 7912 LEQMPLTPNGKIDRNAL 7928
Cdd:PRK03640  460 VEELPRNASGKLLRHEL 476
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1322-1795 1.11e-38

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 153.36  E-value: 1.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTq 1401
Cdd:cd05971     6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 thlqeraqqwgqtlqavlclddeaayaeDASNvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYrrEYRLDQ 1481
Cdd:cd05971    85 ----------------------------DGSD--------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGV--QFPFNL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 FPVR---LLQLASFS-----FDVFVGdiarTLYNGGTMVICpKDDRIDPARLHYWISEEKIT-IFESTPALIIpfmdyVA 1552
Cdd:cd05971   127 FPRDgdlYWTPADWAwigglLDVLLP----SLYFGVPVLAH-RMTKFDPKAALDLMSRYGVTtAFLPPTALKM-----MR 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1553 EHGLDMS----SMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEA--AIDSSlydeplAKLPEAGNVPIGKAALN 1626
Cdd:cd05971   197 QQGEQLKhaqvKLRAIATGGESLGEELLGWAREQFGVE--VNEFYGQTECnlVIGNC------SALFPIKPGSMGKPIPG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1627 AKFYIVDAHLNPVPVGVLGELCIG-GIGVAR-GYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQ 1704
Cdd:cd05971   269 HRVAIVDDNGTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDV 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1705 AKIRGYRIETGEIETQLLKAEGVREAVVVVREDA------KGQKVLCAYFTAESELKlSELRSSLSQELPGYMIPSYFVQ 1778
Cdd:cd05971   342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPirgeivKAFVVLNPGETPSDALA-REIQELVKTRLAAHEYPREIEF 420
                         490
                  ....*....|....*..
gi 386647928 1779 LEQLPLTANGKIDRKAL 1795
Cdd:cd05971   421 VNELPRTATGKIRRREL 437
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
4885-5385 1.84e-38

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 154.92  E-value: 1.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4885 ENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPnqlvgilADR-------SADLLVGALAV 4957
Cdd:COG1021    23 RGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRP-------GDRvvvqlpnVAEFVIVFFAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4958 WKAGGAYVPLdpdYPSDR---IQFMLEDSAASVLLTQTH--------LQERAQQWGQTLQAALCLDD-------EAAYAE 5019
Cdd:COG1021    96 FRAGAIPVFA---LPAHRraeISHFAEQSEAVAYIIPDRhrgfdyraLARELQAEVPSLRHVLVVGDageftslDALLAA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5020 DASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQL-----ASFSFDVFVGdiarT 5094
Cdd:COG1021   173 PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALpaahnFPLSSPGVLG----V 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5095 LYNGGTMVICPkddRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFG 5174
Cdd:COG1021   249 LYAGGTVVLAP---DPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5175 SQfrIINAYGVTEAAI------DS------------SLYDEPLaklpeagnvpigkaalnakfyIVDAHLNPVPVGVLGE 5236
Cdd:COG1021   326 CT--LQQVFGMAEGLVnytrldDPeevilttqgrpiSPDDEVR---------------------IVDEDGNPVPPGEVGE 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5237 LCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRIDNQAkIR-GYRIETGEIETQLLKAE 5315
Cdd:COG1021   383 LLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHP 455
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 5316 GVREAVVVVREDAK-GQKVlCAHFTA-ESELKLSELRSSL-SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:COG1021   456 AVHDAAVVAMPDEYlGERS-CAFVVPrGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
7472-7932 1.90e-38

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 152.66  E-value: 1.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQR 7551
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 HLQECVSfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVV 7631
Cdd:cd05969    81 ELYERTD--------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7632 QFASLSFDA-SCWEIFKALFFGATLYIPAKDtiLDYPLFESYMNENGITAAILPPT-------YAIYLSPD-RLPSLKKL 7702
Cdd:cd05969   135 CTADPGWVTgTVYGIWAPWLNGVTNVVYEGR--FDAESWYGIIERVKVTVWYTAPTairmlmkEGDELARKyDLSSLRFI 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7703 ITGGSAASVEFVQqWKDKV---RYFNAYGPTE-ASIVTsvwaASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAG 7778
Cdd:cd05969   213 HSVGEPLNPEAIR-WGMEVfgvPIHDTWWQTEtGSIMI----ANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKG 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7779 ELCISGA--GLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLK 7856
Cdd:cd05969   288 ILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALME 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7857 IASVQETIVIARGDANGQQQLCAY------FVADRELTVsELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPA 7930
Cdd:cd05969   361 HPAVAEAGVIGKPDPLRGEIIKAFislkegFEPSDELKE-EIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKA 439

                  ..
gi 386647928 7931 PE 7932
Cdd:cd05969   440 KE 441
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4912-5385 2.03e-38

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 152.59  E-value: 2.03e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTq 4991
Cdd:cd05971     6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 thlqeraqqwgqtlqaalclddeaayaeDASNvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYrrEYRLDQ 5071
Cdd:cd05971    85 ----------------------------DGSD--------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGV--QFPFNL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5072 FPVR---LLQLASFS-----FDVFVGdiarTLYNGGTMVICpKDDRIDPARLHYWISEEKIT-IFESTPALIIpfmdyVA 5142
Cdd:cd05971   127 FPRDgdlYWTPADWAwigglLDVLLP----SLYFGVPVLAH-RMTKFDPKAALDLMSRYGVTtAFLPPTALKM-----MR 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5143 EHGLDMS----SMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEA--AIDSSlydeplAKLPEAGNVPIGKAALN 5216
Cdd:cd05971   197 QQGEQLKhaqvKLRAIATGGESLGEELLGWAREQFGVE--VNEFYGQTECnlVIGNC------SALFPIKPGSMGKPIPG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5217 AKFYIVDAHLNPVPVGVLGELCIG-GIGVAR-GYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQ 5294
Cdd:cd05971   269 HRVAIVDDNGTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDV 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5295 AKIRGYRIETGEIETQLLKAEGVREAVVVVREDA------KGQKVLCAHFTAESELKlSELRSSLSQELPGYMIPSYFVQ 5368
Cdd:cd05971   342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPirgeivKAFVVLNPGETPSDALA-REIQELVKTRLAAHEYPREIEF 420
                         490
                  ....*....|....*..
gi 386647928 5369 LEQLPLTANGKIDRKAL 5385
Cdd:cd05971   421 VNELPRTATGKIRRREL 437
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
3853-4337 2.51e-38

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 154.92  E-value: 2.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3853 EQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYI 3932
Cdd:PRK06155   20 ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3933 PIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFV-------AVDDEQAYHAD-GSNLEPV-----------VGP 3993
Cdd:PRK06155  100 PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDlplpavwLLDAPASVSVPaGWSTAPLppldapapaaaVQP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3994 NHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIptsTTILD 4073
Cdd:PRK06155  180 GDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL---EPRFS 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4074 YPLFESYMNENGITATIL-----------PPTYAaylnpDRMPSLKKLITGGSAAsvEFVQQWKDK--VLYFNAYGPTEA 4140
Cdd:PRK06155  257 ASGFWPAVRRHGATVTYLlgamvsillsqPARES-----DRAHRVRVALGPGVPA--ALHAAFRERfgVDLLDGYGSTET 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4141 SIVTsiwdeaSDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISG---VGLARGYLNRPELTAEKFVDNPFE 4217
Cdd:PRK06155  330 NFVI------AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVEAWRNLWFH 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4218 PGERMYRTgdlvrwlPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQlVAYFVAQRELT 4297
Cdd:PRK06155  404 TGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDE-VMAAVVLRDGT 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 386647928 4298 AAELRATMSQ---ELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK06155  476 ALEPVALVRHcepRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
5942-6420 2.81e-38

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 153.48  E-value: 2.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5942 EEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYP 6020
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6021 EDRIRYMLEDSGAKLLLVQGH------LLDRASFADKLVNLND-DGAYHEDGSNLEPVNGPEHLTyVIYTSGTTGRPKGV 6093
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTfqnmalSMQKVSYVQRVISITSlKEIEDRKIDNFVEKNESASFI-ICYTSGTTGKPKGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6094 MVEHRNVV-RLVKNTNYVELNEQT---------HILQTGAVVFDastfeiwgALLNGGRLYVVRNETILDAVSLknaIQQ 6163
Cdd:PRK06839  168 VLTQENMFwNALNNTFAIDLTMHDrsivllplfHIGGIGLFAFP--------TLFAGGVIIVPRKFEPTKALSM---IEK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6164 YGInTMWLTAPLYNQLSQQDSGM----FAGLKTLIVGGDVLSVPHInRVLREHaGLSIVNGYGPTEntTFSTTHTIVGE- 6238
Cdd:PRK06839  237 HKV-TVVMGVPTIHQALINCSKFettnLQSVRWFYNGGAPCPEELM-REFIDR-GFLFGQGFGMTE--TSPTVFMLSEEd 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6239 -QKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPD 6317
Cdd:PRK06839  312 aRRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDED 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6318 GTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERE--LTIGELRAALSQELPNY 6395
Cdd:PRK06839  385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSsvLIEKDVIEHCRLFLAKY 464
                         490       500
                  ....*....|....*....|....*
gi 386647928 6396 MIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK06839  465 KIPKEIVFLKELPKNATGKIQKAQL 489
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
3879-4337 3.01e-38

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 151.86  E-value: 3.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3879 QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTq 3958
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3959 rhlrervsfagtfvavddeqayhadGSNLEpvvgpnHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRV 4038
Cdd:cd05935    80 -------------------------GSELD------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4039 VQ----FASLSFDAScweIFKALFFGATLYIPT---STTILDypLFESYmneNGITATILPPTYAAYLNPDR-----MPS 4106
Cdd:cd05935   129 LAclplFHVTGFVGS---LNTAVYVGGTYVLMArwdRETALE--LIEKY---KVTFWTNIPTMLVDLLATPEfktrdLSS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4107 LKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTSiwdeaSDSLGDRKSVPIGRPLANHRIYVVD-SHNRMLPV 4183
Cdd:cd05935   201 LKVLTGGGAPMPPAVAEKLLKLtgLRFVEGYGLTETMSQTH-----TNPPLRPKLQCLGIP*FGVDARVIDiETGRELPP 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4184 GVAGELCISGVGLARGYLNRPELTAEKFVDnpfEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQL 4263
Cdd:cd05935   276 NEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 4264 AKIDAVQEAIVLAREDANGQQQLVAYFVAQREL----TAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05935   353 YKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgkvTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
5944-6420 3.36e-38

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 153.19  E-value: 3.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5944 QAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDR 6023
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6024 IRYMLEDSGAKLLLVQGHLLDRaSFADKLVNLNDDGAyhEDGSNLEPVNgPEHLTYV---IYTSGTTGRPKGVMVEHRN- 6099
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAK-LIPGISVKFAELMN--GPKEEAEIQE-EFDLDEVatiMYTSGTTGKPKGVIQTYGNh 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6100 ---VVRLVKNtnyVELNEQTHILqtgAVV--FDASTFEI-WGALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTMWLTA 6173
Cdd:PRK03640  167 wwsAVGSALN---LGLTEDDCWL---AAVpiFHISGLSIlMRSVIYGMRVVLVEK---FDAEKINKLLQTGGVTIISVVS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6174 PLYNQLSQQ--DSGMFAGLKTLIVGGDvlsvPhINRVLREHA---GLSIVNGYGPTEnttfsTTHTIVG-EQKEAV---- 6243
Cdd:PRK03640  238 TMLQRLLERlgEGTYPSSFRCMLLGGG----P-APKPLLEQCkekGIPVYQSYGMTE-----TASQIVTlSPEDALtklg 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6244 PIGKPINNSTAYIVDSkLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYK 6323
Cdd:PRK03640  308 SAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6324 GRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVP 6403
Cdd:PRK03640  380 DRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYF 459
                         490
                  ....*....|....*..
gi 386647928 6404 LERMPLTPNGKIDRRAL 6420
Cdd:PRK03640  460 VEELPRNASGKLLRHEL 476
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
3849-4335 3.73e-38

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 154.77  E-value: 3.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3849 EYQQEqTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAG 3928
Cdd:PRK05605   28 DYGDT-TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3929 GAYIPIDPEYPEDRIRYMLEDSGA-------QALLTQRHLRERVSfAGTFVAVD------------------------DE 3977
Cdd:PRK05605  107 AVVVEHNPLYTAHELEHPFEDHGArvaivwdKVAPTVERLRRTTP-LETIVSVNmiaampllqrlalrlpipalrkarAA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3978 QAYHADG----SNL-------------EPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLcslklmFANTLQ-------MT 4033
Cdd:PRK05605  186 LTGPAPGtvpwETLvdaaiggdgsdvsHPRPTPDDVALILYTSGTTGKPKGAQLTHRNL------FANAAQgkawvpgLG 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4034 EQDRVVqFASLSfdascweIFKAlfFGATLYIPTSTTI---------LDYPLFESYMNENgiTATILP---PTY------ 4095
Cdd:PRK05605  260 DGPERV-LAALP-------MFHA--YGLTLCLTLAVSIggelvllpaPDIDLILDAMKKH--PPTWLPgvpPLYekiaea 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4096 AAYLNPDrMPSLKKLITGGSAASVEFVQQWKDKV--LYFNAYGPTEASIVTsiwdeASDSLGD-RKSVPIGRPLANHRIY 4172
Cdd:PRK05605  328 AEERGVD-LSGVRNAFSGAMALPVSTVELWEKLTggLLVEGYGLTETSPII-----VGNPMSDdRRPGYVGVPFPDTEVR 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4173 VVDSHN--RMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIR 4250
Cdd:PRK05605  402 IVDPEDpdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITG 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4251 GYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTP 4328
Cdd:PRK05605  475 GFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEpgAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQ 554

                  ....*..
gi 386647928 4329 NGKIDRK 4335
Cdd:PRK05605  555 LGKVRRR 561
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
268-747 4.38e-38

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 153.98  E-value: 4.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  268 EQAERRPDAVAVTFEDRQ-----LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGG--AYVPI 340
Cdd:cd05906    17 LRAAERGPTKGITYIDADgseefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFvpAPLTV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  341 DPEYPE--------ERIRYMLEDSgtQVLLSQGHLQERVSFSGTWIRLDDEEAYHEDGSNLES-----VNGPEHLTYVIY 407
Cdd:cd05906    97 PPTYDEpnarlrklRHIWQLLGSP--VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAAdhdlpQSRPDDLALLML 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  408 TSGTTGKPKGNLTTHRNII-RVV-KNTNYiDVTGQDklLQLSSYSFD---GSTFDIFGALLNGAKLVLVPKETVL-DVAK 481
Cdd:cd05906   175 TSGSTGFPKAVPLTHRNILaRSAgKIQHN-GLTPQD--VFLNWVPLDhvgGLVELHLRAVYLGCQQVHVPTEEILaDPLR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  482 LAGLIEKQQISVMFITTAFFNVLVDM---------NPDCLRharAILFGGERVSVSHVRKALGHLGP-----GKIKHVYG 547
Cdd:cd05906   252 WLDLIDRYRVTITWAPNFAFALLNDLleeiedgtwDLSSLR---YLVNAGEAVVAKTIRRLLRLLEPyglppDAIRPAFG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  548 PTES---TVFATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKF-AD 623
Cdd:cd05906   329 MTETcsgVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtED 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  624 NPFapgermyRTGDLArWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEK---ATVVVRESANGEKQLCAYY 700
Cdd:cd05906   409 GWF-------RTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAIFF 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  701 V------ADRSLPANEVRSTLSQEL---PAYMLPsyfVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05906   481 VpeydlqDALSETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
2355-2823 6.51e-38

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 153.58  E-value: 6.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVFEGQQLTYRELNERANRLARTLQ-ALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDR 2433
Cdd:PRK08314   20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2434 ISYMLEDSSAQVLLAQRRLQERV---------------SFAGTV-----VTVDDE-------QAYAGDG---------SN 2477
Cdd:PRK08314  100 LAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaQYSDYLpaepeIAVPAWlraepplQALAPGGvvawkealaAG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2478 L---ESAVGPNDLAYIIYTSGTTGKPKGVMVEHhglcslkqmfaNTLQINAQDRVVqFASLSFDASCWEV--------FQ 2546
Cdd:PRK08314  180 LappPHTAGPDDLAVLPYTSGTTGVPKGCMHTH-----------RTVMANAVGSVL-WSNSTPESVVLAVlplfhvtgMV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2547 -----TLFFGATLYIPT---KETILDYqwFERYmsdnGITTATLPPTYAVYL--NPD-HMPDFKRL--IAAGSASSLELL 2613
Cdd:PRK08314  248 hsmnaPIYAGATVVLMPrwdREAAARL--IERY----RVTHWTNIPTMVVDFlaSPGlAERDLSSLryIGGGGAAMPEAV 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2614 -QQWKDK--VKYFNAYGPTEdSICTTIWTPSTEDISQLKSVPIGGpiVNHRiyIVD-AHYQPVPVGVAGELCIAGVGLAR 2689
Cdd:PRK08314  322 aERLKELtgLDYVEGYGLTE-TMAQTHSNPPDRPKLQCLGIPTFG--VDAR--VIDpETLEELPPGEVGEIVVHGPQVFK 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2690 GYLNRPDLTAEKFVDnpFEpGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHD 2769
Cdd:PRK08314  397 GYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 2770 DASGQKQLCAYFVADRTMtvgelRGELSGE---------LPGYMIP--AHFVqlERMPLTPNGKI 2823
Cdd:PRK08314  474 DPRRGETVKAVVVLRPEA-----RGKTTEEeiiawarehMAAYKYPriVEFV--DSLPKSGSGKI 531
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
853-1264 6.96e-38

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 150.68  E-value: 6.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  853 YPLSSAQKrLYILHQLEGAEQSYNLPGVTLLEGA-LDRNRLEEAFRALIARHETLRTG-IEMVGGEPMQRIYPEVEFAV- 929
Cdd:cd19536     2 YPLSSLQE-GMLFHSLLNPGGSVYLHNYTYTVGRrLNLDLLLEALQVLIDRHDILRTSfIEDGLGQPVQVVHRQAQVPVt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  930 EHIRANEEEADAAVKQFI-----RAFDLAKPPLLRVGLIELAPERH-LLMFDMHHIVSDGISMDVLVEEFARLYGG---- 999
Cdd:cd19536    81 ELDLTPLEEQLDPLRAYKeetkiRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQlley 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1000 --EDLPAlRIQYKDYAVWQQSEAQKEQLkrqEAYWLEVFRGelpvLEMPTDYARPAVQSYAGN---ALRFELDAQKREGL 1074
Cdd:cd19536   161 kpLSLPP-AQPYRDFVAHERASIQQAAS---ERYWREYLAG----ATLATLPALSEAVGGGPEqdsELLVSVPLPVRSRS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1075 QriASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHG--DLHPLIGMFVNTLAIRnYPAADKTFLSYLEDVKE 1152
Cdd:cd19536   233 L--AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEttGAERLLGLFLNTLPLR-VTLSEETVEDLLKRAQE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1153 TTLGAFERQDYPFEElvdklkLARDLSRNPLFDTMFTLQNtENKEFRLPGLQLTPYPVE-----EHTSKFDLSLDIMESG 1227
Cdd:cd19536   310 QELESLSHEQVPLAD------IQRCSEGEPLFDSIVNFRH-FDLDFGLPEWGSDEGMRRgllfsEFKSNYDVNLSVLPKQ 382
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 386647928 1228 DGFLCGIEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19536   383 DRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
3850-4337 7.87e-38

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 153.36  E-value: 7.87e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3850 YQQEQTIHGLFEEQALRNPDAVAVVFEK-SQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAG 3928
Cdd:PRK06087   19 YWGDASLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3929 GAYIPIDPEYPEDRIRYMLEDSGAQALLT------QRH------LRERVSFAGTFVAVDDEQAYHADGS----------- 3985
Cdd:PRK06087   99 AVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkqTRPvdlilpLQNQLPQLQQIVGVDKLAPATSSLSlsqiiadyepl 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3986 NLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDAscweifkALFFG--ATL 4063
Cdd:PRK06087  179 TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHAT-------GFLHGvtAPF 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4064 YIPTSTTILDypLFES-----YMNENGIT----ATilpPTYAAYLN-----PDRMPSLKKLITGGSAASVEFVQQ-WKDK 4128
Cdd:PRK06087  252 LIGARSVLLD--IFTPdaclaLLEQQRCTcmlgAT---PFIYDLLNllekqPADLSALRFFLCGGTTIPKKVAREcQQRG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4129 VLYFNAYGPTEASIVTSI-------WDEASDslgdrksvpiGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYL 4201
Cdd:PRK06087  327 IKLLSVYGSTESSPHAVVnlddplsRFMHTD----------GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYL 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4202 NRPELTAeKFVDNpfepgERMYRTGDLVRWLPDGNLEYLGRiDHQVKIR-GYRIELGEVETQLAKIDAVQEAIVLAREDA 4280
Cdd:PRK06087  397 DEPELTA-RALDE-----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDE 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 4281 NGQQQLVAYFVAQRE---LTAAELRATMS-QELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK06087  470 RLGERSCAYVVLKAPhhsLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK07787 PRK07787
acyl-CoA synthetase; Validated
5945-6423 9.40e-38

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 151.30  E-value: 9.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDhlAVTFEDKQLTYGELNERANRLARTLRNAGvqpdqMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK07787   12 AADIAD--AVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHLlDRASFADKLVNLnddgayHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVrlv 6104
Cdd:PRK07787   85 RHILADSGAQAWLGPAPD-DPAGLPHVPVRL------HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIA--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6105 knTNYVELNE-----------------QTHILQTGavvfdastfeIWGALLNGGRL-YVVR--NETILDAVSLKnAIQQY 6164
Cdd:PRK07787  155 --ADLDALAEawqwtaddvlvhglplfHVHGLVLG----------VLGPLRIGNRFvHTGRptPEAYAQALSEG-GTLYF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6165 GINTMWLTAPLYNQLSQQdsgmFAGLKTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTEntTFSTTHTIVGEQKEAVP 6244
Cdd:PRK07787  222 GVPTVWSRIAADPEAARA----LRGARLLVSGSAALPVPVFDR-LAALTGHRPVERYGMTE--TLITLSTRADGERRPGW 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6245 IGKPINNSTAYIVDSKLSLLPVGV--WGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGDLARWLPDGTLEY 6322
Cdd:PRK07787  295 VGLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRI 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6323 KGR--IDeQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQkQLCAYFVAERELTIGELRAALSQELPNYMIPS 6399
Cdd:PRK07787  369 VGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVgVPDDDLGQ-RIVAYVVGADDVAADELIDFVAQQLSVHKRPR 446
                         490       500
                  ....*....|....*....|....
gi 386647928 6400 HFVPLERMPLTPNGKIDRRALPAP 6423
Cdd:PRK07787  447 EVRFVDALPRNAMGKVLKKQLLSE 470
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1321-1722 1.19e-37

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 152.00  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1321 DRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLT 1400
Cdd:cd05904    31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1401 QTHLQERAQQWGQTlqaVLCLDD---EAAYAEDASNVANVNEP-------HDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 1470
Cdd:cd05904   111 TAELAEKLASLALP---VVLLDSaefDSLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGRSKGVMLTHRNLIAMV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGY-RREYRLDQFPVRLLQLASFsFDVF-VGDIAR-TLYNGGTMVICPKDDRIDPARLhywISEEKITIFESTPALIIPF 1547
Cdd:cd05904   188 AQFvAGEGSNSDSEDVFLCVLPM-FHIYgLSSFALgLLRLGATVVVMPRFDLEELLAA---IERYKVTHLPVVPPIVLAL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1548 MDYVAEHGLDMSSMELLITSSDSCSvtdyRVLQERFGSQF---RIINAYGVTEA-AIDSSLYDeplaklPEAGNVPIGKA 1623
Cdd:cd05904   264 VKSPIVDKYDLSSLRQIMSGAAPLG----KELIEAFRAKFpnvDLGQGYGMTEStGVVAMCFA------PEKDRAKYGSV 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1624 AL---NAKFYIVD-AHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegERLYRTGDLARWMPDGNVDFIG 1699
Cdd:cd05904   334 GRlvpNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK------EGWLHTGDLCYIDEDGYLFIVD 407
                         410       420
                  ....*....|....*....|...
gi 386647928 1700 RIDNQAKIRGYRIETGEIETQLL 1722
Cdd:cd05904   408 RLKELIKYKGFQVAPAELEALLL 430
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
287-747 1.24e-37

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 150.29  E-value: 1.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   287 TYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGH 366
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   367 LQERVSFSgtwIRLDDEEAYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDK-LL 444
Cdd:TIGR01923   81 LEEKDFQA---DSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYaSAVGSKENLGFTEDDNwLL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   445 QLSSYSFDGSTFdIFGALLNGAKLVLVPKEtvldvAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRhARAILFGGER 524
Cdd:TIGR01923  158 SLPLYHISGLSI-LFRWLIEGATLRIVDKF-----NQLLEMIANERVTHISLVPTQLNRLLDEGGHNEN-LRKILLGGSA 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   525 VSVSHVRKALGHLGPgkIKHVYGPTEStvfATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQpigvaGELCVAGD 604
Cdd:TIGR01923  231 IPAPLIEEAQQYGLP--IYLSYGMTET---CSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIMVKGA 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   605 GLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATV 684
Cdd:TIGR01923  301 NLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVV 373
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928   685 VVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:TIGR01923  374 VPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
PRK07787 PRK07787
acyl-CoA synthetase; Validated
3869-4341 1.35e-37

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 150.91  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3869 DAVAVVFEKSQLTYGELNERANRLARTLRDAGvrpdqLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLE 3948
Cdd:PRK07787   15 IADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3949 DSGAQALL--TQRHLRERVSfagtfVAVDdeqaYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMF 4026
Cdd:PRK07787   90 DSGAQAWLgpAPDDPAGLPH-----VPVR----LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4027 ANTLQMTEQDRVVQ--------------FASLSFDASCWEIFK--------ALFFGATLY--IPT--STTILDyplfesy 4080
Cdd:PRK07787  161 AEAWQWTADDVLVHglplfhvhglvlgvLGPLRIGNRFVHTGRptpeayaqALSEGGTLYfgVPTvwSRIAAD------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4081 mnengitatilpPTYAAYLNPDRmpslkkLITGGSAA----------------SVEfvqqwkdkvlyfnAYGPTEASIVT 4144
Cdd:PRK07787  234 ------------PEAARALRGAR------LLVSGSAAlpvpvfdrlaaltghrPVE-------------RYGMTETLITL 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4145 SIwdeASDslGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVA--GELCISGVGLARGYLNRPELTAEKFVDNPFepgerm 4222
Cdd:PRK07787  283 ST---RAD--GERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------ 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4223 YRTGDLVRWLPDGNLEYLGR--IDhQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAE 4300
Cdd:PRK07787  352 FRTGDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADE 430
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928 4301 LRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPE 4341
Cdd:PRK07787  431 LIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
7467-7924 1.50e-37

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 151.33  E-value: 1.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7467 FENTQLTYRELNERANRLARTLRaEGVQADQPVGLMIERSLEMIVGAFAIMKAGgaYVPIDPEYP--EDRIRYMLEDSGA 7544
Cdd:cd05909     3 TLGTSLTYRKLLTGAIALARKLA-KMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7545 QVLLTQRHLQE--------CVSFDGKVIAADDEQA------------YG----EDGSNLEPVVG--PNHLAYVIYTSGTT 7598
Cdd:cd05909    80 KTVLTSKQFIEklklhhlfDVEYDARIVYLEDLRAkiskadkckaflAGkfppKWLLRIFGVAPvqPDDPAVILFTSGSE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7599 GKPKGVMVEHHGLCSLKLMFAETLRITEEDRVvqFASLSFdascweiFKALFFGATLYIPAKDTI--------LDYPLFE 7670
Cdd:cd05909   160 GLPKGVVLSHKNLLANVEQITAIFDPNPEDVV--FGALPF-------FHSFGLTGCLWLPLLSGIkvvfhpnpLDYKKIP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7671 SYMNENGITAAILPPT----YAIYLSPDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEASIVTSVWAASPD 7744
Cdd:cd05909   231 ELIYDKKATILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSPVISVNTPQSP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7745 GldlRSVPIGRPIANHQIFIVDSQNHM-LPVGVAGELCISGAGLARGYLNRPELTAekfvdnpFLAGERMYRTGDLARWL 7823
Cdd:cd05909   311 N---KEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKID 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7824 PDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQ-ETIVIARGDANGQQQLCAyFVADRELTVSELRGTLSQ-ELP 7901
Cdd:cd05909   381 GEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVL-LTTTTDTDPSSLNDILKNaGIS 459
                         490       500
                  ....*....|....*....|...
gi 386647928 7902 GYMIPSYFVQLEQMPLTPNGKID 7924
Cdd:cd05909   460 NLAKPSYIHQVEEIPLLGTGKPD 482
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
269-747 1.78e-37

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 150.88  E-value: 1.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  269 QAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEER 348
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  349 IRYMLEDSGTQVLLSQGHLQERVsFSGTWIRLDD-EEAYHEDGSNLESVNGPEHLTyVIYTSGTTGKPKGNLTTHRN--- 424
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKL-IPGISVKFAElMNGPKEEAEIQEEFDLDEVAT-IMYTSGTTGKPKGVIQTYGNhww 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  425 -IIRVVKNtnyIDVTGQDKLL------QLSSYSFdgstfdIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVMFIT 497
Cdd:PRK03640  169 sAVGSALN---LGLTEDDCWLaavpifHISGLSI------LMRSVIYGMRVVLVEK---FDAEKINKLLQTGGVTIISVV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  498 TAFFNVLVDMNPD--CLRHARAILFGGERVSvshvrKALghLGPGKIKHV-----YGPTE--STVFATSYDVHEVEEGAV 568
Cdd:PRK03640  237 STMLQRLLERLGEgtYPSSFRCMLLGGGPAP-----KPL--LEQCKEKGIpvyqsYGMTEtaSQIVTLSPEDALTKLGSA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  569 sipiGGPISNTAIYIVNaQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIE 648
Cdd:PRK03640  310 ----GKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLY 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  649 YVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYF 728
Cdd:PRK03640  378 VLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRF 457
                         490
                  ....*....|....*....
gi 386647928  729 VQLEQMPLTTNGKVDRRAL 747
Cdd:PRK03640  458 YFVEELPRNASGKLLRHEL 476
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
2352-2828 1.99e-37

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 151.17  E-value: 1.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2352 EEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQ-ALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYP 2430
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2431 EDRISYMLEDSSAQVLLAQRR-------LQERVSFAGTVVTVDDEQAYAGDGSNLESavGPNDLAYII-YTSGTTGKPKG 2502
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTfqnmalsMQKVSYVQRVISITSLKEIEDRKIDNFVE--KNESASFIIcYTSGTTGKPKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2503 VMVEHhglcslKQMFAN------TLQINAQDRVVQFASLsFDASCWEVFQ--TLFFGATLYIPTKetiLDYQWFERYMSD 2574
Cdd:PRK06839  167 AVLTQ------ENMFWNalnntfAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIVPRK---FEPTKALSMIEK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2575 NGITTATLPPTY--AVYLNPDHM-PDFK--RLIAAGSAS-SLELLQQWKDKVKYF-NAYGPTEDSicTTIWTPSTEDISQ 2647
Cdd:PRK06839  237 HKVTVVMGVPTIhqALINCSKFEtTNLQsvRWFYNGGAPcPEELMREFIDRGFLFgQGFGMTETS--PTVFMLSEEDARR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2648 lKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermyRTGDLAKWLPDGT 2727
Cdd:PRK06839  315 -KVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDEDGF 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2728 IEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGELPGYMI 2805
Cdd:PRK06839  387 VYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVkkSSSVLIEKDVIEHCRLFLAKYKI 466
                         490       500
                  ....*....|....*....|...
gi 386647928 2806 PAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK06839  467 PKEIVFLKELPKNATGKIQKAQL 489
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6994-7413 2.37e-37

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 149.14  E-value: 2.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6994 PM---QKGMWF-HTALDKEAgAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPR-GEPLQIVYRDKRIGFV 7068
Cdd:cd19532     3 PMsfgQSRFWFlQQYLEDPT-TFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEdGEPMQGVLASSPLRLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7069 YEDLSHlpADERQASVERLEQediaRGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAyvq 7148
Cdd:cd19532    82 HVQISD--EAEVEEEFERLKN----HVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7149 gdrpeQKAAPAYSQYIEWLENQDSAAASAYWSNYLAGYEGQ-----TALP-----QEKAQKRSEGYVAEHVVCELDKELS 7218
Cdd:cd19532   153 -----QPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEfstlpEPLPllpfaKVKSRPPLTRYDTHTAERRLDAALA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7219 ERMNRAAKQCRVTVntlMQ---AVWGVILQKYNATDDVVYGSVVSGRPAEipGIEEMIGLFINTIPVRVACQPEESFADV 7295
Cdd:cd19532   228 ARIKEASRKLRVTP---FHfylAALQVLLARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFADV 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7296 MGRMQE---AALESGRYDFyplyeiqtqsaqkQELINHL----------L--VFENYPMDEQVEQAGGDDsgTLSITDVD 7360
Cdd:cd19532   303 LKETRDkayAALAHSRVPF-------------DVLLDELgvprsathspLfqVFINYRQGVAESRPFGDC--ELEGEEFE 367
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 7361 VAEhTNYNFTVTVF--PGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19532   368 DAR-TPYDLSLDIIdnPDGDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
2345-2828 2.46e-37

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 150.74  E-value: 2.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2345 KTIHQLFEEQAERIPDHPAVVF--EGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAY 2422
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2423 VPIDPEYPEDRISYMLE-DSSAQVLLAQRRLQERVSF--AGTVVTVDDEqayAGDGSNlESA--------VGPNDLAYII 2491
Cdd:cd05923    81 ALINPRLKAAELAELIErGEMTAAVIAVDAQVMDAIFqsGVRVLALSDL---VGLGEP-ESAgpliedppREPEQPAFVF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2492 YTSGTTGKPKGVMVEHHGLCSlKQMFANT---LQINAQDRVVQFASLSFDASCWEVF-QTLFFGATLYIPTKETILD-YQ 2566
Cdd:cd05923   157 YTSGTTGLPKGAVIPQRAAES-RVLFMSTqagLRHGRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVVEEFDPADaLK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2567 WFERYMsdngITTATLPPTY------AVYLNPDHMPDFKRLIAAGSA---SSLELLQQWKDKVKyFNAYGPTEDSICTTI 2637
Cdd:cd05923   236 LIEQER----VTSLFATPTHldalaaAAEFAGLKLSSLRHVTFAGATmpdAVLERVNQHLPGEK-VNIYGTTEAMNSLYM 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2638 WTPSTEDI------SQLKSVPIGGPIVnhriyivdahyQPVPVGVAGELCIAGVGLA--RGYLNRPDLTAEKFVDnpfep 2709
Cdd:cd05923   311 RDARTGTEmrpgffSEVRIVRIGGSPD-----------EALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD----- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2710 geRMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTV 2789
Cdd:cd05923   375 --GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLS 452
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928 2790 GELRGE--LSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05923   453 ADELDQfcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
3880-4337 2.77e-37

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 148.65  E-value: 2.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGaqalltqr 3959
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 hlrervsfagtfVAVDDeqayhadgsnlepvvgpnhLAYVIYTSGTTGKPKGVMvehhglcslkLMFAN----------T 4029
Cdd:cd05912    74 ------------VKLDD-------------------IATIMYTSGTTGKPKGVQ----------QTFGNhwwsaigsalN 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4030 LQMTEQDR------VVQFASLSFdascweIFKALFFGATLYIptsttildYPLFES-----YMNENGITATILPPTY--- 4095
Cdd:cd05912   113 LGLTEDDNwlcalpLFHISGLSI------LMRSVIYGMTVYL--------VDKFDAeqvlhLINSGKVTIISVVPTMlqr 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4096 -AAYLNPDRMPSLKKLITGGSAASVEFVQQWKDKVL-YFNAYGPTEAS--IVTSIWDEASDSLGdrkSVpiGRPLANHRI 4171
Cdd:cd05912   179 lLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIpVYQSYGMTETCsqIVTLSPEDALNKIG---SA--GKPLFPVEL 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4172 YVVDSHNRmlPVGVaGELCISGVGLARGYLNRPELTAEKFVDNPFEpgermyrTGDLVRWLPDGNLEYLGRIDHQVKIRG 4251
Cdd:cd05912   254 KIEDDGQP--PYEV-GEILLKGPNVTKGYLNRPDATEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGG 323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4252 YRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGK 4331
Cdd:cd05912   324 ENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403

                  ....*.
gi 386647928 4332 IDRKAL 4337
Cdd:cd05912   404 LLRHEL 409
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
4911-5312 4.07e-37

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 150.46  E-value: 4.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4911 DRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLT 4990
Cdd:cd05904    31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4991 QTHLQERAQQWGQTLqaaLCLDD---EAAYAEDASNVANVNEP-------HDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd05904   111 TAELAEKLASLALPV---VLLDSaefDSLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGRSKGVMLTHRNLIAMV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGY-RREYRLDQFPVRLLQLASFsFDVF-VGDIAR-TLYNGGTMVICPKDDRIDPARLhywISEEKITIFESTPALIIPF 5137
Cdd:cd05904   188 AQFvAGEGSNSDSEDVFLCVLPM-FHIYgLSSFALgLLRLGATVVVMPRFDLEELLAA---IERYKVTHLPVVPPIVLAL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5138 MDYVAEHGLDMSSMVLLITSSDSCSvtdyRVLQERFGSQF---RIINAYGVTEA-AIDSSLYDeplaklPEAGNVPIGKA 5213
Cdd:cd05904   264 VKSPIVDKYDLSSLRQIMSGAAPLG----KELIEAFRAKFpnvDLGQGYGMTEStGVVAMCFA------PEKDRAKYGSV 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5214 AL---NAKFYIVD-AHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegERLYRTGDLARWMPDGNVDFIG 5289
Cdd:cd05904   334 GRlvpNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK------EGWLHTGDLCYIDEDGYLFIVD 407
                         410       420
                  ....*....|....*....|...
gi 386647928 5290 RIDNQAKIRGYRIETGEIETQLL 5312
Cdd:cd05904   408 RLKELIKYKGFQVAPAELEALLL 430
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
3875-4337 4.24e-37

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 149.79  E-value: 4.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3875 FEKSQLTYGELNERANRLARTLRDaGVRPDQLVGLMVERSLEMVVGIMAIMKAGgaYIPIDPEYP--EDRIRYMLEDSGA 3952
Cdd:cd05909     3 TLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3953 QALLTQRH------------------------LRERVSFA--------GTFVAVD-DEQAYHADgsnlepvVGPNHLAYV 3999
Cdd:cd05909    80 KTVLTSKQfieklklhhlfdveydarivyledLRAKISKAdkckaflaGKFPPKWlLRIFGVAP-------VQPDDPAVI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4000 IYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVvqFASLSFdascweiFKALFFGATLYIPTSTTI-------- 4071
Cdd:cd05909   153 LFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVV--FGALPF-------FHSFGLTGCLWLPLLSGIkvvfhpnp 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4072 LDYPLFESYMNENGITATILPPT----YAAYLNPDRMPSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTS 4145
Cdd:cd05909   224 LDYKKIPELIYDKKATILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSPVIS 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4146 IwdeaSDSLGDRKSVPIGRPL--ANHRIYVVDSHNRmLPVGVAGELCISGVGLARGYLNRPELTAekfvdnpFEPGERMY 4223
Cdd:cd05909   304 V----NTPQSPNKEGTVGRPLpgMEVKIVSVETHEE-VPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWY 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4224 RTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQ-EAIVLAREDANGQQQLVAyFVAQRELTAAELR 4302
Cdd:cd05909   372 DTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVL-LTTTTDTDPSSLN 450
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 4303 ATMSQ-ELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05909   451 DILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK06145 PRK06145
acyl-CoA synthetase; Validated
5945-6420 4.71e-37

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 150.04  E-value: 4.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHLLDRASFADKLVNLndDGAYHEDGSNLEP---------VNGPEHLTYVIYTSGTTGRPKGVMV 6095
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIVI--DAAAQADSRRLAQggleippqaAVAPTDLVRLMYTSGTTDRPKGVMH 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6096 EHRNVV-RLVKNTNYVELNEQTHILQTGAvVFDASTFEIWG--ALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTMWLt 6172
Cdd:PRK06145  170 SYGNLHwKSIDHVIALGLTASERLLVVGP-LYHVGAFDLPGiaVLWVGGTLRIHRE---FDPEAVLAAIERHRLTCAWM- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6173 APLYNQ----LSQQDSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKP 6248
Cdd:PRK06145  245 APVMLSrvltVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRA 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6249 INNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDE 6328
Cdd:PRK06145  325 LAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLTDRKKD 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6329 QVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQKQLCAYFVAE-RELTIGELRAALSQELPNYMIPSHFVPLER 6406
Cdd:PRK06145  398 MIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGERITAVVVLNPgATLTLEALDRHCRQRLASFKVPRQLKVRDE 477
                         490
                  ....*....|....
gi 386647928 6407 MPLTPNGKIDRRAL 6420
Cdd:PRK06145  478 LPRNPSGKVLKRVL 491
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
274-747 5.05e-37

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 149.77  E-value: 5.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd05926     3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLLSQG-----HLQERVSFSGTWIRL------------DDEEAYHEDG---SNLESVNGPEHLTYVIYTSGTTG 413
Cdd:cd05926    83 ADLGSKLVLTPKgelgpASRAASKLGLAILELaldvgvlirapsAESLSNLLADkknAKSEGVPLPDDLALILHTSGTTG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  414 KPKGNLTTHRNIIRVVKNtnyidVTGQDKLlqlssySFDGST------FDIFG-------ALLNGAKLVLVPKetvldva 480
Cdd:cd05926   163 RPKGVPLTHRNLAASATN-----ITNTYKL------TPDDRTlvvmplFHVHGlvasllsTLAAGGSVVLPPR------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  481 klagliekqqisvmFITTAFFNVLVDMNPD------------CLRHARAilFGGERVSVSHVRKALGHLGPGKIK----- 543
Cdd:cd05926   225 --------------FSASTFWPDVRDYNATwytavptihqilLNRPEPN--PESPPPKLRFIRSCSASLPPAVLEaleat 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  544 ------HVYGPTEST--VFATSYDVHEVEEGAVSIPIGgpisnTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPD 615
Cdd:cd05926   289 fgapvlEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVG-----VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  616 LTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEk 694
Cdd:cd05926   364 ANAEAAFKDGW------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFgVPDEKYGE- 436
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928  695 QLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05926   437 EVAAAVVlrEGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
PRK08315 PRK08315
AMP-binding domain protein; Validated
7444-7923 5.54e-37

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 151.12  E-value: 5.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7444 REQTIHGLFEEQAERMPEKAAVVF--ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGG 7521
Cdd:PRK08315   14 LEQTIGQLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7522 AYVPIDPEYPEDRIRYMLEDSGAQVLLTQRH---------LQECV-----SFDGK-----------VIAADDEQAYGEDG 7576
Cdd:PRK08315   94 ILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamLYELApelatCEPGQlqsarlpelrrVIFLGDEKHPGMLN 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7577 SN--LEPVVGPNHLAY-----------VI---YTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRV---VQF---- 7633
Cdd:PRK08315  174 FDelLALGRAVDDAELaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLcipVPLyhcf 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7634 -------ASLS-----------FDA----------SCweifKALFFGATLYIpakdTILDYPLFESYmnengitaailpp 7685
Cdd:PRK08315  254 gmvlgnlACVThgatmvypgegFDPlatlaaveeeRC----TALYGVPTMFI----AELDHPDFARF------------- 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7686 tyaiylspDrLPSLKKLITGGSAASVEFVQQWKDKvryFN------AYGPTEASIVtSVWAASPDGLDLRSVPIGRPIAN 7759
Cdd:PRK08315  313 --------D-LSSLRTGIMAGSPCPIEVMKRVIDK---MHmsevtiAYGMTETSPV-STQTRTDDPLEKRVTTVGRALPH 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7760 HQIFIVD-SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRIDHQV 7838
Cdd:PRK08315  380 LEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWM------HTGDLAVMDEEGYVNIVGRIKDMI 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7839 kIRG----Y-RielgEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPSYFVQ 7911
Cdd:PRK08315  454 -IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIlrPGATLTEEDVRDFCRGKIAHYKIPRYIRF 528
                         570
                  ....*....|..
gi 386647928 7912 LEQMPLTPNGKI 7923
Cdd:PRK08315  529 VDEFPMTVTGKI 540
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
258-747 5.57e-37

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 150.97  E-value: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  258 RDTTIHRLFEEQAERRPDAVAVT------FEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGIL 331
Cdd:PRK13295   22 HDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  332 KAGGAYVPIDPEYPEERIRYMLEDSGTQVLL-------------------SQGHLQERV--------SFSGTWIRLDDEE 384
Cdd:PRK13295  102 RIGAVLNPLMPIFRERELSFMLKHAESKVLVvpktfrgfdhaamarrlrpELPALRHVVvvggdgadSFEALLITPAWEQ 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  385 AYHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHR----NIIRVVKNtnyIDVTGQDKLLQLSSYSFdgSTFDIFG 460
Cdd:PRK13295  182 EPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANtlmaNIVPYAER---LGLGADDVILMASPMAH--QTGFMYG 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  461 ALLN---GAKLVLvpkETVLDVAKLAGLIEKQQISVMFITTAFFNVL---VDMNPDCLRHARAILFGGERVSVSHVRKAL 534
Cdd:PRK13295  257 LMMPvmlGATAVL---QDIWDPARAAELIRTEGVTFTMASTPFLTDLtraVKESGRPVSSLRTFLCAGAPIPGALVERAR 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  535 GHLGpGKIKHVYGPTEStvfatsydvheveeGAVSIPI------------GGPISNTAIYIVNAQNKLQPIGVAGELCVA 602
Cdd:PRK13295  334 AALG-AKIVSAWGMTEN--------------GAVTLTKlddpderasttdGCPLPGVEVRVVDADGAPLPAGQIGRLQVR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  603 GDGLARGYLNRPDLTAEKFadnpfapgERMYRTGDLARWLPDGTIEYVGRIDDqVKIRGFR-IELGEIEAHLLKLEAIEK 681
Cdd:PRK13295  399 GCSNFGGYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGRSKD-VIIRGGEnIPVVEIEALLYRHPAIAQ 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928  682 ATVVVRESANGEKQLCAYYV--ADRSLPANEVRSTL-SQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK13295  470 VAIVAYPDERLGERACAFVVprPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3402-3817 9.27e-37

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 147.41  E-value: 9.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3402 PM---QKGMWF-HNTLNrhggayiEQTLFNV------RGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYK 3471
Cdd:cd20483     3 PMstfQRRLWFlHNFLE-------DKTFLNLllvchiKGKPDVNLLQKALSELVRRHEVLRTAYFEG-DDFGEQQVLDDP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3472 PVEFAYEDLRHLAEAEwsAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTY 3551
Cdd:cd20483    75 SFHLIVIDLSEAADPE--AALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3552 EAYL-RNDLSERPAAP-SYSHYI----EWLEKQDMEAAARYWTGFLAGY-DSQTTLPQGKLH---NKDGEYTEANIlrSL 3621
Cdd:cd20483   153 DALRaGRDLATVPPPPvQYIDFTlwhnALLQSPLVQPLLDFWKEKLEGIpDASKLLPFAKAErppVKDYERSTVEA--TL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3622 GKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAeiAGIEEMIGLFINTIPVRVSCEAEQSFA 3701
Cdd:cd20483   231 DKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3702 DVMKRVQEAALESGGYDYYPL-YEIQAQSAQKQdlITHIMAFE---NFPMDEQIeqaGSYEDGKLAITDVDIAE-QTNYD 3776
Cdd:cd20483   309 DLLESTKTTCLEAYEHSAVPFdYIVDALDVPRS--TSHFPIGQiavNYQVHGKF---PEYDTGDFKFTDYDHYDiPTACD 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 386647928 3777 FTLVVM--PGEELAVRFYYNASVYEHSAMERLMGHLIHVLEQV 3817
Cdd:cd20483   384 IALEAEedPDGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSV 426
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
2370-2828 1.09e-36

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 147.24  E-value: 1.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2370 QLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAq 2449
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2450 rrlqervsfagtvvtvddeqayagdGSNLEsavgpnDLAYIIYTSGTTGKPKGVMVEHHGLC--SLKQMFANTLqiNAQD 2527
Cdd:cd05935    80 -------------------------GSELD------DLALIPYTSGTTGLPKGCMHTHFSAAanALQSAVWTGL--TPSD 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2528 RVVQ----FASLSFDAScweVFQTLFFGATLYIPT---KETILDYqwFERYmsdnGITTATLPPTYAVYLNPDhmPDFK- 2599
Cdd:cd05935   127 VILAclplFHVTGFVGS---LNTAVYVGGTYVLMArwdRETALEL--IEKY----KVTFWTNIPTMLVDLLAT--PEFKt 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2600 ------RLIAAGSASSLE-LLQQWKDK--VKYFNAYGPTEDSICTTIWTPstediSQLKSVPIGGPIVNHRIYIVDAHY- 2669
Cdd:cd05935   196 rdlsslKVLTGGGAPMPPaVAEKLLKLtgLRFVEGYGLTETMSQTHTNPP-----LRPKLQCLGIP*FGVDARVIDIETg 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2670 QPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGE 2749
Cdd:cd05935   271 RELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAE 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2750 IEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRtmtvgELRGELSGE---------LPGYMIPAHFVQLERMPLTPN 2820
Cdd:cd05935   348 VEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-----EYRGKVTEEdiiewareqMAAYKYPREVEFVDELPRSAS 422

                  ....*...
gi 386647928 2821 GKIDRKAL 2828
Cdd:cd05935   423 GKILWRLL 430
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
3878-4337 1.43e-36

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 147.36  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3878 SQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLt 3957
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3958 qrhlrervsfagtfvaVDDeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDR 4037
Cdd:cd05907    83 ----------------VED----------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDR 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4038 VVQFASLS--FDASCWEIFkALFFGATLYIPTS-------------TTILDYP-LFE-SYmneNGITATILPPTYAAYLN 4100
Cdd:cd05907   131 HLSFLPLAhvFERRAGLYV-PLLAGARIYFASSaetllddlsevrpTVFLAVPrVWEkVY---AAIKVKAVPGLKRKLFD 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4101 PDRMPSLKKLITGGSAASVEFVQQW-KDKVLYFNAYGPTEASIVTSIWDeasdsLGDRKSVPIGRPLANHRIYVVDShnr 4179
Cdd:cd05907   207 LAVGGRLRFAASGGAPLPAELLHFFrALGIPVYEGYGLTETSAVVTLNP-----PGDNRIGTVGKPLPGVEVRIADD--- 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4180 mlpvgvaGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRI-DHQVKIRGYRIELGE 4258
Cdd:cd05907   279 -------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEP 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4259 VETQLAKIDAVQEA-------------IVLAREDANG--QQQLVAYFVAQRELTAAELRATM-------SQELPNYMIPS 4316
Cdd:cd05907   346 IENALKASPLISQAvvigdgrpflvalIVPDPEALEAwaEEHGIAYTDVAELAANPAVRAEIeaaveaaNARLSRYEQIK 425
                         490       500
                  ....*....|....*....|....*..
gi 386647928 4317 YFVQLAQMP------LTPNGKIDRKAL 4337
Cdd:cd05907   426 KFLLLPEPFtiengeLTPTLKLKRPVI 452
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
2369-2828 2.19e-36

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 146.97  E-value: 2.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2369 QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLa 2448
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2449 qrrlqervsfagtvvtVDDeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDR 2528
Cdd:cd05907    83 ----------------VED----------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDR 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2529 VVQFASLS--FDASCWEvFQTLFFGATLYIPTK-ETILDyqwferymsdngiTTATLPPTY---------AVYLNPDH-- 2594
Cdd:cd05907   131 HLSFLPLAhvFERRAGL-YVPLLAGARIYFASSaETLLD-------------DLSEVRPTVflavprvweKVYAAIKVka 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2595 MPDFKRLIAA-------------GSASSLELLQQW-KDKVKYFNAYGPTEDSICTTIWTPSTEDISQLKSvPIGGPIVnh 2660
Cdd:cd05907   197 VPGLKRKLFDlavggrlrfaasgGAPLPAELLHFFrALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGK-PLPGVEV-- 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2661 RIyivdahyqpvpvGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRI-DHQVK 2739
Cdd:cd05907   274 RI------------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKkDLIIT 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2740 IRGYRIELGEIEEQLLKVASVQEAIVIAHDDA--SGQKQLCAYFVADR-------TMTVGELRG-------------ELS 2797
Cdd:cd05907   336 SGGKNISPEPIENALKASPLISQAVVIGDGRPflVALIVPDPEALEAWaeehgiaYTDVAELAAnpavraeieaaveAAN 415
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 2798 GELPGYMIPAHFVQLERMP------LTPNGKIDRKAL 2828
Cdd:cd05907   416 ARLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRPVI 452
PRK06188 PRK06188
acyl-CoA synthetase; Validated
271-750 2.48e-36

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 148.21  E-value: 2.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  271 ERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIR 350
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  351 YMLEDSGTQVLLSQ--------GHLQERVSFSGTWIRLDD--------EEAYHEDGSNLESVNGPEHLTYVIYTSGTTGK 414
Cdd:PRK06188  103 YVLEDAGISTLIVDpapfveraLALLARVPSLKHVLTLGPvpdgvdllAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  415 PKGNLTTHRNIirvVKNTNYI----DVTGQDKLLQLSSYSFDGSTFdIFGALLNGAKLVLVPK---ETVLDVaklaglIE 487
Cdd:PRK06188  183 PKGVMGTHRSI---ATMAQIQlaewEWPADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVLAKfdpAEVLRA------IE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  488 KQQISVMFITTAFFNVLVDmNPDClrHAR------AILFGGERVSVSHVRKALGHLGPgKIKHVYGPTESTVFAT--SYD 559
Cdd:PRK06188  253 EQRITATFLVPTMIYALLD-HPDL--RTRdlssleTVYYGASPMSPVRLAEAIERFGP-IFAQYYGQTEAPMVITylRKR 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  560 VHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLA 639
Cdd:PRK06188  329 DHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-------WLHTGDVA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  640 RWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKqLCAYYV--ADRSLPANEVRSTLS 716
Cdd:PRK06188  402 REDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIgVPDEKWGEA-VTAVVVlrPGAAVDAAELQAHVK 480
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928  717 QELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAP 750
Cdd:PRK06188  481 ERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7593-7928 2.71e-36

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 143.96  E-value: 2.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7593 YTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLsfdascWEIF-------KALFFGATLYIPAKdtILD 7665
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPL------FHCFgsvlgvlACLTHGATMVFPSP--SFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7666 -YPLFESYMNENGiTAAILPPTYAIYL--SPDR----LPSLKKLITGGSAASVEFVQQWKDKVR---YFNAYGPTEASIV 7735
Cdd:cd05917    81 pLAVLEAIEKEKC-TALHGVPTMFIAEleHPDFdkfdLSSLRTGIMAGAPCPPELMKRVIEVMNmkdVTIAYGMTETSPV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7736 TSVwAASPDGLDLRSVPIGRPIANHQIFIVDSQ-NHMLPVGVAGELCISGAGLARGYLNRPELTAEKfvdnpfLAGERMY 7814
Cdd:cd05917   160 STQ-TRTDDSIEKRVNTVGRIMPHTEAKIVDPEgGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGWL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7815 RTGDLARWLPDGNIEYLGRIDHQVkIRG-YRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSE 7891
Cdd:cd05917   233 HTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRlkEGAELTEED 311
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 386647928 7892 LRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05917   312 IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
5935-6420 3.07e-36

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 148.58  E-value: 3.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5935 KTIHQLFEEQAERIPDHlAVTFEDKQ-----LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAG 6009
Cdd:cd05906    10 RTLLELLLRAAERGPTK-GITYIDADgseefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6010 G--AYVPIDPDYPEDR--------IRYMLE------DSG-----AKLLLVQGHLLDRASFADKLvnlnDDGAYHEDGsnl 6068
Cdd:cd05906    89 FvpAPLTVPPTYDEPNarlrklrhIWQLLGspvvltDAElvaefAGLETLSGLPGIRVLSIEEL----LDTAADHDL--- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6069 ePVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVV-RLV-KNTNYvELNEQTHIL------QTGAVVFdastFEIWGALLNG 6140
Cdd:cd05906   162 -PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILaRSAgKIQHN-GLTPQDVFLnwvpldHVGGLVE----LHLRAVYLGC 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6141 GRLYVVRNETILDAVSLKNAIQQYGINTMWltAP--LYNQLSQQ------DSGMFAGLKTLIVGGDVLSVPHINRVLREH 6212
Cdd:cd05906   236 QQVHVPTEEILADPLRWLDLIDRYRVTITW--APnfAFALLNDLleeiedGTWDLSSLRYLVNAGEAVVAKTIRRLLRLL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6213 A--GL---SIVNGYGPTE-------NTTFST-THTivgEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGV 6279
Cdd:cd05906   314 EpyGLppdAIRPAFGMTEtcsgviySRSFPTyDHS---QALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVV 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6280 ARGYLNRPELTAEKFVESSFlpgercYRTGDLArWLPDGTLEYKGRIDEQVKIRGYRIELGEIE---EQLLKVASVKEAT 6356
Cdd:cd05906   391 TKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEaavEEVPGVEPSFTAA 463
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 6357 VIVREDESGQKQLCAYFVAEREL------TIGELRAALSQEL---PNYMIPshfVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05906   464 FAVRDPGAETEELAIFFVPEYDLqdalseTLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
4894-5380 3.29e-36

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 147.06  E-value: 3.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4894 EKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 4973
Cdd:cd12118    11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4974 DRIQFMLEDSAASVLLTQTHLQ-ERAQQWGQTLQAALCLDDEaayaedasnvanvnepHDLAYVIYTSGTTGRPKGVMIE 5052
Cdd:cd12118    91 EEIAFILRHSEAKVLFVDREFEyEDLLAEGDPDFEWIPPADE----------------WDPIALNYTSGTTGRPKGVVYH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5053 HRS--LVNTAAGYrrEYRLDQFPVRLLQLASFSFD--VFVGDIARtlyNGGTMVICPKddrIDPARLHYWISEEKITIFE 5128
Cdd:cd12118   155 HRGayLNALANIL--EWEMKQHPVYLWTLPMFHCNgwCFPWTVAA---VGGTNVCLRK---VDAKAIYDLIEKHKVTHFC 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5129 STPALIIPFMDYVAEHGLDMSSMVLLITSSdscSVTDYRVLQ--ERFGsqFRIINAYGVTEAAIDSSLydepLAKLPEAG 5206
Cdd:cd12118   227 GAPTVLNMLANAPPSDARPLPHRVHVMTAG---APPPAAVLAkmEELG--FDVTHVYGLTETYGPATV----CAWKPEWD 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5207 NVPIG-KAALNAK----------FYIVDAH-LNPVPV-GV-LGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyR 5272
Cdd:cd12118   298 ELPTEeRARLKARqgvryvgleeVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGGWF-------H 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5273 TGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAE--SELKLSELR 5350
Cdd:cd12118   371 SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKegAKVTEEEII 450
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 5351 SSLSQELPGYMIPSYFVQLEqLPLTANGKI 5380
Cdd:cd12118   451 AFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
6990-7413 3.98e-36

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 145.20  E-value: 3.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6990 YTLTPMQKGMWFHTALDKEAGAY--FEQMRFTvqGSLDAEQFARSWNDLVARHAILRTNFFSGPrGEPLQIVYRDKRIGF 7067
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYnlAEYLEIT--GPVDLAVLERALRQVIAEAETLRLRFTEEE-GEPYQWIDPYTPVPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7068 VYEDLSHLPADErqASVERLEQEDIARGFDLEQDALVRVAVIRTQETsyRVLW--SFHHILMDGWCLPLVVKELFETYEA 7145
Cdd:cd19533    79 RHIDLSGDPDPE--GAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDN--RHFWyqRVHHIVMDGFSFALFGQRVAEIYTA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7146 YVQGDRPEQKAAPAYSQYIEwlENQDSAAAS------AYWSNYLAGyEGQTALPQEKAQKRSEGyvAEHVVCELDKELSE 7219
Cdd:cd19533   155 LLKGRPAPPAPFGSFLDLVE--EEQAYRQSErferdrAFWTEQFED-LPEPVSLARRAPGRSLA--FLRRTAELPPELTR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7220 RMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGR--PAEIpgieEMIGLFINTIPVRVACQPEESFADVMG 7297
Cdd:cd19533   230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgAAAR----QTPGMVANTLPLRLTVDPQQTFAELVA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7298 RMQEAALESGRYDFYPLYEIQTQSAQKQELINHLLVFENY-PMDEQveqaggddsgtLSITDVDVAEHTNYN-----FTV 7371
Cdd:cd19533   306 QVSRELRSLLRHQRYRYEDLRRDLGLTGELHPLFGPTVNYmPFDYG-----------LDFGGVVGLTHNLSSgptndLSI 374
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 7372 TVFP---GDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19533   375 FVYDrddESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
5932-6420 4.25e-36

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 147.98  E-value: 4.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5932 PSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGA 6011
Cdd:PRK06155   18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6012 YVPIDPDYPEDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVN-------LNDDGAYHED-----------GSNLEPVN- 6072
Cdd:PRK06155   98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLplpavwlLDAPASVSVPagwstaplpplDAPAPAAAv 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6073 GPEHLTYVIYTSGTTGRPKGVMVEH-------RNVVRLVkntnyvELNEQtHILQTGAVVFDAS---TFeiWGALLNGGR 6142
Cdd:PRK06155  178 QPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDL------EIGAD-DVLYTTLPLFHTNalnAF--FQALLAGAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6143 lYVVrnETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYG 6222
Cdd:PRK06155  249 -YVL--EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYG 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6223 PTE-NTTFSTTHtivGEQKEAVpIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGD---GVARGYLNRPELTAEKFVESS 6298
Cdd:PRK06155  326 STEtNFVIAVTH---GSQRPGS-MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLW 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6299 FLPGERCYRTgdlarwlPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE-- 6376
Cdd:PRK06155  402 FHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRdg 474
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 386647928 6377 RELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK06155  475 TALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
3880-4341 4.30e-36

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 145.72  E-value: 4.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQR 3959
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 HLRERVSfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVV 4039
Cdd:cd05969    81 ELYERTD--------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4040 QFASLSFDA-SCWEIFKALFFGATLYIPTSTtiLDYPLFESYMNENGITATILPPT-------YAAYLNPD-RMPSLKKL 4110
Cdd:cd05969   135 CTADPGWVTgTVYGIWAPWLNGVTNVVYEGR--FDAESWYGIIERVKVTVWYTAPTairmlmkEGDELARKyDLSSLRFI 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4111 ITGGSAASVEFVqQWKDKVL---YFNAYGPTE-ASIVTsiwdeASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVA 4186
Cdd:cd05969   213 HSVGEPLNPEAI-RWGMEVFgvpIHDTWWQTEtGSIMI-----ANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTK 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4187 GELCISG--VGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLA 4264
Cdd:cd05969   287 GILALKPgwPSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALM 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4265 KIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAA-----ELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:cd05969   360 EHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSdelkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKA 439

                  ..
gi 386647928 4340 PE 4341
Cdd:cd05969   440 KE 441
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1298-1797 5.88e-36

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 148.79  E-value: 5.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1298 VFHALFEKQAERTPEVAAVVYENDR-----LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGG 1372
Cdd:cd05968    62 IVEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1373 AYVPLDPDYPSDRIQFMLEDSAASVLLTQ-------------THLQERAQQWGQTLQAV----LCLDDEAAYAEDAS--- 1432
Cdd:cd05968   142 IVVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQCPTVEKVVvvrhLGNDFTPAKGRDLSyde 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1433 ------NVANVNEPHDLAYVIYTSGTTGRPKGVmiehrslVNTAAGyrreyrldqFPVRLLQLASFSFDVFVGD------ 1500
Cdd:cd05968   222 eketagDGAERTESEDPLMIIYTSGTTGKPKGT-------VHVHAG---------FPLKAAQDMYFQFDLKPGDlltwft 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1501 ----------IARTLYNGGTMVI---CPkdDRIDPARLHYWISEEKITIFESTPALIIPFM----DYVAEHGLdmSSMEL 1563
Cdd:cd05968   286 dlgwmmgpwlIFGGLILGATMVLydgAP--DHPKADRLWRMVEDHEITHLGLSPTLIRALKprgdAPVNAHDL--SSLRV 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1564 LITSSDSCSVTDYRVLQE-RFGSQFRIINAYGVTEAA--IDSSLYDEPLAKLPEAGNVPIGKAAlnakfyIVDAHLNPVP 1640
Cdd:cd05968   362 LGSTGEPWNPEPWNWLFEtVGKGRNPIINYSGGTEISggILGNVLIKPIKPSSFNGPVPGMKAD------VLDESGKPAR 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1641 vGVLGELCIGG--IGVARGYLNrpelTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIE 1718
Cdd:cd05968   436 -PEVGELVLLApwPGMTRGFWR----DEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIE 510
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1719 TqLLKAEGVREAVVV--VREDAKGQKVLCayFT------AESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:cd05968   511 S-VLNAHPAVLESAAigVPHPVKGEAIVC--FVvlkpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKV 587

                  ....*..
gi 386647928 1791 DRKALPA 1797
Cdd:cd05968   588 MRRVIRA 594
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
286-747 5.93e-36

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 145.17  E-value: 5.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSqg 365
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  366 hlqervsfsgtwirlDDEEayhedgsnlesvngpehLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTNY-IDVTGQDKLL 444
Cdd:cd05972    79 ---------------DAED-----------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYwLGLRPDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  445 QLSSYSF-DGSTFDIFGALLNGAKlVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLR--HARAILFG 521
Cdd:cd05972   127 NIADPGWaKGAWSSFFGPWLLGAT-VFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKfsHLRLVVSA 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  522 GERVSVSHVRKALGHLGPgKIKHVYGPTESTVFATSYDVHEVEEGAvsipIGGPISNTAIYIVNAQNKLQPIGVAGELCV 601
Cdd:cd05972   206 GEPLNPEVIEWWRAATGL-PIRDGYGQTETGLTVGNFPDMPVKPGS----MGRPTPGYDVAIIDDDGRELPPGEEGDIAI 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  602 --AGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLK---- 675
Cdd:cd05972   281 klPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEhpav 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  676 LEA------------IEKATVVVRESANGEKQLcayyvadrslpANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVD 743
Cdd:cd05972   354 AEAavvgspdpvrgeVVKAFVVLTSGYEPSEEL-----------AEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422

                  ....
gi 386647928  744 RRAL 747
Cdd:cd05972   423 RVEL 426
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
2359-2823 7.76e-36

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 148.11  E-value: 7.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQ------LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPED 2432
Cdd:cd17634    67 GDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2433 RISYMLEDSSAQVLL-----------------AQRRLQERVSFAGTVVTVDDEQA-YAGDGS---------------NLE 2479
Cdd:cd17634   147 AVAGRIIDSSSRLLItadggvragrsvplkknVDDALNPNVTSVEHVIVLKRTGSdIDWQEGrdlwwrdliakaspeHQP 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2480 SAVGPNDLAYIIYTSGTTGKPKGVMVEHHG-LCSLKQMFANTLQINAQDRVVQFASLSF-DASCWEVFQTLFFGATLYI- 2556
Cdd:cd17634   227 EAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWvTGHSYLLYGPLACGATTLLy 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2557 ------PTKetilDYQWfeRYMSDNGITTATLPPTYAVYLnpdhMPDFKRLIAAGSASSLELL-----------QQW--- 2616
Cdd:cd17634   307 egvpnwPTP----ARMW--QVVDKHGVNILYTAPTAIRAL----MAAGDDAIEGTDRSSLRILgsvgepinpeaYEWywk 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2617 ---KDKVKYFNAYGPTEDS--ICTTIwtPSTEdisQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGV--GLAR 2689
Cdd:cd17634   377 kigKEKCPVVDTWWQTETGgfMITPL--PGAI---ELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTR 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2690 GYLNRPDltaeKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHD 2769
Cdd:cd17634   452 TLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIP 527
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 2770 DASGQKQLCAYFVADRTMTVG-----ELRGELSGELPGYMIP--AHFVQleRMPLTPNGKI 2823
Cdd:cd17634   528 HAIKGQAPYAYVVLNHGVEPSpelyaELRNWVRKEIGPLATPdvVHWVD--SLPKTRSGKI 586
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
7451-7925 9.47e-36

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 147.45  E-value: 9.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:PRK05605   37 LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLY 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLL-------TQRHLQECVSFDGKV----------------------IAADDEQ----------- 7570
Cdd:PRK05605  117 TAHELEHPFEDHGARVAIvwdkvapTVERLRRTTPLETIVsvnmiaampllqrlalrlpipaLRKARAAltgpapgtvpw 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7571 ------AYGEDGSNLE-PVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLM---FAETLRiteEDRVVQFASLSfda 7640
Cdd:PRK05605  197 etlvdaAIGGDGSDVShPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkaWVPGLG---DGPERVLAALP--- 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7641 scweIFKAlfFGATL------YIPAKDTIL---DYPLFESYMNENgiTAAILPPTYAIYlspDR-----------LPSLK 7700
Cdd:PRK05605  271 ----MFHA--YGLTLcltlavSIGGELVLLpapDIDLILDAMKKH--PPTWLPGVPPLY---EKiaeaaeergvdLSGVR 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7701 KLITGGSAASVEFVQQWKDKV--RYFNAYGPTEASIVTsvwAASPDGLDLRSVPIGRPIANHQIFIVDSQN--HMLPVGV 7776
Cdd:PRK05605  340 NAFSGAMALPVSTVELWEKLTggLLVEGYGLTETSPII---VGNPMSDDRRPGYVGVPFPDTEVRIVDPEDpdETMPDGE 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7777 AGELCISGAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLK 7856
Cdd:PRK05605  417 EGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE 489
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 7857 IASVQETIVIARGDANGQQQLCAYFVADRELTVSE--LRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:PRK05605  490 HPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
PRK06188 PRK06188
acyl-CoA synthetase; Validated
7457-7931 1.16e-35

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 146.28  E-value: 1.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7457 ERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIR 7536
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7537 YMLEDSGAQVLL------TQRHLQECVSFDG-KVIAADDEQAYGEDGSNLEPVVGPNHL---------AYVIYTSGTTGK 7600
Cdd:PRK06188  103 YVLEDAGISTLIvdpapfVERALALLARVPSlKHVLTLGPVPDGVDLLAAAAKFGPAPLvaaalppdiAGLAYTGGTTGK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7601 PKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSfDASCWEIFKALFFGATLYIPAKdtiLDYPLFESYMNENGITA 7680
Cdd:PRK06188  183 PKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVLAK---FDPAEVLRAIEEQRITA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7681 AILPPT--YAIYLSPD----RLPSLKKLITGGSAASVEFVQQWKDKVR--YFNAYGPTEASIVTSVWA-ASPDGLD---L 7748
Cdd:PRK06188  259 TFLVPTmiYALLDHPDlrtrDLSSLETVYYGASPMSPVRLAEAIERFGpiFAQYYGQTEAPMVITYLRkRDHDPDDpkrL 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7749 RSVpiGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNpFLagermyRTGDLARWLPDGNI 7828
Cdd:PRK06188  339 TSC--GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-WL------HTGDVAREDEDGFY 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7829 EYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIP 7906
Cdd:PRK06188  410 YIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVlrPGAAVDAAELQAHVKERKGSVHAP 489
                         490       500
                  ....*....|....*....|....*
gi 386647928 7907 SYFVQLEQMPLTPNGKIDRNALPAP 7931
Cdd:PRK06188  490 KQVDFVDSLPLTALGKPDKKALRAR 514
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
3880-4337 1.42e-35

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 145.84  E-value: 1.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQR 3959
Cdd:cd05904    33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 HLRERV-SFAGTFVAVDDEQAYHADGSNL----------EPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAN 4028
Cdd:cd05904   113 ELAEKLaSLALPVVLLDSAEFDSLSFSDLlfeadeaeppVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4029 TLQMTEQDRVVQFASLSFdascWEIFK-ALFFGATLYIPTSTTIL---DYPLFESYMNENGIT-ATILPP-----TYAAY 4098
Cdd:cd05904   193 GEGSNSDSEDVFLCVLPM----FHIYGlSSFALGLLRLGATVVVMprfDLEELLAAIERYKVThLPVVPPivlalVKSPI 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4099 LNPDRMPSLKKLITGGSAASVEFVQQWKDK---VLYFNAYGPTEAS-IVTSIWDEASDSlgdRKSVPIGRPLANHRIYVV 4174
Cdd:cd05904   269 VDKYDLSSLRQIMSGAAPLGKELIEAFRAKfpnVDLGQGYGMTESTgVVAMCFAPEKDR---AKYGSVGRLVPNVEAKIV 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4175 D-SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDnpfepgERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYR 4253
Cdd:cd05904   346 DpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK------EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQ 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4254 IELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAElratmsQELPNYM----IP------SYFVqlAQ 4323
Cdd:cd05904   420 VAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE------DEIMDFVakqvAPykkvrkVAFV--DA 491
                         490
                  ....*....|....
gi 386647928 4324 MPLTPNGKIDRKAL 4337
Cdd:cd05904   492 IPKSPSGKILRKEL 505
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
261-747 1.46e-35

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 145.34  E-value: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFEDRQ--LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYV 338
Cdd:cd05923     2 TVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  339 PIDPEYPEERIRYMLE-DSGTQVLLSQGHLQERVSFSGTW--IRLDDEEAYHEDGSNLESV----NGPEHLTYVIYTSGT 411
Cdd:cd05923    82 LINPRLKAAELAELIErGEMTAAVIAVDAQVMDAIFQSGVrvLALSDLVGLGEPESAGPLIedppREPEQPAFVFYTSGT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  412 TGKPKGNLTTHRNI----IRVVKNTNYIDVTGQDKLLQLSSYSFDGsTFDIFGALLNGAKLVLVPKEtvLDVAKLAGLIE 487
Cdd:cd05923   162 TGLPKGAVIPQRAAesrvLFMSTQAGLRHGRHNVVLGLMPLYHVIG-FFAVLVAALALDGTYVVVEE--FDPADALKLIE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  488 KQQISVMFITTAFFNVLV---DMNPDCLRHARAILFGGERVSVSHVRKALGHLgPGKIKHVYGPTESTVFATSYDVHEVE 564
Cdd:cd05923   239 QERVTSLFATPTHLDALAaaaEFAGLKLSSLRHVTFAGATMPDAVLERVNQHL-PGEKVNIYGTTEAMNSLYMRDARTGT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  565 EGAVS-------IPIGGPISNTAiyivnaqnklqPIGVAGELCVAGDGLA--RGYLNRPDLTAEKFADnpfapgeRMYRT 635
Cdd:cd05923   318 EMRPGffsevriVRIGGSPDEAL-----------ANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRT 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  636 GDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKQLCAYYVADRSLPANEVRS- 713
Cdd:cd05923   380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgVADERWGQSVTACVVPREGTLSADELDQf 459
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928  714 TLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05923   460 CRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
7445-7928 1.63e-35

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 146.44  E-value: 1.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7445 EQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYV 7524
Cdd:PRK06155   20 ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7525 PIDPEYPEDRIRYMLEDSGAQVLLTQRHLQECV-SFDGKVIAADDEQAYGEDGSNLEPV------------------VGP 7585
Cdd:PRK06155  100 PINTALRGPQLEHILRNSGARLLVVEAALLAALeAADPGDLPLPAVWLLDAPASVSVPAgwstaplppldapapaaaVQP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7586 NHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKdtiLD 7665
Cdd:PRK06155  180 GDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPR---FS 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7666 YPLFESYMNENGITA-----AILPptyaIYLSP-----DRLPSLKKLITGGSAAsvEFVQQWKDK--VRYFNAYGPTEAS 7733
Cdd:PRK06155  257 ASGFWPAVRRHGATVtyllgAMVS----ILLSQparesDRAHRVRVALGPGVPA--ALHAAFRERfgVDLLDGYGSTETN 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7734 IVTSVWAASPdgldlRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGA---GLARGYLNRPELTAEKFVDNPFLAG 7810
Cdd:PRK06155  331 FVIAVTHGSQ-----RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7811 ERMYRTgdlarwlPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVAdRELTVS 7890
Cdd:PRK06155  406 DRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVL-RDGTAL 477
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928 7891 E----LRGTLSQeLPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK06155  478 EpvalVRHCEPR-LAYFAVPRYVEFVAALPKTENGKVQKFVL 518
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
255-745 1.78e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 146.68  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  255 DYPrDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAG 334
Cdd:PRK05605   28 DYG-DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  335 GAYVPIDPEYPEERIRYMLEDSGTQVLL----SQGHLQE-------------------------------------RVSF 373
Cdd:PRK05605  107 AVVVEHNPLYTAHELEHPFEDHGARVAIvwdkVAPTVERlrrttpletivsvnmiaampllqrlalrlpipalrkaRAAL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  374 SG------TWIRL-DDEEAYHEDGSNLESVNgPEHLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDKLLQ 445
Cdd:PRK05605  187 TGpapgtvPWETLvDAAIGGDGSDVSHPRPT-PDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQGKAWVPGLGDGPERV 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  446 LSSYSFdgstFDIFGALLN-------GAKLVLVPK---ETVLDVAK----------------LAGLIEKQQISvmfitta 499
Cdd:PRK05605  266 LAALPM----FHAYGLTLCltlavsiGGELVLLPApdiDLILDAMKkhpptwlpgvpplyekIAEAAEERGVD------- 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  500 ffnvlvdmnpdcLRHARAILFGGERVSVSHVRKALGHLGpGKIKHVYGPTESTVFATSYDVHEVEE-GAVSIPIggPisN 578
Cdd:PRK05605  335 ------------LSGVRNAFSGAMALPVSTVELWEKLTG-GLLVEGYGLTETSPIIVGNPMSDDRRpGYVGVPF--P--D 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  579 TAIYIVNAQN--KLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQ 656
Cdd:PRK05605  398 TEVRIVDPEDpdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKEL 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  657 VKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVAD--RSLPANEVRSTLSQELPAYMLPSYFVQLEQM 734
Cdd:PRK05605  471 IITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEpgAALDPEGLRAYCREHLTRYKVPRRFYHVDEL 550
                         570
                  ....*....|.
gi 386647928  735 PLTTNGKVDRR 745
Cdd:PRK05605  551 PRDQLGKVRRR 561
PRK07470 PRK07470
acyl-CoA synthetase; Validated
2355-2828 1.85e-35

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 145.95  E-value: 1.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRI 2434
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 SYMLEDSSAQVLLAQR--------------RLQERVSFAGTVVTVDDEQAYAGD-GSNLESA-VGPNDLAYIIYTSGTTG 2498
Cdd:PRK07470   97 AYLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHlGARVANAaVDHDDPCWFFFTSGTTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2499 KPKGVMVEHHG--------LCSLkqmFANTLQinaQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETILDYQW--F 2568
Cdd:PRK07470  177 RPKAAVLTHGQmafvitnhLADL---MPGTTE---QDASLVVAPLSHGAGIHQLCQVARGAATVLLPSERFDPAEVWalV 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2569 ERYMSDNGITTATL------PPTYAVYlnpDHmPDFKRLIAAGSASSLE-----LLQQWKDKVKYFnayGPTEDSICTTI 2637
Cdd:PRK07470  251 ERHRVTNLFTVPTIlkmlveHPAVDRY---DH-SSLRYVIYAGAPMYRAdqkraLAKLGKVLVQYF---GLGEVTGNITV 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2638 WTP---STEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermy 2714
Cdd:PRK07470  324 LPPalhDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF------- 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2715 RTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVA--DRTMTVGEL 2792
Cdd:PRK07470  397 RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVArdGAPVDEAEL 476
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 2793 RGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK07470  477 LAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
5949-6415 2.08e-35

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 144.75  E-value: 2.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYML 6028
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6029 EDSGAKLLLVqghllDRASFADKLVNLNDDGAyhedgsNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVvrlvkntn 6108
Cdd:cd12118    98 RHSEAKVLFV-----DREFEYEDLLAEGDPDF------EWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGA-------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6109 YVEL--NEQTHILQTGAV------VFDAS--TFeIWGALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTMWLTAPLYNQ 6178
Cdd:cd12118   159 YLNAlaNILEWEMKQHPVylwtlpMFHCNgwCF-PWTVAAVGGTNVCLRK---VDAKAIYDLIEKHKVTHFCGAPTVLNM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6179 L---SQQDSGMFAGLKTLIVGGdvlSVPH---INRVlrEHAGLSIVNGYGPTENTTFSTthtiVGEQK---EAVPI---- 6245
Cdd:cd12118   235 LanaPPSDARPLPHRVHVMTAG---APPPaavLAKM--EELGFDVTHVYGLTETYGPAT----VCAWKpewDELPTeera 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6246 ------GKPINNSTAYIVDSKLSLLPV---GV-WGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWL 6315
Cdd:cd12118   306 rlkarqGVRYVGLEEVDVLDPETMKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGGWF-------HSGDLAVIH 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6316 PDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAyFVAERE---LTIGELRAALSQEL 6392
Cdd:cd12118   379 PDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA-FVELKEgakVTEEEIIAFCREHL 457
                         490       500
                  ....*....|....*....|....*
gi 386647928 6393 PNYMIPSH--FVPLermPLTPNGKI 6415
Cdd:cd12118   458 AGFMVPKTvvFGEL---PKTSTGKI 479
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
5959-6378 2.25e-35

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 144.42  E-value: 2.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5959 KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLV 6038
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6039 QghlldrasfadklvnlnddgayhedgsnlepvNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNtnyveLNEqthI 6118
Cdd:cd17640    84 E--------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRS-----LSD---I 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6119 LQTGAVVFDASTFEIWGALLNGGRLYVVR---NETILDAVSLKNAIQQYGINTMwLTAP-----LYNQLSQQDSGMFAG- 6189
Cdd:cd17640   124 VPPQPGDRFLSILPIWHSYERSAEYFIFAcgcSQAYTSIRTLKDDLKRVKPHYI-VSVPrlwesLYSGIQKQVSKSSPIk 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6190 ---LKTLIVGGDV---LS-----VPHINRVLrEHAGLSIVNGYGPTENTTFSTT----HTIVGEqkeavpIGKPINNSTA 6254
Cdd:cd17640   203 qflFLFFLSGGIFkfgISgggalPPHVDTFF-EAIGIEVLNGYGLTETSPVVSArrlkCNVRGS------VGRPLPGTEI 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6255 YIVDSKL-SLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRI-DEQVKI 6332
Cdd:cd17640   276 KIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWF------NTGDLGWLTCGGELVLTGRAkDTIVLS 349
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 386647928 6333 RGYRIELGEIEEQLLKVASVKEAtVIVREDesgQKQLCAYFVAERE 6378
Cdd:cd17640   350 NGENVEPQPIEEALMRSPFIEQI-MVVGQD---QKRLGALIVPNFE 391
PRK08315 PRK08315
AMP-binding domain protein; Validated
2344-2823 2.27e-35

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 146.11  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2344 DKTIHQLFEEQAERIPDHPAVVFEGQQL--TYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGA 2421
Cdd:PRK08315   15 EQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2422 YVPIDPEYPEDRISYMLEDSSAQVLLAQRR---------LQE----------------RVSFAGTVVTVDDE-------- 2468
Cdd:PRK08315   95 LVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamLYElapelatcepgqlqsaRLPELRRVIFLGDEkhpgmlnf 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2469 QAYAGDGSN--------LESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRV---VQF----- 2532
Cdd:PRK08315  175 DELLALGRAvddaelaaRQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLcipVPLyhcfg 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2533 ------ASLSfdascwevfqtlfFGATLYIP--------TKETILDyqwfERYMSDNGITT---ATLpptyavylnpDHm 2595
Cdd:PRK08315  255 mvlgnlACVT-------------HGATMVYPgegfdplaTLAAVEE----ERCTALYGVPTmfiAEL----------DH- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2596 PDFKRL--------IAAGSASSLELLQQWKDKvkyFN------AYGPTEDS--ICTTiwtpSTEDISQLKSVPIGGPIVN 2659
Cdd:PRK08315  307 PDFARFdlsslrtgIMAGSPCPIEVMKRVIDK---MHmsevtiAYGMTETSpvSTQT----RTDDPLEKRVTTVGRALPH 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2660 HRIYIVDAHY-QPVPVGVAGELCIAGVGLARGYLNRPDLTAEKfVDnpfepGERMYRTGDLAKWLPDGTIEYLGRIDHQV 2738
Cdd:PRK08315  380 LEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-ID-----ADGWMHTGDLAVMDEEGYVNIVGRIKDMI 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2739 kIRG----Y-RielgEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGELPGYMIPAHFVQ 2811
Cdd:PRK08315  454 -IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIlrPGATLTEEDVRDFCRGKIAHYKIPRYIRF 528
                         570
                  ....*....|..
gi 386647928 2812 LERMPLTPNGKI 2823
Cdd:PRK08315  529 VDEFPMTVTGKI 540
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
286-747 2.43e-35

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 142.87  E-value: 2.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGtqvllsqg 365
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  366 hlqervsfsgtwIRLDDeeayhedgsnlesvngpehLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTNY-IDVTGQDK-L 443
Cdd:cd05912    74 ------------VKLDD-------------------IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALnLGLTEDDNwL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  444 LQLSSYSFDGSTFdIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPD-CLRHARAILFGG 522
Cdd:cd05912   123 CALPLFHISGLSI-LMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEgYPNNLRCILLGG 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  523 ERVSVSHVRKALGHLGPgkIKHVYGPTE--STVFATSYDVHEVEEGAVsipiGGPISNTAIYIVNAqnkLQPIGVAGELC 600
Cdd:cd05912   199 GPAPKPLLEQCKEKGIP--VYQSYGMTEtcSQIVTLSPEDALNKIGSA----GKPLFPVELKIEDD---GQPPYEVGEIL 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  601 VAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIE 680
Cdd:cd05912   270 LKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIK 342
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  681 KATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05912   343 EAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
PRK06145 PRK06145
acyl-CoA synthetase; Validated
2355-2828 2.82e-35

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 144.64  E-value: 2.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRI 2434
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 SYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQ-------AYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEH 2507
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAqadsrrlAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSY 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2508 HGLC--SLKQMFAntLQINAQDRVVQFASLSFDASC-WEVFQTLFFGATLYIptkETILDYQWFERYMSDNGITTATLPP 2584
Cdd:PRK06145  172 GNLHwkSIDHVIA--LGLTASERLLVVGPLYHVGAFdLPGIAVLWVGGTLRI---HREFDPEAVLAAIERHRLTCAWMAP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2585 --TYAVYLNPDH----MPDFKRLIAAGSASSLELLQQWKD---KVKYFNAYGPTEDSICTTIWTPSTEdISQLKSVpiGG 2655
Cdd:PRK06145  247 vmLSRVLTVPDRdrfdLDSLAWCIGGGEKTPESRIRDFTRvftRARYIDAYGLTETCSGDTLMEAGRE-IEKIGST--GR 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2656 PIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermyRTGDLAKWLPDGTIEYLGRID 2735
Cdd:PRK06145  324 ALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLTDRKK 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2736 HQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGELPGYMIPAHFVQLE 2813
Cdd:PRK06145  397 DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlnPGATLTLEALDRHCRQRLASFKVPRQLKVRD 476
                         490
                  ....*....|....*
gi 386647928 2814 RMPLTPNGKIDRKAL 2828
Cdd:PRK06145  477 ELPRNPSGKVLKRVL 491
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
3400-3821 2.84e-35

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 143.33  E-value: 2.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3400 LTPMQKGMWFHNTLNRHGGAYieqtlfNV------RGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYrykPV 3473
Cdd:cd19540     4 LSFAQQRLWFLNRLDGPSAAY------NIplalrlTGALDVDALRAALADVVARHESLRTVFPED-DGGPYQVVL---PA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3474 EFAYEDLR--HLAEAEwsayLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESfHVL-WSFHHILMDGWCLPLIAKELFDT 3550
Cdd:cd19540    74 AEARPDLTvvDVTEDE----LAARLAEAARRGFDLTAELPLRARLFRLGPDE-HVLvLVVHHIAADGWSMAPLARDLATA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3551 YEAYLRNDLSERPAAP-SYSHYI----EWL---EKQDMEAAA--RYWTGFLAGYDSQTTLP-----------QGKLHnkd 3609
Cdd:cd19540   149 YAARRAGRAPDWAPLPvQYADYAlwqrELLgdeDDPDSLAARqlAYWRETLAGLPEELELPtdrprpavasyRGGTV--- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3610 gEYTeanilrsLGKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEiaGIEEMIGLFINTIP 3689
Cdd:cd19540   226 -EFT-------IDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDE--ALDDLVGMFVNTLV 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3690 VRVSCEAEQSFADVMKRVQEAALESggYD--------------------YYPLYEIqaqsaqkqdlithIMAFENFPmde 3749
Cdd:cd19540   296 LRTDVSGDPTFAELLARVRETDLAA--FAhqdvpferlvealnpprstaRHPLFQV-------------MLAFQNTA--- 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3750 qieqAGSYEDGKLAITDVDI-AEQTNYD--FTLVVMPGEE-----LAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19540   358 ----AATLELPGLTVEPVPVdTGVAKFDlsFTLTERRDADgapagLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1288-1701 2.86e-35

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 146.40  E-value: 2.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1288 PAAPDAPENEVFHALFEKQAERTPEVAAVVYEND----RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVG 1363
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1364 ALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQThlQERAQQWGQ------TLQAVLCLDDEA------------ 1425
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVED--QEQLDKLLEvrdelpSLRHIVVLDPRGlrddprllslde 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1426 --AYAEDASNVANVNE------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRL--LQLA-SFsf 1494
Cdd:COG1022   160 llALGREVADPAELEArraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsfLPLAhVF-- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1495 dvfvgdiART-----LYNGGTMVICPKDDRIDPArlhywISEEKITIFESTPAL-------II-------PFMDYVAEHG 1555
Cdd:COG1022   238 -------ERTvsyyaLAAGATVAFAESPDTLAED-----LREVKPTFMLAVPRVwekvyagIQakaeeagGLKRKLFRWA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1556 LDMS-SMELLITSSDSCSVTD-----------YRVLQERFGSQFR-----------------------IINAYGVTEAAi 1600
Cdd:COG1022   306 LAVGrRYARARLAGKSPSLLLrlkhaladklvFSKLREALGGRLRfavsggaalgpelarffralgipVLEGYGLTETS- 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1601 dsslydePLAklpeAGNVP-------IGKAALNAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPELTEEKFVDsp 1673
Cdd:COG1022   385 -------PVI----TVNRPgdnrigtVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA-- 441
                         490       500
                  ....*....|....*....|....*...
gi 386647928 1674 fvegERLYRTGDLARWMPDGNVDFIGRI 1701
Cdd:COG1022   442 ----DGWLHTGDIGELDEDGFLRITGRK 465
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
4843-5380 3.51e-35

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 146.18  E-value: 3.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4843 FEQLLTAIVNDPA----AKIASLGILTADEKAQIVhVFNPAAP------DAPENEAFHALfEKQAECTPEAAAVVYEND- 4911
Cdd:cd17634     1 YETKYRQSINDPDtfwgEAGKILDWITPYQKVKNT-SFAPGAPsikwfeDATLNLAANAL-DRHLRENGDRTAIIYEGDd 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 -----RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAAS 4986
Cdd:cd17634    79 tsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4987 VLLTQTHLQERAQ--------------------------------QWgqTLQAALCLDDEAAYAEDASNVANVNePHDLA 5034
Cdd:cd17634   159 LLITADGGVRAGRsvplkknvddalnpnvtsvehvivlkrtgsdiDW--QEGRDLWWRDLIAKASPEHQPEAMN-AEDPL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5035 YVIYTSGTTGRPKGVmiehrslVNTAAGYrreyrldqfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICP--------- 5105
Cdd:cd17634   236 FILYTSGTTGKPKGV-------LHTTGGY---------LVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSyllygplac 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5106 ---------KDDRIDPARLHYWISEEKITIFESTPALIIPFM----DYVAEHglDMSSMVLLITSSDSCSVTDYRVLQER 5172
Cdd:cd17634   300 gattllyegVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMaagdDAIEGT--DRSSLRILGSVGEPINPEAYEWYWKK 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5173 FGSQFR-IINAYGVTEA--AIDSSLYDEPLAKLPEAGNVPIGKAALnakfyIVDAHLNPVPVGVLGELCIGGI--GVARG 5247
Cdd:cd17634   378 IGKEKCpVVDTWWQTETggFMITPLPGAIELKAGSATRPVFGVQPA-----VVDNEGHPQPGGTEGNLVITDPwpGQTRT 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5248 YLNRPElteeKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED 5327
Cdd:cd17634   453 LFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPH 528
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5328 A-KGQK-----VLCAHFTAESELKlSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:cd17634   529 AiKGQApyayvVLNHGVEPSPELY-AELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK08316 PRK08316
acyl-CoA synthetase; Validated
5936-6420 3.62e-35

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 144.69  E-value: 3.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPI 6015
Cdd:PRK08316   12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6016 DPDYPEDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLND-------DGAYHEDG-------SNLEPVNGP------E 6075
Cdd:PRK08316   92 NFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTlilslvlGGREAPGGwldfadwAEAGSVAEPdveladD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTYVIYTSGTTGRPKGVMVEHRNVVrlvknTNYVelneqthilqtGAVV---FDASTFEIwGAL----------LNGGR 6142
Cdd:PRK08316  172 DLAQILYTSGTESLPKGAMLTHRALI-----AEYV-----------SCIVagdMSADDIPL-HALplyhcaqldvFLGPY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6143 LYVVRNETILDAVSLKN---AIQQYGIN------TMW---LTAPLYNQ--LSqqdsgmfaGLKTLIVGGDVLSVPHINRV 6208
Cdd:PRK08316  235 LYVGATNVILDAPDPELilrTIEAERITsffappTVWislLRHPDFDTrdLS--------SLRKGYYGASIMPVEVLKEL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6209 LREHAGLSIVNGYGPTEnttFSTTHTIVG--EQKE-AVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLN 6285
Cdd:PRK08316  307 RERLPGLRFYNCYGQTE---IAPLATVLGpeEHLRrPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWD 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6286 RPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESG 6365
Cdd:PRK08316  384 DPEKTAEAFRGGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKW 456
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 6366 QKQLCAYFV--AERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK08316  457 IEAVTAVVVpkAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
4890-5387 5.29e-35

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 145.71  E-value: 5.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4890 HALFEKQAECTPEAAAVVYENDR-----LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAY 4964
Cdd:cd05968    64 EQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4965 VPLDPDYPSDRIQFMLEDSAASVLLTQ-------------THLQERAQQWGQTLQAA----LCLDDEAAYAEDAS----- 5022
Cdd:cd05968   144 VPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQCPTVEKVVvvrhLGNDFTPAKGRDLSydeek 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5023 ----NVANVNEPHDLAYVIYTSGTTGRPKGVmiehrslVNTAAGyrreyrldqFPVRLLQLASFSFDVFVGD-------- 5090
Cdd:cd05968   224 etagDGAERTESEDPLMIIYTSGTTGKPKGT-------VHVHAG---------FPLKAAQDMYFQFDLKPGDlltwftdl 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5091 --------IARTLYNGGTMVI---CPkdDRIDPARLHYWISEEKITIFESTPALIIPFM----DYVAEHGLdmSSMVLLI 5155
Cdd:cd05968   288 gwmmgpwlIFGGLILGATMVLydgAP--DHPKADRLWRMVEDHEITHLGLSPTLIRALKprgdAPVNAHDL--SSLRVLG 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5156 TSSDSCSVTDYRVLQE-RFGSQFRIINAYGVTEAA--IDSSLYDEPLAKLPEAGNVPIGKAAlnakfyIVDAHLNPVPvG 5232
Cdd:cd05968   364 STGEPWNPEPWNWLFEtVGKGRNPIINYSGGTEISggILGNVLIKPIKPSSFNGPVPGMKAD------VLDESGKPAR-P 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5233 VLGELCIGG--IGVARGYLNrpelTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETq 5310
Cdd:cd05968   437 EVGELVLLApwPGMTRGFWR----DEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIES- 511
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5311 LLKAEGVREAVVV--VREDAKGQKVLCahFT------AESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 5382
Cdd:cd05968   512 VLNAHPAVLESAAigVPHPVKGEAIVC--FVvlkpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589

                  ....*
gi 386647928 5383 KALPA 5387
Cdd:cd05968   590 RVIRA 594
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
2347-2830 5.38e-35

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 145.71  E-value: 5.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2347 IHQLFEEQAERIPDHPAVVFEGQQ-----LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGA 2421
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2422 YVPIDPEYPEDRISYMLEDSSAQVLLAQ----RR---------LQERVSFAGTVVTV--------------------DDE 2468
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITAdgftRRgrevnlkeeADKACAQCPTVEKVvvvrhlgndftpakgrdlsyDEE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2469 QAYAGDGSnleSAVGPNDLAYIIYTSGTTGKPKGVmVEHHGLCSLKQMFANTLQINAQ--DRVVQFASLSFDASCWEVFQ 2546
Cdd:cd05968   223 KETAGDGA---ERTESEDPLMIIYTSGTTGKPKGT-VHVHAGFPLKAAQDMYFQFDLKpgDLLTWFTDLGWMMGPWLIFG 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2547 TLFFGATLYI-------PTKETIldyqWfeRYMSDNGITTATLPPTYAVYLnpdhMPDFKRLIAAGSASSLELL----QQ 2615
Cdd:cd05968   299 GLILGATMVLydgapdhPKADRL----W--RMVEDHEITHLGLSPTLIRAL----KPRGDAPVNAHDLSSLRVLgstgEP 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2616 W-------------KDKVKYFNAYGPTEDS---ICTTIwtpstedISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVaGE 2679
Cdd:cd05968   369 WnpepwnwlfetvgKGRNPIINYSGGTEISggiLGNVL-------IKPIKPSSFNGPVPGMKADVLDESGKPARPEV-GE 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2680 LCIAG--VGLARGYLNRPDltaeKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKV 2757
Cdd:cd05968   441 LVLLApwPGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAH 516
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 2758 ASVQEAIVIA-HDDASGQKQLCAYFVADRTMTVGELRGEL----SGELPGYMIPAHFVQLERMPLTPNGKIDRKALPA 2830
Cdd:cd05968   517 PAVLESAAIGvPHPVKGEAIVCFVVLKPGVTPTEALAEELmervADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1901-2312 5.51e-35

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 141.82  E-value: 5.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1901 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN-GEPVQRVYKEVNFAV-E 1978
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVtE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1979 HYRTSEAEAGEVVRGFV-----RTFDLAKPPLLRVGLVELAEDLHILL-LDMHHIVSDGMSTDVLTEEFGRLYNG----- 2047
Cdd:cd19536    82 LDLTPLEEQLDPLRAYKeetkiRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQlleyk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2048 -ESLATlRIQYKDYAVWQQSEEQLErvkRQEAYWLDMFRG-ELPVLEmptdYPRPAVRRFEGSTLSFRLDAGLNEALKRV 2125
Cdd:cd19536   162 pLSLPP-AQPYRDFVAHERASIQQA---ASERYWREYLAGaTLATLP----ALSEAVGGGPEQDSELLVSVPLPVRSRSL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2126 AAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTHG--DLQPLIGMFVNTLAIRnYPAGGKTFRSFLEEVKETTL 2203
Cdd:cd19536   234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEttGAERLLGLFLNTLPLR-VTLSEETVEDLLKRAQEQEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2204 GAYEHQTYPFEELveklqvPRDLSRNPIFDAMFVLQNtENEELQLDGLKLAPYPSGNTI-ARFDLTLD----VTETGSGL 2278
Cdd:cd19536   313 ESLSHEQVPLADI------QRCSEGEPLFDSIVNFRH-FDLDFGLPEWGSDEGMRRGLLfSEFKSNYDvnlsVLPKQDRL 385
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 2279 ECNLEYATSLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19536   386 ELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6994-7412 6.15e-35

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 142.01  E-value: 6.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6994 PM---QKGMWF-HTAL-DKEAgaYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSG-PRGEplQIVYRDKRIGF 7067
Cdd:cd20483     3 PMstfQRRLWFlHNFLeDKTF--LNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGdDFGE--QQVLDDPSFHL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7068 VYEDLSHlpADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYV 7147
Cdd:cd20483    79 IVIDLSE--AADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7148 QGDRPEQKAAPAYsQYIE-------WLENQDSAAASAYWSNYLAGYEGQTA-LPQEKAqKRSEGYVAEHVVCE--LDKEL 7217
Cdd:cd20483   157 AGRDLATVPPPPV-QYIDftlwhnaLLQSPLVQPLLDFWKEKLEGIPDASKlLPFAKA-ERPPVKDYERSTVEatLDKEL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7218 SERMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAeiPGIEEMIGLFINTIPVRVACQPEESFADVMG 7297
Cdd:cd20483   235 LARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7298 RMQEAALESGRYDFYPL-YEIQTQSAQKQEliNHLLVFE---NYPMDEQVEQAggdDSGTLSITDVDvaeHTN------Y 7367
Cdd:cd20483   313 STKTTCLEAYEHSAVPFdYIVDALDVPRST--SHFPIGQiavNYQVHGKFPEY---DTGDFKFTDYD---HYDiptacdI 384
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 7368 NFTVTVFPGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVAD 7412
Cdd:cd20483   385 ALEAEEDPDGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
6082-6417 7.77e-35

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 139.72  E-value: 7.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6082 YTSGTTGRPKGVMVEHRNVVrlvKNTNYV----ELNEQT---------HILqtGAVVfdastfEIWGALLNGGRlyVVRN 6148
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIV---NNGYFIgerlGLTEQDrlcipvplfHCF--GSVL------GVLACLTHGAT--MVFP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6149 ETILDAVSLKNAIQQ------YGINTMWLtaplyNQLSQQDSGMF--AGLKTLIVGGDVLSVPHINRVLREHAGLSIVNG 6220
Cdd:cd05917    76 SPSFDPLAVLEAIEKekctalHGVPTMFI-----AELEHPDFDKFdlSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6221 YGPTENTTFSTTHTIVGEQ-KEAVPIGKPINNSTAYIVDSK-LSLLPVGVWGELIVGGDGVARGYLNRPELTAEKfvess 6298
Cdd:cd05917   151 YGMTETSPVSTQTRTDDSIeKRVNTVGRIMPHTEAKIVDPEgGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA----- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6299 fLPGERCYRTGDLARWLPDGTLEYKGRIDEQVkIRG-YRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFV--A 6375
Cdd:cd05917   226 -IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRlkE 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 386647928 6376 ERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDR 6417
Cdd:cd05917   304 GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
1323-1795 8.86e-35

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 141.33  E-value: 8.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGgayvpldpdypsdriqfmledsaASVLLTQT 1402
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLG-----------------------AEAVLLNT 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 HL--QERAQQwgqtlqavlcLDDEAAYAEDAsnvanvnephdlAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLD 1480
Cdd:cd05912    59 RLtpNELAFQ----------LKDSDVKLDDI------------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1481 Q-----FPVRLLQLASFSFdvfvgdIARTLYNGGTMVICpkdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHg 1555
Cdd:cd05912   117 EddnwlCALPLFHISGLSI------LMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEG- 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1556 lDMSSMELLITSSDSCSVTDYRVLQERfgsQFRIINAYGVTEAA--IDSSLYDEPLAKLPEAGnvpigKAALNAKFYIVD 1633
Cdd:cd05912   187 -YPNNLRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAG-----KPLFPVELKIED 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1634 AHLNPVPVGvlgELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIE 1713
Cdd:cd05912   258 DGQPPYEVG---EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIY 327
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1714 TGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRK 1793
Cdd:cd05912   328 PAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRH 407

                  ..
gi 386647928 1794 AL 1795
Cdd:cd05912   408 EL 409
PRK06145 PRK06145
acyl-CoA synthetase; Validated
3864-4337 9.62e-35

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 143.10  E-value: 9.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRI 3943
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 RYMLEDSGAQALLTQRHLRERVSFaGTFVAVDDEQAyHADGSNLEP---------VVGPNHLAYVIYTSGTTGKPKGVMV 4014
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVAL-ETPKIVIDAAA-QADSRRLAQggleippqaAVAPTDLVRLMYTSGTTDRPKGVMH 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4015 EHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASC-WEIFKALFFGATLYIPTSttiLDYPLFESYMNENGITATILPP 4093
Cdd:PRK06145  170 SYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFdLPGIAVLWVGGTLRIHRE---FDPEAVLAAIERHRLTCAWMAP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4094 TYAAYL----NPDR--MPSLKKLITGGSAASVEFVQQWKD---KVLYFNAYGPTEaSIVTSIWDEASDSLgdRKSVPIGR 4164
Cdd:PRK06145  247 VMLSRVltvpDRDRfdLDSLAWCIGGGEKTPESRIRDFTRvftRARYIDAYGLTE-TCSGDTLMEAGREI--EKIGSTGR 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4165 PLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermyRTGDlVRWLPDGNLEYL-GRI 4243
Cdd:PRK06145  324 ALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGD-VGYLDEEGFLYLtDRK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4244 DHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV--AQRELTAAELRATMSQELPNYMIPSYFVQL 4321
Cdd:PRK06145  396 KDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlnPGATLTLEALDRHCRQRLASFKVPRQLKVR 475
                         490
                  ....*....|....*.
gi 386647928 4322 AQMPLTPNGKIDRKAL 4337
Cdd:PRK06145  476 DELPRNPSGKVLKRVL 491
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
7588-7928 9.91e-35

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 138.62  E-value: 9.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7588 LAYVIYTSGTTGKPKGVMVEHHGLcslkLMFAETLRiteedrvvqfASLSFDAS-CW-------------EIFKALFFGA 7653
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANL----LASAAGLH----------SRLGFGGGdSWllslplyhvgglaILVRSLLAGA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7654 TLYIPAKDtildyPLFESYMNENGITAAILPPTYAIYL-----SPDRLPSLKKLITGGSAASVEFVQQWKDK-VRYFNAY 7727
Cdd:cd17630    68 ELVLLERN-----QALAEDLAPPGVTHVSLVPTQLQRLldsgqGPAALKSLRAVLLGGAPIPPELLERAADRgIPLYTTY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7728 GPTEASIVTSVWAasPDGLDLRSVpiGRPIANHQIFIVDsqnhmlpvgvAGELCISGAGLARGYLNRPELtaekfvdnPF 7807
Cdd:cd17630   143 GMTETASQVATKR--PDGFGRGGV--GVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQLV--------PE 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7808 LAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADREL 7887
Cdd:cd17630   201 FNEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 386647928 7888 TVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd17630   281 DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
2344-2825 1.27e-34

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 143.76  E-value: 1.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2344 DKTIHQLFEEQAERIPDHPAVVF--EGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGA 2421
Cdd:PRK12583   17 TQTIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2422 YVPIDPEYPEDRISYMLEDSSAQVL-----------------------LAQR---------RLQERVSFAGTV---VTVD 2466
Cdd:PRK12583   97 LVNINPAYRASELEYALGQSGVRWVicadafktsdyhamlqellpglaEGQPgalacerlpELRGVVSLAPAPppgFLAW 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2467 DEQAYAGDGSNLE------SAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQ-------FA 2533
Cdd:PRK12583  177 HELQARGETVSREalaerqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVpvplyhcFG 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2534 SLSFDASCWEVfqtlffGATLYIPTKEtiLDYQWFERYMSDNGITTATLPPTYAVyLNPDHmPDFKRL--------IAAG 2605
Cdd:PRK12583  257 MVLANLGCMTV------GACLVYPNEA--FDPLATLQAVEEERCTALYGVPTMFI-AELDH-PQRGNFdlsslrtgIMAG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2606 SASSLELLQQWKDKVKYFN---AYGPTEDSICTTIWTPstEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCI 2682
Cdd:PRK12583  327 APCPIEVMRRVMDEMHMAEvqiAYGMTETSPVSLQTTA--ADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2683 AGVGLARGYLNRPDLTAEKFVDNPFepgerMYrTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQE 2762
Cdd:PRK12583  405 RGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVAD 478
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 2763 AIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDR 2825
Cdd:PRK12583  479 VQVFGVPDEKYGEEIVAWVRlhPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
285-747 1.68e-34

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 140.69  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  285 QLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSq 364
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  365 ghlqervsfsgtwirlddeeayhedGSNLESvngpehLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDKL 443
Cdd:cd05935    80 -------------------------GSELDD------LALIPYTSGTTGLPKGCMHTHFSAAaNALQSAVWTGLTPSDVI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  444 LQLSSY----SFDGStfdIFGALLNGAKLVLVpkeTVLDVAKLAGLIEKQQISVMF-ITTAFFNVLVDMN--PDCLRHAR 516
Cdd:cd05935   129 LACLPLfhvtGFVGS---LNTAVYVGGTYVLM---ARWDRETALELIEKYKVTFWTnIPTMLVDLLATPEfkTRDLSSLK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  517 AILFGGERVSVSHVRKALGHLGpgkIKHV--YGPTESTVFATSYDVHEVEEGAVSIPIggpiSNTAIYIVNAQN-KLQPI 593
Cdd:cd05935   203 VLTGGGAPMPPAVAEKLLKLTG---LRFVegYGLTETMSQTHTNPPLRPKLQCLGIP*----FGVDARVIDIETgRELPP 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  594 GVAGELCVAGDGLARGYLNRPDLTAEKFADNPfapGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHL 673
Cdd:cd05935   276 NEVGEIVVRGPQIFKGYWNRPEETEESFIEIK---GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  674 LKLEAIEKATVVVRESANGEKQLCAYYVADrslpaNEVRSTLSQE---------LPAYMLPSYFVQLEQMPLTTNGKVDR 744
Cdd:cd05935   353 YKHPAI*EVCVISVPDERVGEEVKAFIVLR-----PEYRGKVTEEdiiewareqMAAYKYPREVEFVDELPRSASGKILW 427

                  ...
gi 386647928  745 RAL 747
Cdd:cd05935   428 RLL 430
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
7472-7891 1.91e-34

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 142.37  E-value: 1.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQR 7551
Cdd:cd05904    33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 HLQECV-SFDGKVI----------AADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAE 7620
Cdd:cd05904   113 ELAEKLaSLALPVVlldsaefdslSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7621 TLRITEEDRVVQFASLSFdascWEIFKALFF-------GATLYIPAKdtiLDYPLFESYMNENGIT-AAILPPTY-AIYL 7691
Cdd:cd05904   193 GEGSNSDSEDVFLCVLPM----FHIYGLSSFalgllrlGATVVVMPR---FDLEELLAAIERYKVThLPVVPPIVlALVK 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7692 SPD----RLPSLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEAS-IVTSVwaASPDGLDLRSVPIGRPIANHQIF 7763
Cdd:cd05904   266 SPIvdkyDLSSLRQIMSGAAPLGKELIEAFRAKfpnVDLGQGYGMTESTgVVAMC--FAPEKDRAKYGSVGRLVPNVEAK 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7764 IVD-SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRIDHQVKIRG 7842
Cdd:cd05904   344 IVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWL------HTGDLCYIDEDGYLFIVDRLKELIKYKG 417
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 7843 YRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSE 7891
Cdd:cd05904   418 FQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE 466
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
2366-2828 1.93e-34

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 142.09  E-value: 1.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2366 FEGQQLTYRELNERANRLARTLQAlGVKTDQPVGLMLERSLEMVVGMFAVLKAGgaYVPIDPEYP--EDRISYMLEDSSA 2443
Cdd:cd05909     3 TLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2444 QVLLAQRRLQER--------VSFAGTVVTVDDEQAYAGDGSNLESAVG------------------PNDLAYIIYTSGTT 2497
Cdd:cd05909    80 KTVLTSKQFIEKlklhhlfdVEYDARIVYLEDLRAKISKADKCKAFLAgkfppkwllrifgvapvqPDDPAVILFTSGSE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2498 GKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQ----FASLSFDASCWEVFQTLFFGATLYIPtketiLDYQWFERYMS 2573
Cdd:cd05909   160 GLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGCLWLPLLSGIKVVFHPNP-----LDYKKIPELIY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2574 DNGIT----TATLPPTYAVYLNPDhmpDFKRL---IAAGSASSLELLQQWKDK--VKYFNAYGPTEDSICTTIWTPSTED 2644
Cdd:cd05909   235 DKKATillgTPTFLRGYARAAHPE---DFSSLrlvVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSPVISVNTPQSPN 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2645 isqlKSVPIGGPI--VNHRIYIVDAHyQPVPVGVAGELCIAGVGLARGYLNRPDLTAekfvdnpFEPGERMYRTGDLAKW 2722
Cdd:cd05909   312 ----KEGTVGRPLpgMEVKIVSVETH-EEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKI 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2723 LPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQ-EAIVIAHDDAS-GQKQLCAYFvaDRTMTVGELRGEL-SGE 2799
Cdd:cd05909   380 DGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRkGEKIVLLTT--TTDTDPSSLNDILkNAG 457
                         490       500
                  ....*....|....*....|....*....
gi 386647928 2800 LPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05909   458 ISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1440-1792 1.99e-34

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 138.56  E-value: 1.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1440 PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA--AGYRREYRLDQ---FPVRLLQlasfSFDVFVGDIARTLYnGGTMVic 1514
Cdd:cd05917     1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGyfIGERLGLTEQDrlcIPVPLFH----CFGSVLGVLACLTH-GATMV-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1515 PKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFG-SQFRIinAY 1593
Cdd:cd05917    74 FPSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTI--AY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1594 GVTEAA--IDSSLYDEPlaklPEAGNVPIGKAALNAKFYIVDAHLNPVP-VGVLGELCIGGIGVARGYLNRPELTEEKfv 1670
Cdd:cd05917   152 GMTETSpvSTQTRTDDS----IEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEA-- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1671 dspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAkIRG-YRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAY-- 1747
Cdd:cd05917   226 ----IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWir 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 1748 FTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 1792
Cdd:cd05917   301 LKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
3864-4332 3.17e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 142.41  E-value: 3.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKSQLTYGELNERANRLARTL-RDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDR 3942
Cdd:PRK08314   20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3943 IRYMLEDSGAQALLTQRHLRERV---------------SFAGTF------------------VAVDDEQAYH---ADGSN 3986
Cdd:PRK08314  100 LAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaQYSDYLpaepeiavpawlraepplQALAPGGVVAwkeALAAG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3987 LEP---VVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASL--------SFDAscweifk 4055
Cdd:PRK08314  180 LAPpphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLfhvtgmvhSMNA------- 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4056 ALFFGATLYIptsTTILDYPLFESYMNENGITATILPPTYAAYL--NPD----RMPSLkKLITGGSAASVEFV-QQWKDK 4128
Cdd:PRK08314  253 PIYAGATVVL---MPRWDREAAARLIERYRVTHWTNIPTMVVDFlaSPGlaerDLSSL-RYIGGGGAAMPEAVaERLKEL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4129 --VLYFNAYGPTEAsivtsiwdeASDSLGDRKSVP----IGRPLANHRIYVVD-SHNRMLPVGVAGELCISGVGLARGYL 4201
Cdd:PRK08314  329 tgLDYVEGYGLTET---------MAQTHSNPPDRPklqcLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYW 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4202 NRPELTAEKFVDnpFEpGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN 4281
Cdd:PRK08314  400 NRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPR 476
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 4282 GQQQLVAYFV----AQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK08314  477 RGETVKAVVVlrpeARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1301-1792 4.92e-34

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 142.22  E-value: 4.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1301 ALFEKQAERTPEVAAVVYEND--RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 1378
Cdd:PRK12583   22 DAFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNIN 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1379 PDYPSDRIQFMLEDSAASVLLT---------QTHLQERAQQWGQT------------LQAVLCLDDEA-----AYAE--- 1429
Cdd:PRK12583  102 PAYRASELEYALGQSGVRWVICadafktsdyHAMLQELLPGLAEGqpgalacerlpeLRGVVSLAPAPppgflAWHElqa 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1430 --DASNVANVNE------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ-----FPVRLLQlasfSFDV 1496
Cdd:PRK12583  182 rgETVSREALAErqasldRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEhdrlcVPVPLYH----CFGM 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1497 FVGDIArTLYNGGTMVIcpKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDY 1576
Cdd:PRK12583  258 VLANLG-CMTVGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVM 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1577 -RVLQERFGSQFRIinAYGVTEAA--IDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIG 1653
Cdd:PRK12583  335 rRVMDEMHMAEVQI--AYGMTETSpvSLQTTAADDLERRVET----VGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1654 VARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVV 1733
Cdd:PRK12583  409 VMKGYWNNPEATAES------IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 1734 VREDAKGQKVLCAYFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 1792
Cdd:PRK12583  483 GVPDEKYGEEIVAWVRLHPGHAASeeELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1307-1686 5.22e-34

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 141.61  E-value: 5.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVY------ENDRLTYRELNERANRLARMLRAQGvKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 1380
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1381 YPS---DRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQA----VLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTT 1453
Cdd:cd05931    82 TPGrhaERLAAILADAGPRVVLTTAAALAAVRAFAASRPAagtpRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1454 GRPKGVMIEHRSLVNTAAGYRREYRLDqfpvrllqlasfSFDVFV------------GDIARTLYNGGTMVICPKDDRI- 1520
Cdd:cd05931   162 GTPKGVVVTHRNLLANVRQIRRAYGLD------------PGDVVVswlplyhdmgliGGLLTPLYSGGPSVLMSPAAFLr 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1521 DPARLHYWISEEKITIfesTPAliiP-F-MDYVAEH-------GLDMSSMELLITSSDSCSVTDYRVLQERF-GSQFR-- 1588
Cdd:cd05931   230 RPLRWLRLISRYRATI---SAA---PnFaYDLCVRRvrdedleGLDLSSWRVALNGAEPVRPATLRRFAEAFaPFGFRpe 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1589 -IINAYGVTEAAI-----------------DSSLYDEPLAKLPEAGN----VPIGKAALNAKFYIVDA-HLNPVPVGVLG 1645
Cdd:cd05931   304 aFRPSYGLAEATLfvsggppgtgpvvlrvdRDALAGRAVAVAADDPAarelVSCGRPLPDQEVRIVDPeTGRELPDGEVG 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 386647928 1646 ELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDL 1686
Cdd:cd05931   384 EIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDL 424
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
4897-5276 5.98e-34

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 141.61  E-value: 5.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4897 AECTPEAAAVVY------ENDRLTYRELNERANRLARTLRAQGvKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 4970
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4971 YPS---DRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAA----LCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTT 5043
Cdd:cd05931    82 TPGrhaERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAgtprLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5044 GRPKGVMIEHRSLVNTAAGYRREYRLDqfpvrllqlasfSFDVFV------------GDIARTLYNGGTMVICPKDDRI- 5110
Cdd:cd05931   162 GTPKGVVVTHRNLLANVRQIRRAYGLD------------PGDVVVswlplyhdmgliGGLLTPLYSGGPSVLMSPAAFLr 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5111 DPARLHYWISEEKITIfesTPAliiP-F-MDYVAEH-------GLDMSSMVLLITSSDSCSVTDYRVLQERF-GSQFR-- 5178
Cdd:cd05931   230 RPLRWLRLISRYRATI---SAA---PnFaYDLCVRRvrdedleGLDLSSWRVALNGAEPVRPATLRRFAEAFaPFGFRpe 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5179 -IINAYGVTEAAI-----------------DSSLYDEPLAKLPEAGN----VPIGKAALNAKFYIVDA-HLNPVPVGVLG 5235
Cdd:cd05931   304 aFRPSYGLAEATLfvsggppgtgpvvlrvdRDALAGRAVAVAADDPAarelVSCGRPLPDQEVRIVDPeTGRELPDGEVG 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 386647928 5236 ELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDL 5276
Cdd:cd05931   384 EIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDL 424
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
4913-5385 6.77e-34

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 138.63  E-value: 6.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGgayvpldpdypsdriqfmledsaASVLLTQT 4992
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLG-----------------------AEAVLLNT 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 HL--QERAQQwgqtlqaalcLDDEAAYAEDAsnvanvnephdlAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLD 5070
Cdd:cd05912    59 RLtpNELAFQ----------LKDSDVKLDDI------------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5071 Q-----FPVRLLQLASFSFdvfvgdIARTLYNGGTMVICpkdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHG 5145
Cdd:cd05912   117 EddnwlCALPLFHISGLSI------LMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGY 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5146 LDMSSMVLLitSSDSCSVTDYRVLQERfgsQFRIINAYGVTEAA--IDSSLYDEPLAKLPEAGnvpigKAALNAKFYIVD 5223
Cdd:cd05912   188 PNNLRCILL--GGGPAPKPLLEQCKEK---GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAG-----KPLFPVELKIED 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5224 AHLNPVPVGvlgELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIE 5303
Cdd:cd05912   258 DGQPPYEVG---EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIY 327
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5304 TGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRK 5383
Cdd:cd05912   328 PAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRH 407

                  ..
gi 386647928 5384 AL 5385
Cdd:cd05912   408 EL 409
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1253-1790 6.85e-34

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 141.95  E-value: 6.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1253 FEQLLTAIVNNPA----AKIASLGILTVEEKAQLVhVFNPAAP------DAPENEVFHALfEKQAERTPEVAAVVYEND- 1321
Cdd:cd17634     1 YETKYRQSINDPDtfwgEAGKILDWITPYQKVKNT-SFAPGAPsikwfeDATLNLAANAL-DRHLRENGDRTAIIYEGDd 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 -----RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAAS 1396
Cdd:cd17634    79 tsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1397 VLLTQTHLQER-------------AQQWGQTLQAVLCLD-----------------DEAAYAEDASNVANVNePHDLAYV 1446
Cdd:cd17634   159 LLITADGGVRAgrsvplkknvddaLNPNVTSVEHVIVLKrtgsdidwqegrdlwwrDLIAKASPEHQPEAMN-AEDPLFI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1447 IYTSGTTGRPKGVmiehrslVNTAAGYrreyrldqfPVRLLQLASFSFDVFVGDIARTLYNGGTMVICP----------- 1515
Cdd:cd17634   238 LYTSGTTGKPKGV-------LHTTGGY---------LVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSyllygplacga 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1516 -------KDDRIDPARLHYWISEEKITIFESTPALIIPFM----DYVAEHglDMSSMELLITSSDSCSVTDYRVLQERFG 1584
Cdd:cd17634   302 ttllyegVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMaagdDAIEGT--DRSSLRILGSVGEPINPEAYEWYWKKIG 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1585 SQFR-IINAYGVTEA--AIDSSLYDEPLAKLPEAGNVPIGKAALnakfyIVDAHLNPVPVGVLGELCIGGI--GVARGYL 1659
Cdd:cd17634   380 KEKCpVVDTWWQTETggFMITPLPGAIELKAGSATRPVFGVQPA-----VVDNEGHPQPGGTEGNLVITDPwpGQTRTLF 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1660 NRPElteeKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA- 1738
Cdd:cd17634   455 GDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAi 530
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1739 KGQK-----VLCAYFTAESELKlSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:cd17634   531 KGQApyayvVLNHGVEPSPELY-AELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
3996-4337 6.89e-34

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 136.31  E-value: 6.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3996 LAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDR------VVQFASLSFdascweIFKALFFGATLYIPTST 4069
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSwllslpLYHVGGLAI------LVRSLLAGAELVLLERN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4070 tildyPLFESYMNENGITATILPPTYAAYL-----NPDRMPSLKKLITGGSAASVEFVQQWKDK-VLYFNAYGPTEASIV 4143
Cdd:cd17630    76 -----QALAEDLAPPGVTHVSLVPTQLQRLldsgqGPAALKSLRAVLLGGAPIPPELLERAADRgIPLYTTYGMTETASQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4144 TSIWDEASDSLGDrksvpIGRPLANHRIYVVDshnrmlpvgvAGELCISGVGLARGYLNRPEltaekfVDNPFEPGerMY 4223
Cdd:cd17630   151 VATKRPDGFGRGG-----VGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL------VPEFNEDG--WF 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4224 RTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRA 4303
Cdd:cd17630   208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRA 287
                         330       340       350
                  ....*....|....*....|....*....|....
gi 386647928 4304 TMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd17630   288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
407-744 6.93e-34

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 137.02  E-value: 6.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  407 YTSGTTGKPKGNLTTHRNIIrvvKNTNYI----DVTGQDKL-LQLSSYSFDGSTFDIFGALLNGAKLVLVpkETVLDVAK 481
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIV---NNGYFIgerlGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFP--SPSFDPLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  482 LAGLIEKQQISVMFIT-TAFFNVLVDMNPDC--LRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTEST--VFAT 556
Cdd:cd05917    84 VLEAIEKEKCTALHGVpTMFIAELEHPDFDKfdLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSpvSTQT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  557 SYDVhEVEEGAVSipIGGPISNTAIYIVNAQNKLQP-IGVAGELCVAGDGLARGYLNRPDLTAEKfadnpfAPGERMYRT 635
Cdd:cd05917   164 RTDD-SIEKRVNT--VGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGWLHT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  636 GDLARWLPDGTIEYVGRIDDQVkIRGFR-IELGEIEAHLLKLEAIEKATVV-VRESANGEkQLCAYYV--ADRSLPANEV 711
Cdd:cd05917   235 GDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVgVPDERYGE-EVCAWIRlkEGAELTEEDI 312
                         330       340       350
                  ....*....|....*....|....*....|...
gi 386647928  712 RSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDR 744
Cdd:cd05917   313 KAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
4878-5291 7.01e-34

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 142.16  E-value: 7.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4878 PAAPDAPENEAFHALFEKQAECTPEAAAVVYEND----RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVG 4953
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4954 ALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQThlQERAQQWGQ------TLQAALCLDDEA------------ 5015
Cdd:COG1022    82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVED--QEQLDKLLEvrdelpSLRHIVVLDPRGlrddprllslde 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5016 --AYAEDASNVANVNE------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRL--LQLA-SFsf 5084
Cdd:COG1022   160 llALGREVADPAELEArraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsfLPLAhVF-- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5085 dvfvgdiART-----LYNGGTMVICPKDDRIDPA-------------RLhyWiseEKI------TIFESTPALIIPFmDY 5140
Cdd:COG1022   238 -------ERTvsyyaLAAGATVAFAESPDTLAEDlrevkptfmlavpRV--W---EKVyagiqaKAEEAGGLKRKLF-RW 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5141 VAEHGLDMSsmvLLITSSDSCSVTD-----------YRVLQERFGSQFR-----------------------IINAYGVT 5186
Cdd:COG1022   305 ALAVGRRYA---RARLAGKSPSLLLrlkhaladklvFSKLREALGGRLRfavsggaalgpelarffralgipVLEGYGLT 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5187 EAAidsslydePLAklpeAGNVP-------IGKAALNAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPELTEEKF 5259
Cdd:COG1022   382 ETS--------PVI----TVNRPgdnrigtVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAF 439
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 5260 VDspfvegERLYRTGDLARWMPDGNVDFIGRI 5291
Cdd:COG1022   440 DA------DGWLHTGDIGELDEDGFLRITGRK 465
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
2371-2830 8.07e-34

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 139.17  E-value: 8.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQR 2450
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2451 RLQERVSfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVV 2530
Cdd:cd05969    81 ELYERTD--------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2531 QFASLSFDA-SCWEVFQTLFFGATLYIptKETILDYQ-WFERyMSDNGITTATLPPTyavylnpdhmpDFKRLIAAGSA- 2607
Cdd:cd05969   135 CTADPGWVTgTVYGIWAPWLNGVTNVV--YEGRFDAEsWYGI-IERVKVTVWYTAPT-----------AIRMLMKEGDEl 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2608 ------SSLELLQ-----------QWKDKVkyFNAygPTEDsictTIWTPSTED--ISQLKSVPI-----GGPIVNHRIY 2663
Cdd:cd05969   201 arkydlSSLRFIHsvgeplnpeaiRWGMEV--FGV--PIHD----TWWQTETGSimIANYPCMPIkpgsmGKPLPGVKAA 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2664 IVDAHYQPVPVGVAGELCI-AGV-GLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIR 2741
Cdd:cd05969   273 VVDENGNELPPGTKGILALkPGWpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTS 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2742 GYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGE-LRGELSG----ELPGYMIP--AHFVqlER 2814
Cdd:cd05969   346 GHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDeLKEEIINfvrqKLGAHVAPreIEFV--DN 423
                         490
                  ....*....|....*.
gi 386647928 2815 MPLTPNGKIDRKALPA 2830
Cdd:cd05969   424 LPKTRSGKIMRRVLKA 439
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1304-1790 8.20e-34

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 140.13  E-value: 8.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1304 EKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 1383
Cdd:cd12118    11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1384 DRIQFMLEDSAASVLLTQTHLQ-ERAQQWGQTLQAVLCLDDEaayaedasnvanvnepHDLAYVIYTSGTTGRPKGVMIE 1462
Cdd:cd12118    91 EEIAFILRHSEAKVLFVDREFEyEDLLAEGDPDFEWIPPADE----------------WDPIALNYTSGTTGRPKGVVYH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1463 HRS--LVNTAAGYrrEYRLDQFPVRLLQLASFSFD--VFVGDIARtlyNGGTMVICPKddrIDPARLHYWISEEKITIFE 1538
Cdd:cd12118   155 HRGayLNALANIL--EWEMKQHPVYLWTLPMFHCNgwCFPWTVAA---VGGTNVCLRK---VDAKAIYDLIEKHKVTHFC 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1539 STPALIIPFMDYVAEHGLDMSSMELLITSSdscSVTDYRVLQ--ERFGsqFRIINAYGVTEAAIDSSLydepLAKLPEAG 1616
Cdd:cd12118   227 GAPTVLNMLANAPPSDARPLPHRVHVMTAG---APPPAAVLAkmEELG--FDVTHVYGLTETYGPATV----CAWKPEWD 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1617 NVPIG-KAALNAK----------FYIVDAH-LNPVPV-GV-LGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyR 1682
Cdd:cd12118   298 ELPTEeRARLKARqgvryvgleeVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGGWF-------H 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1683 TGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAE--SELKLSELR 1760
Cdd:cd12118   371 SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKegAKVTEEEII 450
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 1761 SSLSQELPGYMIPSYFVQLEqLPLTANGKI 1790
Cdd:cd12118   451 AFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
PRK09088 PRK09088
acyl-CoA synthetase; Validated
7455-7928 8.70e-34

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 139.94  E-value: 8.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7455 QAERMPEKAAVV--FENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPE 7532
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7533 DRIRYMLEDSGAQVLLTQRHLQ----ECVSFDGKVIAADDEQAygedgsNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEH 7608
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVAagrtDVEDLAAFIASADALEP------ADTPSIPPERVSLILFTSGTSGQPKGVMLSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7609 HGLCSLKLMFAETLRITEEDRVVqfaslsFDASCWEIFkALFFGATLYIPAKDTILDYPLFESYMNEN-------GITAA 7681
Cdd:PRK09088  158 RNLQQTAHNFGVLGRVDAHSSFL------CDAPMFHII-GLITSVRPVLAVGGSILVSNGFEPKRTLGrlgdpalGITHY 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7682 ILPPTYAIYL------SPDRLPSLKKLITGGSAASVEFVQQWKDK-VRYFNAYGPTEASIVTSVwAASPDGLDLRSVPIG 7754
Cdd:PRK09088  231 FCVPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWLDDgIPMVDGFGMSEAGTVFGM-SVDCDVIRAKAGAAG 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7755 RPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFvdnpflAGERMYRTGDLARWLPDGNIEYLGRI 7834
Cdd:PRK09088  310 IPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGFFWVVDRK 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7835 DHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDAN-GQQQLCAYFVADR-ELTVSELRGTLSQELPGYMIPSYFVQL 7912
Cdd:PRK09088  384 KDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLAIVPADGaPLDLERIRSHLSTRLAKYKVPKHLRLV 463
                         490
                  ....*....|....*.
gi 386647928 7913 EQMPLTPNGKIDRNAL 7928
Cdd:PRK09088  464 DALPRTASGKLQKARL 479
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
2355-2742 9.19e-34

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 141.22  E-value: 9.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVF------EGQQLTYRELNERANRLARTLQALGvKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI-DP 2427
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2428 EYPE--DRISYMLEDSSAQVLLAQRRLQERV--------SFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTT 2497
Cdd:cd05931    82 TPGRhaERLAAILADAGPRVVLTTAAALAAVrafaasrpAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2498 GKPKGVMVEHHGLCS-LKQMFaNTLQINAQDRVVQFASL-------SFdascweVFQTLFFGATLYIPTKETILD--YQW 2567
Cdd:cd05931   162 GTPKGVVVTHRNLLAnVRQIR-RAYGLDPGDVVVSWLPLyhdmgliGG------LLTPLYSGGPSVLMSPAAFLRrpLRW 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2568 FERyMSDNGITTaTLPPTYA-----VYLNPDHMP--DFKRLIAAGSAS---SLELLQQWkdkVKYFNAYGPTEDSIC--- 2634
Cdd:cd05931   235 LRL-ISRYRATI-SAAPNFAydlcvRRVRDEDLEglDLSSWRVALNGAepvRPATLRRF---AEAFAPFGFRPEAFRpsy 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2635 ---------TTIW----------------------TPSTEDISQLKSVpiGGPIVNHRIYIVDA-HYQPVPVGVAGELCI 2682
Cdd:cd05931   310 glaeatlfvSGGPpgtgpvvlrvdrdalagravavAADDPAARELVSC--GRPLPDQEVRIVDPeTGRELPDGEVGEIWV 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2683 AGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAkWLPDGTIEYLGRIDHQVKIRG 2742
Cdd:cd05931   388 RGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRG 446
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
268-747 9.67e-34

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 140.46  E-value: 9.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  268 EQAER-RPDAVAVT----FEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMV---ERSLEMIVGIMGIlkaGGAYVP 339
Cdd:cd12119     3 EHAARlHGDREIVSrtheGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGM---GAVLHT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  340 IDPEYPEERIRYMLEDSGTQVLLSQGHLQ-------ERVSFSGTWIRLDDEEAYHEDGSN--------LESVNG------ 398
Cdd:cd12119    80 INPRLFPEQIAYIINHAEDRVVFVDRDFLplleaiaPRLPTVEHVVVMTDDAAMPEPAGVgvlayeelLAAESPeydwpd 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  399 -PEHLTYVI-YTSGTTGKPKGNLTTHRNII---RVVKNTNYIDVTGQDKLLQLSSYsFDGSTFDI-FGALLNGAKLVLVP 472
Cdd:cd12119   160 fDENTAAAIcYTSGTTGNPKGVVYSHRSLVlhaMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLPG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  473 KEtvLDVAKLAGLIEKQQISVMF-ITTAFFNVL--VDMNPDCLRHARAILFGGERVSVSHVRKALGHLGPgkIKHVYGPT 549
Cdd:cd12119   239 PY--LDPASLAELIEREGVTFAAgVPTVWQGLLdhLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVR--VIHAWGMT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  550 EST---VFATSYDVH----EVEEGAVSIPIGGPISNTAIYIVNAQNKLQPI-GVA-GELCVAGDGLARGYLNRPDLTAEK 620
Cdd:cd12119   315 ETSplgTVARPPSEHsnlsEDEQLALRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEAL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  621 FADNPFapgermyRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKQLcAY 699
Cdd:cd12119   395 TEDGWL-------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIgVPHPKWGERPL-AV 466
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928  700 YVA--DRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd12119   467 VVLkeGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
5932-6418 9.97e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 141.29  E-value: 9.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5932 PSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGA 6011
Cdd:PRK05605   29 YGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6012 YVPIDPDYPEDRIRYMLEDSGAKLLLVqghlLDR-ASFADKL-----------VNLND---------------------- 6057
Cdd:PRK05605  109 VVEHNPLYTAHELEHPFEDHGARVAIV----WDKvAPTVERLrrttpletivsVNMIAampllqrlalrlpipalrkara 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6058 ----------------DGAYHEDGSNLE-PVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVV-RLVKNTNYV-ELNEQTHI 6118
Cdd:PRK05605  185 altgpapgtvpwetlvDAAIGGDGSDVShPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQGKAWVpGLGDGPER 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6119 LQTGAVVFDA------STFeiwgALLNGGRLYV---VRNETILDAVSLKNAiqqygintMWLTA--PLYNQLSQ--QDSG 6185
Cdd:PRK05605  265 VLAALPMFHAygltlcLTL----AVSIGGELVLlpaPDIDLILDAMKKHPP--------TWLPGvpPLYEKIAEaaEERG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6186 M-FAGLKTLIVGGDVLSVpHINRVLREHAGLSIVNGYGPTEnttfsTTHTIVG----EQKEAVPIGKPINNSTAYIVDSK 6260
Cdd:PRK05605  333 VdLSGVRNAFSGAMALPV-STVELWEKLTGGLLVEGYGLTE-----TSPIIVGnpmsDDRRPGYVGVPFPDTEVRIVDPE 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6261 -LS-LLPVGVWGELIVGGDGVARGYLNRPELTAEkfvesSFLPGerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIE 6338
Cdd:PRK05605  407 dPDeTMPDGEEGELLVRGPQVFKGYWNRPEETAK-----SFLDG--WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVY 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6339 LGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGE--LRAALSQELPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:PRK05605  480 PAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVR 559

                  ..
gi 386647928 6417 RR 6418
Cdd:PRK05605  560 RR 561
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
5935-6420 1.14e-33

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 141.11  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5935 KTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLR-NAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYV 6013
Cdd:PRK12492   24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQqHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6014 PIDPDYPEDRIRYMLEDSGAKLL--------LVQGHLLD-------RASFADK-------LVNLNDDG------AYH--- 6062
Cdd:PRK12492  104 NTNPLYTAREMRHQFKDSGARALvylnmfgkLVQEVLPDtgieyliEAKMGDLlpaakgwLVNTVVDKvkkmvpAYHlpq 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6063 ----------EDGSNLEPVN-GPEHLTYVIYTSGTTGRPKGVMVEHRNvvrLVKNTNYVELNEQTH------ILQTGAVV 6125
Cdd:PRK12492  184 avpfkqalrqGRGLSLKPVPvGLDDIAVLQYTGGTTGLAKGAMLTHGN---LVANMLQVRACLSQLgpdgqpLMKEGQEV 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6126 FDAST--FEIWGALLNGGRLYVVRNETIL-----DAVSLKNAIQQY------GINTMWLTAPLYNQLSQQDsgmFAGLKT 6192
Cdd:PRK12492  261 MIAPLplYHIYAFTANCMCMMVSGNHNVLitnprDIPGFIKELGKWrfsallGLNTLFVALMDHPGFKDLD---FSALKL 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6193 LIVGGDVLSVPHINRvLREHAGLSIVNGYGPTENTTFSTTHTiVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGEL 6272
Cdd:PRK12492  338 TNSGGTALVKATAER-WEQLTGCTIVEGYGLTETSPVASTNP-YGELARLGTVGIPVPGTALKVIDDDGNELPLGERGEL 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6273 IVGGDGVARGYLNRPELTAEKfvessfLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLL---KV 6349
Cdd:PRK12492  416 CIKGPQVMKGYWQQPEATAEA------LDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMahpKV 489
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 6350 ASVkeATVIVREDESGQKqlCAYFVAERE--LTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK12492  490 ANC--AAIGVPDERSGEA--VKLFVVARDpgLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
5943-6420 1.74e-33

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 139.69  E-value: 1.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5943 EQAERI-PDHLAVT----FEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDP 6017
Cdd:cd12119     3 EHAARLhGDREIVSrtheGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6018 DYPEDRIRYMLEDSGAKLLLVQGHLL-------DRASFADKLVNLNDDGAYHEDGSN--------LEPVNG-------PE 6075
Cdd:cd12119    83 RLFPEQIAYIINHAEDRVVFVDRDFLplleaiaPRLPTVEHVVVMTDDAAMPEPAGVgvlayeelLAAESPeydwpdfDE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTYVI-YTSGTTGRPKGVMVEHRNVVrlvkntnyvelneqTH---ILQTGAVVFDAS--------TFEI--WG----AL 6137
Cdd:cd12119   163 NTAAAIcYTSGTTGNPKGVVYSHRSLV--------------LHamaALLTDGLGLSESdvvlpvvpMFHVnaWGlpyaAA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6138 LNGGRL-YVVRNetiLDAVSLKNAIQQY------GINTMWLTapLYNQLSQQDSGMFAgLKTLIVGGDVLSVPHINRVLR 6210
Cdd:cd12119   229 MVGAKLvLPGPY---LDPASLAELIEREgvtfaaGVPTVWQG--LLDHLEANGRDLSS-LRRVVIGGSAVPRSLIEAFEE 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6211 ehAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVP---------IGKPINNSTAYIVDSKLSLLPvgvW-----GELIVGG 6276
Cdd:cd12119   303 --RGVRVIHAWGMTETSPLGTVARPPSEHSNLSEdeqlalrakQGRPVPGVELRIVDDDGRELP---WdgkavGELQVRG 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6277 DGVARGYLNRPElTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEAT 6356
Cdd:cd12119   378 PWVTKSYYKNDE-ESEALTEDGWL------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAA 450
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 6357 VIVREDESGQKQLCAYFVA--ERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd12119   451 VIGVPHPKWGERPLAVVVLkeGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK07787 PRK07787
acyl-CoA synthetase; Validated
7461-7932 1.95e-33

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 138.58  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7461 EKAAVVFENTQLTYRELNERANRLARTLRAEGvqadqPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLE 7540
Cdd:PRK07787   15 IADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7541 DSGAQVLL--TQRHLQECVSFDGKVIAaddeqaygeDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMF 7618
Cdd:PRK07787   90 DSGAQAWLgpAPDDPAGLPHVPVRLHA---------RSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7619 AETLRITEEDRVVQ--------------FASLSFDASCWEIFK--------ALFFGATLYipakdtiLDYPLFESYMNEN 7676
Cdd:PRK07787  161 AEAWQWTADDVLVHglplfhvhglvlgvLGPLRIGNRFVHTGRptpeayaqALSEGGTLY-------FGVPTVWSRIAAD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7677 gitaailpPTYAIYLSPDRLpslkkLITGGSAASVEFVQQWKDKV--RYFNAYGPTEASIVTSVWAaspDGlDLRSVPIG 7754
Cdd:PRK07787  234 --------PEAARALRGARL-----LVSGSAALPVPVFDRLAALTghRPVERYGMTETLITLSTRA---DG-ERRPGWVG 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7755 RPIANHQIFIVDSQNHMLPVGVA--GELCISGAGLARGYLNRPELTAEKFVDNPFlagermYRTGDLARWLPDGNIEYLG 7832
Cdd:PRK07787  297 LPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVG 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7833 R--IDhQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFV 7910
Cdd:PRK07787  371 ResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPREVR 449
                         490       500
                  ....*....|....*....|..
gi 386647928 7911 QLEQMPLTPNGKIDRNALPAPE 7932
Cdd:PRK07787  450 FVDALPRNAMGKVLKKQLLSEG 471
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
3854-4334 2.17e-33

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 140.29  E-value: 2.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3854 QTIHGLFEEQALRNPDAVAVVFEKSQL--TYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAY 3931
Cdd:PRK12583   18 QTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3932 IPIDPEYPEDRIRYMLEDSGAQALLT-----------------------QR---------HLRERVSFAGT----FVAVD 3975
Cdd:PRK12583   98 VNINPAYRASELEYALGQSGVRWVICadafktsdyhamlqellpglaegQPgalacerlpELRGVVSLAPApppgFLAWH 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3976 DEQAyHADGSN---LEPVVGPNHLAYVI---YTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQ-------FA 4042
Cdd:PRK12583  178 ELQA-RGETVSreaLAERQASLDRDDPIniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVpvplyhcFG 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4043 SLSFDASCWEIFKALFFGATLYIPTSTtildyplFESYMNENGITATILPPTYAAYLN-PDR----MPSLKKLITGGSAA 4117
Cdd:PRK12583  257 MVLANLGCMTVGACLVYPNEAFDPLAT-------LQAVEEERCTALYGVPTMFIAELDhPQRgnfdLSSLRTGIMAGAPC 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4118 SVEFVQQWKD-----KVLYfnAYGPTEASIVtSIWDEASDSLgDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCIS 4192
Cdd:PRK12583  330 PIEVMRRVMDemhmaEVQI--AYGMTETSPV-SLQTTAADDL-ERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4193 GVGLARGYLNRPELTAEKFVDNPFepgerMYrTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEA 4272
Cdd:PRK12583  406 GYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4273 IVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDR 4334
Cdd:PRK12583  480 QVFGVPDEKYGEEIVAWVRLHpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
3398-3821 2.22e-33

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 137.12  E-value: 2.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3398 YALTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYKPVEFAY 3477
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTPVPIRH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3478 EDLRHLAEAEWSAylDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLRN 3557
Cdd:cd19533    81 IDLSGDPDPEGAA--QQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3558 DLSERPAAPSYSHYIEwlEKQDMEAAAR------YWTGFLAGydsqttLPQGKLHNKDGEYTEANILR---SLGKSLTER 3628
Cdd:cd19533   159 RPAPPAPFGSFLDLVE--EEQAYRQSERferdraFWTEQFED------LPEPVSLARRAPGRSLAFLRrtaELPPELTRT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3629 MSRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGR--SAEIagieEMIGLFINTIPVRVSCEAEQSFADVMKR 3706
Cdd:cd19533   231 LLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgAAAR----QTPGMVANTLPLRLTVDPQQTFAELVAQ 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3707 VQEAALESGGYDYYPLYEIQAQSAQKQDLITHIMAFENF-PMDEQIEQAGSYedgklAITDVDIAEQTNyDFTLVV---M 3782
Cdd:cd19533   307 VSRELRSLLRHQRYRYEDLRRDLGLTGELHPLFGPTVNYmPFDYGLDFGGVV-----GLTHNLSSGPTN-DLSIFVydrD 380
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 386647928 3783 PGEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19533   381 DESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
7456-7842 2.31e-33

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 139.68  E-value: 2.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVF------ENTQLTYRELNERANRLARTLRAEGVQADqPVGLMIERSLEMIVGAFAIMKAGGAYVPI-DP 7528
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7529 EYPE--DRIRYMLEDSGAQVLLTQ--------RHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTT 7598
Cdd:cd05931    82 TPGRhaERLAAILADAGPRVVLTTaaalaavrAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7599 GKPKGVMVEHHGLCS-LKLMFaETLRITEEDRVVQFASL-------SFdascweIFKALFFGATLYI---------PAK- 7660
Cdd:cd05931   162 GTPKGVVVTHRNLLAnVRQIR-RAYGLDPGDVVVSWLPLyhdmgliGG------LLTPLYSGGPSVLmspaaflrrPLRw 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7661 -DTILDYPLfesymnenGITAAilpPTYAIYLSPDR----------LPSLKKLITGG---SAASVE-FVQQWKDkvryFN 7725
Cdd:cd05931   235 lRLISRYRA--------TISAA---PNFAYDLCVRRvrdedlegldLSSWRVALNGAepvRPATLRrFAEAFAP----FG 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7726 --------AYGPTEAS-IVTSVWAASP--------DGLDLRSVPI-------------GRPIANHQIFIVDSQNHM-LPV 7774
Cdd:cd05931   300 frpeafrpSYGLAEATlFVSGGPPGTGpvvlrvdrDALAGRAVAVaaddpaarelvscGRPLPDQEVRIVDPETGReLPD 379
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7775 GVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARwLPDGNIEYLGRIDHQVKIRG 7842
Cdd:cd05931   380 GEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRG 446
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
284-685 2.33e-33

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 138.11  E-value: 2.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  284 RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLs 363
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  364 qghlqervsfsgtwirlddeeayhedgsnlesVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKN-TNYIDVTGQDK 442
Cdd:cd05907    83 --------------------------------VEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALAlAERLPATEGDR 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  443 LLQL--SSYSFdGSTFDIFGALLNGAKLVLVPKETVLdvakLAGLIEkqqisvmFITTAFFNVlvdmnpdcLRHARAILF 520
Cdd:cd05907   131 HLSFlpLAHVF-ERRAGLYVPLLAGARIYFASSAETL----LDDLSE-------VRPTVFLAV--------PRVWEKVYA 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  521 GGERVSVSHVRKALGHLGPGK--------------------------IKHVYGPTESTVFATSYDVHEVEEGAVSIPIGG 574
Cdd:cd05907   191 AIKVKAVPGLKRKLFDLAVGGrlrfaasggaplpaellhffralgipVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  575 PisntaiyivnaqnKLQpIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRID 654
Cdd:cd05907   271 V-------------EVR-IADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKK 330
                         410       420       430
                  ....*....|....*....|....*....|..
gi 386647928  655 D-QVKIRGFRIELGEIEAHLLKLEAIEKATVV 685
Cdd:cd05907   331 DlIITSGGKNISPEPIENALKASPLISQAVVI 362
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5030-5382 2.35e-33

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 135.48  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA--AGYRREYRLDQ---FPVRLLQlasfSFDVFVGDIARTLYnGGTMVic 5104
Cdd:cd05917     1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGyfIGERLGLTEQDrlcIPVPLFH----CFGSVLGVLACLTH-GATMV-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5105 PKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFG-SQFRIinAY 5183
Cdd:cd05917    74 FPSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTI--AY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5184 GVTEAA--IDSSLYDEPlaklPEAGNVPIGKAALNAKFYIVDAHLNPVP-VGVLGELCIGGIGVARGYLNRPELTEEKfv 5260
Cdd:cd05917   152 GMTETSpvSTQTRTDDS----IEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEA-- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5261 dspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAkIRG-YRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCA--H 5337
Cdd:cd05917   226 ----IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAwiR 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 5338 FTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 5382
Cdd:cd05917   301 LKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
7456-7928 2.51e-33

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 138.59  E-value: 2.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:cd12118    14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLLTQRhlqecvSFDGkviaaDDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG--LCS 7613
Cdd:cd12118    94 AFILRHSEAKVLFVDR------EFEY-----EDLLAEGDPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGayLNA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7614 LklmfAETLRITEEDRVVQFASLS-FDASCWEIFKALF-FGATLYIPAKdtiLDYPLFESYMNENGIT----AAILPPTY 7687
Cdd:cd12118   163 L----ANILEWEMKQHPVYLWTLPmFHCNGWCFPWTVAaVGGTNVCLRK---VDAKAIYDLIEKHKVThfcgAPTVLNML 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7688 AIYLSPDR--LPSLKKLITGGS---AASVEFVQQWKDKVryFNAYGPTEAS--IVTSVWAASPDGL--DLRSVPIGRP-- 7756
Cdd:cd12118   236 ANAPPSDArpLPHRVHVMTAGApppAAVLAKMEELGFDV--THVYGLTETYgpATVCAWKPEWDELptEERARLKARQgv 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7757 --IANHQIFIVDSQNhMLPV---GV-AGELCISGAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEY 7830
Cdd:cd12118   314 ryVGLEEVDVLDPET-MKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGG-------WFHSGDLAVIHPDGYIEI 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7831 LGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAyFVA---DRELTVSELRGTLSQELPGYMIPS 7907
Cdd:cd12118   386 KDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA-FVElkeGAKVTEEEIIAFCREHLAGFMVPK 464
                         490       500
                  ....*....|....*....|.
gi 386647928 7908 YFVQLEqMPLTPNGKIDRNAL 7928
Cdd:cd12118   465 TVVFGE-LPKTSTGKIQKFVL 484
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4001-4334 2.56e-33

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 135.10  E-value: 2.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4001 YTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLsfdascWEIF-------KALFFGATLYIPTSTtiLD 4073
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPL------FHCFgsvlgvlACLTHGATMVFPSPS--FD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4074 -YPLFESYMNENgitATIL---PPTYAAYLNPDRMP-----SLKKLITGGSAASVEFVQQWKdKVLYFN----AYGPTEA 4140
Cdd:cd05917    81 pLAVLEAIEKEK---CTALhgvPTMFIAELEHPDFDkfdlsSLRTGIMAGAPCPPELMKRVI-EVMNMKdvtiAYGMTET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4141 SIVTSIwDEASDSLgDRKSVPIGRPLANHRIYVVDSHNR-MLPVGVAGELCISGVGLARGYLNRPELTAEKfvdnpfEPG 4219
Cdd:cd05917   157 SPVSTQ-TRTDDSI-EKRVNTVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4220 ERMYRTGDLVRWLPDGNLEYLGRIDHQVkIRG-YRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--REL 4296
Cdd:cd05917   229 DGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKegAEL 307
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 386647928 4297 TAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDR 4334
Cdd:cd05917   308 TEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
2359-2823 2.77e-33

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 138.59  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYML 2438
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2439 EDSSAQVLLaqrrlqervsfagtvvtVDDEQAY-----AGDGS-NLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGlCS 2512
Cdd:cd12118    98 RHSEAKVLF-----------------VDREFEYedllaEGDPDfEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRG-AY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2513 LKQMfANTLQINAQDRVVQFASLS-FDASCWEVFQTLF-FGATLYIPTKetiLDYQWFERYMSDNGITTATLPPT-YAVY 2589
Cdd:cd12118   160 LNAL-ANILEWEMKQHPVYLWTLPmFHCNGWCFPWTVAaVGGTNVCLRK---VDAKAIYDLIEKHKVTHFCGAPTvLNML 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2590 LNPDH-----MPDFKRLIAAGS---ASSLELLQQWKDKVkyFNAYGPTED----SICttIWTP-----STEDISQLKS-- 2650
Cdd:cd12118   236 ANAPPsdarpLPHRVHVMTAGApppAAVLAKMEELGFDV--THVYGLTETygpaTVC--AWKPewdelPTEERARLKArq 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2651 -VPIggpIVNHRIYIVDAH-YQPVPV-GV-AGELCIAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDG 2726
Cdd:cd12118   312 gVRY---VGLEEVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGG-------WFHSGDLAVIHPDG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2727 TIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAyFVA---DRTMTVGELRGELSGELPGY 2803
Cdd:cd12118   382 YIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA-FVElkeGAKVTEEEIIAFCREHLAGF 460
                         490       500
                  ....*....|....*....|
gi 386647928 2804 MIPAHFVQLErMPLTPNGKI 2823
Cdd:cd12118   461 MVPKTVVFGE-LPKTSTGKI 479
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1322-1795 3.66e-33

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 138.53  E-value: 3.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 1401
Cdd:cd12119    25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 THLQER-AQQWGQ--TLQAVLCLDDEAAYAED------------ASNVANVNEP----HDLAYVIYTSGTTGRPKGVMIE 1462
Cdd:cd12119   105 RDFLPLlEAIAPRlpTVEHVVVMTDDAAMPEPagvgvlayeellAAESPEYDWPdfdeNTAAAICYTSGTTGNPKGVVYS 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1463 HRSLVntaagyrreyrldqfpvrLLQLASFSFDVF---VGDIA----------------RTLYNGGTMVIcPkDDRIDPA 1523
Cdd:cd12119   185 HRSLV------------------LHAMAALLTDGLglsESDVVlpvvpmfhvnawglpyAAAMVGAKLVL-P-GPYLDPA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1524 RLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSvtdyRVLQERFGSQF-RIINAYGVTEAA--I 1600
Cdd:cd12119   245 SLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVP----RSLIEAFEERGvRVIHAWGMTETSplG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1601 DSSLYDEPLAKLPEAGNVPI----GKAALNAKFYIVDAHLNPVPV--GVLGELCIGGIGVARGYLNRPELTEEKFVDSPF 1674
Cdd:cd12119   321 TVARPPSEHSNLSEDEQLALrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1675 vegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQK--VLCAYFTAES 1752
Cdd:cd12119   401 -------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErpLAVVVLKEGA 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 386647928 1753 ELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd12119   474 TVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1323-1795 3.79e-33

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 136.70  E-value: 3.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTqt 1402
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 hlqeraqqwgqtlqavlclDDEaayaedasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRslvntaagyrreyrldqF 1482
Cdd:cd05972    79 -------------------DAE-----------------DPALIYFTSGTTGLPKGVLHTHS-----------------Y 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1483 PVRLLQLASFSFDVFVGDI---------ARTLYNG-------GTMVICPKDDRIDPARLHYWISEEKITIFESTPAlIIP 1546
Cdd:cd05972   106 PLGHIPTAAYWLGLRPDDIhwniadpgwAKGAWSSffgpwllGATVFVYEGPRFDAERILELLERYGVTSFCGPPT-AYR 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1547 FMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQFRiiNAYGVTEAAIdsslydePLAKLPEAGNVP--IGKAA 1624
Cdd:cd05972   185 MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIR--DGYGQTETGL-------TVGNFPDMPVKPgsMGRPT 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1625 LNAKFYIVDAHLNPVPVGVLGELCI--GGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRID 1702
Cdd:cd05972   256 PGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRAD 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1703 NQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED------AKGQKVLCAYFTAESELKLsELRSSLSQELPGYMIPSYF 1776
Cdd:cd05972   329 DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDpvrgevVKAFVVLTSGYEPSEELAE-ELQGHVKKVLAPYKYPREI 407
                         490
                  ....*....|....*....
gi 386647928 1777 VQLEQLPLTANGKIDRKAL 1795
Cdd:cd05972   408 EFVEELPKTISGKIRRVEL 426
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3402-3821 3.89e-33

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 136.43  E-value: 3.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3402 PM---QKGMWF-HNTLNrhggayiEQTLFNV------RGALNIELFSRSWNELAARHAVLRTNF-HSGWRGEPLQIVYRY 3470
Cdd:cd19532     3 PMsfgQSRFWFlQQYLE-------DPTTFNVtfsyrlTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVLAS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3471 KPVEFAYEDLRHLAEAEwsAYLDQLvnddKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDT 3550
Cdd:cd19532    76 SPLRLEHVQISDEAEVE--EEFERL----KNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3551 YeaylrNDLSERPAAPSYSHYIEW----LEKQDMEAAARYWTGFLAgydsqtTLPQ-------------GKLHNkdgeYT 3613
Cdd:cd19532   150 Y-----NGQPLLPPPLQYLDFAARqrqdYESGALDEDLAYWKSEFS------TLPEplpllpfakvksrPPLTR----YD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3614 EANILRSLGKSLTERMSRIAKQHQVTVntlMQ---AAWGIILQKYNGTDDAVFGSVVSGRSAEiaGIEEMIGLFINTIPV 3690
Cdd:cd19532   215 THTAERRLDAALAARIKEASRKLRVTP---FHfylAALQVLLARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPL 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3691 RVSCEAEQSFADVMKRVQE---AALESGG--YD-------------YYPLYeiQA-----QSAQKQdlithiMAFENFPM 3747
Cdd:cd19532   290 RFRRDPSQTFADVLKETRDkayAALAHSRvpFDvlldelgvprsatHSPLF--QVfinyrQGVAES------RPFGDCEL 361
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 3748 DEQieqagSYEDGKlaitdvdiaeqTNYDFTLVV--MPGEELAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19532   362 EGE-----EFEDAR-----------TPYDLSLDIidNPDGDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1305-1795 5.06e-33

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 137.79  E-value: 5.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1305 KQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSD 1384
Cdd:PRK03640   10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1385 RIQFMLEDSAASVLLTQTHLQERaqqwgqtLQAVLCLDDEAAYAEDASNVANVNEPH--DLAYVIYTSGTTGRPKGVMIE 1462
Cdd:PRK03640   90 ELLWQLDDAEVKCLITDDDFEAK-------LIPGISVKFAELMNGPKEEAEIQEEFDldEVATIMYTSGTTGKPKGVIQT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1463 HR----SLVNTA--AGYRREyrlDQF--PVRLLQLASFSFdvfvgdIARTLYNGGTMVICPKddrIDPARLHYWISEEKI 1534
Cdd:PRK03640  163 YGnhwwSAVGSAlnLGLTED---DCWlaAVPIFHISGLSI------LMRSVIYGMRVVLVEK---FDAEKINKLLQTGGV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1535 TIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDscsvTDYRVLQERFGSQFRIINAYGVTEAA--IDSSLYDEPLAKL 1612
Cdd:PRK03640  231 TIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGP----APKPLLEQCKEKGIPVYQSYGMTETAsqIVTLSPEDALTKL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1613 PEAGnvpigKAALNAKFYIVDaHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPD 1692
Cdd:PRK03640  307 GSAG-----KPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1693 GNVDFIGRidnqakiRGYRIETG-------EIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQ 1765
Cdd:PRK03640  374 GFLYVLDR-------RSDLIISGgeniypaEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEE 446
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 1766 ELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK03640  447 KLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
4913-5385 5.35e-33

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 136.31  E-value: 5.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTqt 4992
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 hlqeraqqwgqtlqaalclDDEaayaedasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRslvntaagyrreyrldqF 5072
Cdd:cd05972    79 -------------------DAE-----------------DPALIYFTSGTTGLPKGVLHTHS-----------------Y 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5073 PVRLLQLASFSFDVFVGDI---------ARTLYNG-------GTMVICPKDDRIDPARLHYWISEEKITIFESTPAlIIP 5136
Cdd:cd05972   106 PLGHIPTAAYWLGLRPDDIhwniadpgwAKGAWSSffgpwllGATVFVYEGPRFDAERILELLERYGVTSFCGPPT-AYR 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5137 FMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQFRiiNAYGVTEAAIdsslydePLAKLPEAGNVP--IGKAA 5214
Cdd:cd05972   185 MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIR--DGYGQTETGL-------TVGNFPDMPVKPgsMGRPT 255
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5215 LNAKFYIVDAHLNPVPVGVLGELCI--GGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRID 5292
Cdd:cd05972   256 PGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRAD 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5293 NQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED------AKGQKVLCAHFTAESELKLsELRSSLSQELPGYMIPSYF 5366
Cdd:cd05972   329 DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDpvrgevVKAFVVLTSGYEPSEELAE-ELQGHVKKVLAPYKYPREI 407
                         490
                  ....*....|....*....
gi 386647928 5367 VQLEQLPLTANGKIDRKAL 5385
Cdd:cd05972   408 EFVEELPKTISGKIRRVEL 426
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
3880-4337 5.73e-33

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 138.57  E-value: 5.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGG--AYIPIDPEYPEDR--------IRYMLED 3949
Cdd:cd05906    40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFvpAPLTVPPTYDEPNarlrklrhIWQLLGS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3950 -------SGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADGsnlePVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSl 4022
Cdd:cd05906   120 pvvltdaELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDL----PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILA- 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4023 klMFANTLQM---TEQDrvVQFASLSFD--ASCWEI-FKALFFGA-TLYIPTSTTILDYPLFESYMNENGITATILPPTY 4095
Cdd:cd05906   195 --RSAGKIQHnglTPQD--VFLNWVPLDhvGGLVELhLRAVYLGCqQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFA 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4096 AAYLN------PDR---MPSLKKLITGG----SAASVEFVQQWKDKVLYFNA----YGPTE--ASIVTSIWDEASDSLGD 4156
Cdd:cd05906   271 FALLNdlleeiEDGtwdLSSLRYLVNAGeavvAKTIRRLLRLLEPYGLPPDAirpaFGMTEtcSGVIYSRSFPTYDHSQA 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4157 RKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVrWLPDGN 4236
Cdd:cd05906   351 LEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGN 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4237 LEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLA---REDANGQQQLVAYFV------AQRELTAAELRATMSQ 4307
Cdd:cd05906   424 LTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAfavRDPGAETEELAIFFVpeydlqDALSETLRAIRSVVSR 503
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 4308 EL---PNYMIPsyfVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05906   504 EVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1296-1721 5.77e-33

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 137.70  E-value: 5.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1296 NEVFHALFEKQAERTpEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYV 1375
Cdd:PRK07514    3 NNLFDALRAAFADRD-APFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1376 PLDPDYPSDRIQFMLEDSAASVLLTQTH----LQERAQQWGqtLQAVLCLDD-------EAAYAEDASNVANVNEPHDLA 1444
Cdd:PRK07514   82 PLNTAYTLAELDYFIGDAEPALVVCDPAnfawLSKIAAAAG--APHVETLDAdgtgsllEAAAAAPDDFETVPRGADDLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1445 YVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASF-SFDVFVGdIARTLYNGGTMVICPKddrIDPA 1523
Cdd:PRK07514  160 AILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFhTHGLFVA-TNVALLAGASMIFLPK---FDPD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1524 RLHYWIseEKITIFESTPALiipfmdYV---AEHGLD---MSSMELLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTE 1597
Cdd:PRK07514  236 AVLALM--PRATVMMGVPTF------YTrllQEPRLTreaAAHMRLFISGSAPLLAETHREFQERTG--HAILERYGMTE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1598 AAIDSSlydEPLAKLPEAGNVpiGKAALNAKFYIVDAHLN-PVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFve 1676
Cdd:PRK07514  306 TNMNTS---NPYDGERRAGTV--GFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-- 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 1677 gerlYRTGDLARWMPDGNVDFIGRidnqAK---IR-GYRIETGEIETQL 1721
Cdd:PRK07514  379 ----FITGDLGKIDERGYVHIVGR----GKdliISgGYNVYPKEVEGEI 419
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
3404-3821 6.29e-33

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 136.24  E-value: 6.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3404 QKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYrykPVEFAYEDLRHL 3483
Cdd:cd19538     8 QRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEE-DGVPYQLIL---EEDEATPKLEIK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3484 --AEAEwsayLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCL-PLIaKELFDTYEAYLRNDLS 3560
Cdd:cd19538    84 evDEEE----LESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLaPLT-RDLSKAYRARCKGEAP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3561 ERPAAP-SYSHYI----EWL--EKQDMEAAAR---YWTGFLAGYDSQTTLPQGKLHNKDGEYtEANILR-SLGKSLTERM 3629
Cdd:cd19538   159 ELAPLPvQYADYAlwqqELLgdESDPDSLIARqlaYWKKQLAGLPDEIELPTDYPRPAESSY-EGGTLTfEIDSELHQQL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3630 SRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEiaGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQE 3709
Cdd:cd19538   238 LQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3710 AALESGGYDYYPLYEI-----QAQSAQKQDLITHIMAFENFPmDEQIEQAGSyeDGKLAITDVDIAEqtnYDFTLVV--- 3781
Cdd:cd19538   316 TNLEAYEHQDIPFERLvealnPTRSRSRHPLFQIMLALQNTP-QPSLDLPGL--EAKLELRTVGSAK---FDLTFELreq 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 386647928 3782 -MPGEE--LAVRFYYNASVYEHSAMERLMGHLIHVLEQVTASP 3821
Cdd:cd19538   390 yNDGTPngIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
3864-4336 6.52e-33

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 138.53  E-value: 6.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVF------EKSQLTYGELNERANRLARTLRDAGVRPDqLVGLMVERSLEMVVGIMAIMKAGGAYIPI-DP 3936
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3937 EYPE--DRIRYMLEDSGAQALLTQ--------RHLRERVSFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTT 4006
Cdd:cd05931    82 TPGRhaERLAAILADAGPRVVLTTaaalaavrAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4007 GKPKGVMVEHHGLCS-LKLMFaNTLQMTEQDRVVQFASL-------SFdascweIFKALFFGATLYIPTSTTILDYPLF- 4077
Cdd:cd05931   162 GTPKGVVVTHRNLLAnVRQIR-RAYGLDPGDVVVSWLPLyhdmgliGG------LLTPLYSGGPSVLMSPAAFLRRPLRw 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4078 -ESyMNENGITATILPP-TY---AAYLNPDRMP-----SLKKLITGG---SAASVE-FVQQWKD-----KVLYfNAYGPT 4138
Cdd:cd05931   235 lRL-ISRYRATISAAPNfAYdlcVRRVRDEDLEgldlsSWRVALNGAepvRPATLRrFAEAFAPfgfrpEAFR-PSYGLA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4139 EAS-IVTSIWDE--------------------ASDSLGDRKSVPIGRPLANHRIYVVDS-HNRMLPVGVAGELCISGVGL 4196
Cdd:cd05931   313 EATlFVSGGPPGtgpvvlrvdrdalagravavAADDPAARELVSCGRPLPDQEVRIVDPeTGRELPDGEVGEIWVRGPSV 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4197 ARGYLNRPELTAEKFVDNPFEPGERMYRTGDLvRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETqlakidAVQEAIVLA 4276
Cdd:cd05931   393 ASGYWGRPEATAETFGALAATDEGGWLRTGDL-GFLHDGELYITGRLKDLIIVRGRNHYPQDIEA------TAEEAHPAL 465
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 4277 RE--------DANGQQQLVAyfVAQRELT---------AAELRATMSQE--LPNYMIpsYFVQLAQMPLTPNGKIDRKA 4336
Cdd:cd05931   466 RPgcvaafsvPDDGEERLVV--VAEVERGadpadlaaiAAAIRAAVAREhgVAPADV--VLVRPGSIPRTSSGKIQRRA 540
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
5961-6420 7.81e-33

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 137.08  E-value: 7.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNaGVQPDQMVGLMVERSLEMVVGMIAILKAGgaYVPIDPDYP--EDRIRYMLEDSGAKLLLV 6038
Cdd:cd05909     8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIKTVLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6039 QGHLLDRA------------------------SFADKLVNLNDDGAYHEDGSNLEPVNG--PEHLTYVIYTSGTTGRPKG 6092
Cdd:cd05909    85 SKQFIEKLklhhlfdveydarivyledlrakiSKADKCKAFLAGKFPPKWLLRIFGVAPvqPDDPAVILFTSGSEGLPKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6093 VMVEHRNVVRLVKN-TNYVELNEQTHILqtGAV-VFDASTFE--IWGALLNGgrLYVVRNETILDAVSLKNAIQQYGINT 6168
Cdd:cd05909   165 VVLSHKNLLANVEQiTAIFDPNPEDVVF--GALpFFHSFGLTgcLWLPLLSG--IKVVFHPNPLDYKKIPELIYDKKATI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6169 MWLTAPLYNQ-LSQQDSGMFAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVpIGK 6247
Cdd:cd05909   241 LLGTPTFLRGyARAAHPEDFSSLRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGT-VGR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6248 PINNSTAYIVDSK-LSLLPVGVWGELIVGGDGVARGYLNRPELTaekfvesSFLPGERCYRTGDLARWLPDGTLEYKGRI 6326
Cdd:cd05909   319 PLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELT-------SFAFGDGWYDTGDIGKIDGEGFLTITGRL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6327 DEQVKIRGYRIELGEIEEQLLKV--ASVKEATVIVREDESGQKQLCAYFvaERELTIGELRAALSQ-ELPNYMIPSHFVP 6403
Cdd:cd05909   392 SRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGRKGEKIVLLTT--TTDTDPSSLNDILKNaGISNLAKPSYIHQ 469
                         490
                  ....*....|....*..
gi 386647928 6404 LERMPLTPNGKIDRRAL 6420
Cdd:cd05909   470 VEEIPLLGTGKPDYVTL 486
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
2369-2785 7.83e-33

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 136.72  E-value: 7.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2369 QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLa 2448
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2449 qrrlqervsfagtvvtvddeqayagdgsnLESavGPNDLAYIIYTSGTTGKPKGVMVEHHGLcsLKQM--FANTLQINAQ 2526
Cdd:cd17640    83 -----------------------------VEN--DSDDLATIIYTSGTTGNPKGVMLTHANL--LHQIrsLSDIVPPQPG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2527 DRVVQFASL--SFDASCwEVFQTLFFGATLY--IPT-KETILDYQwfERYMsdngittATLPPTY-AVYLNPDH----MP 2596
Cdd:cd17640   130 DRFLSILPIwhSYERSA-EYFIFACGCSQAYtsIRTlKDDLKRVK--PHYI-------VSVPRLWeSLYSGIQKqvskSS 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2597 DFKRLIAAGSASSLEL---------LQQWKDK------VKYFNAYGPTEDSICTTIWTPStedISQLKSVpiGGPIVNHR 2661
Cdd:cd17640   200 PIKQFLFLFFLSGGIFkfgisgggaLPPHVDTffeaigIEVLNGYGLTETSPVVSARRLK---CNVRGSV--GRPLPGTE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2662 IYIVDAHYQ-PVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRI-DHQVK 2739
Cdd:cd17640   275 IKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAkDTIVL 348
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 386647928 2740 IRGYRIELGEIEEQLLKVASVQEAIVIAHDdasgQKQLCAYFVADR 2785
Cdd:cd17640   349 SNGENVEPQPIEEALMRSPFIEQIMVVGQD----QKRLGALIVPNF 390
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
256-747 8.24e-33

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 138.34  E-value: 8.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  256 YPRDTTIHRLFEEQAERRPDAVAVTfeDRQ---LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILK 332
Cdd:PRK06087   19 YWGDASLADYWQQTARAMPDKIAVV--DNHgasYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  333 AGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGH------------LQERVSFSGTWIRLDDEEAYH---------EDGS 391
Cdd:PRK06087   97 VGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLfkqtrpvdlilpLQNQLPQLQQIVGVDKLAPATsslslsqiiADYE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  392 NLES---VNGPEhLTYVIYTSGTTGKPKGNLTTHRNIIRVVKN-TNYIDVTGQDKLLQLSSYS-----FDGSTfdifGAL 462
Cdd:PRK06087  177 PLTTaitTHGDE-LAAVLFTSGTEGLPKGVMLTHNNILASERAyCARLNLTWQDVFMMPAPLGhatgfLHGVT----APF 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  463 LNGAKLVLvpkETVLDVAKLAGLIEKQQISVMFITTAF-FNVL--VDMNPDCLRHARAILFGGERVSVSHVRKALGHlgp 539
Cdd:PRK06087  252 LIGARSVL---LDIFTPDACLALLEQQRCTCMLGATPFiYDLLnlLEKQPADLSALRFFLCGGTTIPKKVARECQQR--- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  540 G-KIKHVYGPTEST--VFATSYDVHEVEEGAVSIPIGGpisnTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDL 616
Cdd:PRK06087  326 GiKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAG----VEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPEL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  617 TAEKFADnpfapgERMYRTGDLARWLPDGTIEYVGRIDDqVKIRGFR-IELGEIEAHLLKLEAI-EKATVVVRESANGEK 694
Cdd:PRK06087  402 TARALDE------EGWYYSGDLCRMDEAGYIKITGRKKD-IIVRGGEnISSREVEDILLQHPKIhDACVVAMPDERLGER 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  695 qLCAYYV---ADRSLPANEVRSTLS-QELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK06087  475 -SCAYVVlkaPHHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK07787 PRK07787
acyl-CoA synthetase; Validated
275-751 9.16e-33

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 136.66  E-value: 9.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  275 DAVAVTFEDRQLTYGELNERANRLARTLRNAGvqadqLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLE 354
Cdd:PRK07787   15 IADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  355 DSGTQVLL--SQGHLQERVSFSgtwIRLddeeayHEDGSNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIirvvknT 432
Cdd:PRK07787   90 DSGAQAWLgpAPDDPAGLPHVP---VRL------HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAI------A 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  433 NYIDV-------TGQDKLLQ-LSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKlagliekqqiSVMFITTAFFNV- 503
Cdd:PRK07787  155 ADLDAlaeawqwTADDVLVHgLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQ----------ALSEGGTLYFGVp 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  504 -----LVDmNPDclrHARAilFGGERVSVS-------HVRKALGHLGPGKIKHVYGPTEsTVFATSYDVH-EVEEGAVSI 570
Cdd:PRK07787  225 tvwsrIAA-DPE---AARA--LRGARLLVSgsaalpvPVFDRLAALTGHRPVERYGMTE-TLITLSTRADgERRPGWVGL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  571 PIGGpisnTAIYIVNAQNKLQPIGVA--GELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIE 648
Cdd:PRK07787  298 PLAG----VETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHR 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  649 YVGRID-DQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSY 727
Cdd:PRK07787  368 IVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPRE 447
                         490       500
                  ....*....|....*....|....
gi 386647928  728 FVQLEQMPLTTNGKVDRRALPAPE 751
Cdd:PRK07787  448 VRFVDALPRNAMGKVLKKQLLSEG 471
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1302-1795 9.53e-33

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 137.71  E-value: 9.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1302 LFEKQAERTPEVAAVVYENDR--LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP 1379
Cdd:PRK05852   21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1380 DYPSDRIQFMLEDSAASVLLTQT-----HLQERAQQWGQTL---------QAVLCLDDEAAYAEDASNVANVNEPHDLAY 1445
Cdd:PRK05852  101 ALPIAEQRVRSQAAGARVVLIDAdgphdRAEPTTRWWPLTVnvggdsgpsGGTLSVHLDAATEPTPATSTPEGLRPDDAM 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1446 VIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpkddridPAR- 1524
Cdd:PRK05852  181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLL--------PARg 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1525 ---LH-YW--ISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVT--DYRVLQERFGSQfrIINAYGVT 1596
Cdd:PRK05852  253 rfsAHtFWddIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTaeTAQALQTEFAAP--VVCAFGMT 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1597 EA-------AIDSSLYDEPlaklPEAGNVPIGKAAlNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKF 1669
Cdd:PRK05852  331 EAthqvtttQIEGIGQTEN----PVVSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1670 VDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA-KGQKVLCAYF 1748
Cdd:PRK05852  406 TDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQlYGEAVAAVIV 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 1749 TAES-ELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK05852  479 PRESaPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
4895-5385 9.56e-33

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 136.63  E-value: 9.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4895 KQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSD 4974
Cdd:PRK03640   10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4975 RIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAALclddEAAYAEDASNVANVNEpHDLAYVIYTSGTTGRPKGVMIEHR 5054
Cdd:PRK03640   90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAEL----MNGPKEEAEIQEEFDL-DEVATIMYTSGTTGKPKGVIQTYG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5055 ----SLVNTA--AGYRREyrlDQF--PVRLLQLASFSFdvfvgdIARTLYNGGTMVICPKddrIDPARLHYWISEEKITI 5126
Cdd:PRK03640  165 nhwwSAVGSAlnLGLTED---DCWlaAVPIFHISGLSI------LMRSVIYGMRVVLVEK---FDAEKINKLLQTGGVTI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5127 FESTPAliipfmdyvaehgldMSSMVLLITSSDSCSV-----------TDYRVLQERFGSQFRIINAYGVTEAA--IDSS 5193
Cdd:PRK03640  233 ISVVST---------------MLQRLLERLGEGTYPSsfrcmllgggpAPKPLLEQCKEKGIPVYQSYGMTETAsqIVTL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5194 LYDEPLAKLPEAgnvpiGKAALNAKFYIVDaHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRT 5273
Cdd:PRK03640  298 SPEDALTKLGSA-----GKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KT 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5274 GDLARWMPDGNVDFIGRidnqakiRGYRIETG-------EIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKL 5346
Cdd:PRK03640  365 GDIGYLDEEGFLYVLDR-------RSDLIISGgeniypaEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTE 437
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 386647928 5347 SELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK03640  438 EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
262-752 1.03e-32

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 138.24  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  262 IHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPID 341
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  342 PEYPEERIRYMLEDSGTQVLLSQGHLQERVSF----------------------------------SGTWIRLDDEEAYH 387
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILCLDLVFPRVTNvqsatkiehvivtriadflpfpknllypfvqkkqSNLVVKVSESETIH 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  388 -------EDGSNLESVNGPEH-LTYVIYTSGTTGKPKGNLTTHRNIirvVKNT------NYIDVTGQDKLLQ-LSSYSFD 452
Cdd:PRK06710  186 lwnsvekEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNL---VSNTlmgvqwLYNCKEGEEVVLGvLPFFHVY 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  453 GSTFDIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVM----FITTAFFNVLVDMNPDcLRHARAILFGGERVSVs 528
Cdd:PRK06710  263 GMTAVMNLSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFpgapTIYIALLNSPLLKEYD-ISSIRACISGSAPLPV- 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  529 HVRKALGHLGPGKIKHVYGPTESTVFATSydvHEVEEGAVSIPIGGPISNTAIYIVNAQN-KLQPIGVAGELCVAGDGLA 607
Cdd:PRK06710  338 EVQEKFETVTGGKLVEGYGLTESSPVTHS---NFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQIM 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  608 RGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-V 686
Cdd:PRK06710  415 KGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIgV 487
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  687 RESANGEkQLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEE 752
Cdd:PRK06710  488 PDPYRGE-TVKAFVVlkEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEK 554
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3880-4337 1.31e-32

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 135.34  E-value: 1.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQR 3959
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 HLRERVSfAGTFVavddeqayhadgsnlepvvgpnhlayVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRvv 4039
Cdd:cd05973    81 ANRHKLD-SDPFV--------------------------MMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS-- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4040 qFASLSFDASCWEIFKALFfgATLYIPTSTTILD----YPLFESYMNENGITATILPPTYAAYLNPDRMP-------SLK 4108
Cdd:cd05973   132 -FWNAADPGWAYGLYYAIT--GPLALGHPTILLEggfsVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEvparpkgRLR 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4109 KLITGGSAASVEfVQQWKDK---VLYFNAYGPTEASIVTSIWDEASDSLgdrKSVPIGRPLANHRIYVVDSHNRMLPVGV 4185
Cdd:cd05973   209 RVSSAGEPLTPE-VIRWFDAalgVPIHDHYGQTELGMVLANHHALEHPV---HAGSAGRAMPGWRVAVLDDDGDELGPGE 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4186 AGELCI----SGVGLARGYLNRPELTaekfvdnpfePGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVET 4261
Cdd:cd05973   285 PGRLAIdianSPLMWFRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4262 QLAKIDAVQEAIVLAREDANgQQQLVAYFVAQRELT------AAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRK 4335
Cdd:cd05973   355 ALIEHPAVAEAAVIGVPDPE-RTEVVKAFVVLRGGHegtpalADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRF 433

                  ..
gi 386647928 4336 AL 4337
Cdd:cd05973   434 LL 435
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
2320-2826 1.65e-32

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 137.82  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2320 EMLTAAEQTQLHHVFNATAADYE-ADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPV 2398
Cdd:PRK05605    6 EMSAFADKPWLQSYAPWTPHDLDyGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2399 GLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQ-------RRLQERVSfAGTVVTVDDEQA- 2470
Cdd:PRK05605   86 AIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWdkvaptvERLRRTTP-LETIVSVNMIAAm 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2471 -----YA----------------------------------GDGSNLES-AVGPNDLAYIIYTSGTTGKPKGVMVEHHGL 2510
Cdd:PRK05605  165 pllqrLAlrlpipalrkaraaltgpapgtvpwetlvdaaigGDGSDVSHpRPTPDDVALILYTSGTTGKPKGAQLTHRNL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2511 cslkqmFANTLQINA-------QDRVVQFASLSFDASCWEVFQTL--FFGATL-YIPTKETILDYQWFERYmsdngitta 2580
Cdd:PRK05605  245 ------FANAAQGKAwvpglgdGPERVLAALPMFHAYGLTLCLTLavSIGGELvLLPAPDIDLILDAMKKH--------- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2581 tlPPTYAvylnPDHMPDFKRLIAAGS---------------ASSL--ELLQQWKDKVKYF--NAYGPTEDSicttiwtps 2641
Cdd:PRK05605  310 --PPTWL----PGVPPLYEKIAEAAEergvdlsgvrnafsgAMALpvSTVELWEKLTGGLlvEGYGLTETS--------- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2642 tedisqlksvPI--GGPIVNHR-------------IYIVDAH--YQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVD 2704
Cdd:PRK05605  375 ----------PIivGNPMSDDRrpgyvgvpfpdteVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLD 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2705 NpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVAD 2784
Cdd:PRK05605  445 G-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLE 517
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 386647928 2785 RTMTVGE--LRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRK 2826
Cdd:PRK05605  518 PGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1296-1795 1.72e-32

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 137.11  E-value: 1.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1296 NEVFHALFEKQAERTPEVAAVVYEND------RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWK 1369
Cdd:PRK13295   23 DRTINDDLDACVASCPDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1370 AGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQ--------ERAQQWGQTLQAVLCLDDEAA-------------YA 1428
Cdd:PRK13295  103 IGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaamaRRLRPELPALRHVVVVGGDGAdsfeallitpaweQE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1429 EDASNV--ANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLL-----QLASFSFDVFVgdi 1501
Cdd:PRK13295  183 PDAPAIlaRLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMaspmaHQTGFMYGLMM--- 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1502 arTLYNGGTMVIcpkDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQE 1581
Cdd:PRK13295  260 --PVMLGATAVL---QDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARA 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1582 RFGSqfRIINAYGVTE-AAIDSSLYDEPLAKLPEAGNVPIGKAALNakfyIVDAHLNPVPVGVLGELCIGGIGVARGYLN 1660
Cdd:PRK13295  335 ALGA--KIVSAWGMTEnGAVTLTKLDDPDERASTTDGCPLPGVEVR----VVDADGAPLPAGQIGRLQVRGCSNFGGYLK 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1661 RPELTEekfvdspfVEGERLYRTGDLARWMPDGNVdfigRIDNQAK---IRG-YRIETGEIETQLLKAEGVREAVVVVRE 1736
Cdd:PRK13295  409 RPQLNG--------TDADGWFDTGDLARIDADGYI----RISGRSKdviIRGgENIPVVEIEALLYRHPAIAQVAIVAYP 476
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 1737 DAKGQKVLCAYFT--AESELKLSELRSSL-SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK13295  477 DERLGERACAFVVprPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
4879-5385 1.77e-32

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 136.94  E-value: 1.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4879 AAPDAPENEAFHALFEKQAECTPEAAAVVYENDR--LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALA 4956
Cdd:PRK05852    8 APMASDFGPRIADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4957 VWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT-----HLQERAQQWGQTL---------QAALCLDDEAAYAEDAS 5022
Cdd:PRK05852   88 ASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDAdgphdRAEPTTRWWPLTVnvggdsgpsGGTLSVHLDAATEPTPA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5023 NVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMV 5102
Cdd:PRK05852  168 TSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5103 IcpkddridPAR----LH-YW--ISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVT--DYRVLQERF 5173
Cdd:PRK05852  248 L--------PARgrfsAHtFWddIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTaeTAQALQTEF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5174 GSQfrIINAYGVTEA-------AIDSSLYDEPlaklPEAGNVPIGKAAlNAKFYIVDAHLNPVPVGVLGELCIGGIGVAR 5246
Cdd:PRK05852  320 AAP--VVCAFGMTEAthqvtttQIEGIGQTEN----PVVSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVR 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5247 GYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRE 5326
Cdd:PRK05852  393 GYLGDPTITAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVP 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 5327 DA-KGQKVLCAHFTAES-ELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK05852  466 DQlYGEAVAAVIVPRESaPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK09088 PRK09088
acyl-CoA synthetase; Validated
269-747 2.15e-32

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 135.70  E-value: 2.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  269 QAERRPDAVAVT--FEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPE 346
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  347 ERIRYMLEDSGTQVLLSQGHLQervsfSGTWIRLD----DEEAYHEDGSNLESVNgPEHLTYVIYTSGTTGKPKGNLTTH 422
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVA-----AGRTDVEDlaafIASADALEPADTPSIP-PERVSLILFTSGTSGQPKGVMLSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  423 RNIIRVVKNtnyIDVTGqdKLLQLSSYSFDGSTFDIFGaLLNGAKLVLVPKETVL-----DVAKLAGLIEKQQISVmfit 497
Cdd:PRK09088  158 RNLQQTAHN---FGVLG--RVDAHSSFLCDAPMFHIIG-LITSVRPVLAVGGSILvsngfEPKRTLGRLGDPALGI---- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  498 TAFFNV--LVDM-------NPDCLRHARAILFGGERVSVSHVRkalGHLGPGkIKHV--YGPTES-TVFATSYDVHEVEE 565
Cdd:PRK09088  228 THYFCVpqMAQAfraqpgfDAAALRHLTALFTGGAPHAAEDIL---GWLDDG-IPMVdgFGMSEAgTVFGMSVDCDVIRA 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  566 GAVSIPIGGPISNTAIyiVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFAdnpfapGERMYRTGDLARWLPDG 645
Cdd:PRK09088  304 KAGAAGIPTPTVQTRV--VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGWFRTGDIARRDADG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  646 TIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKQLCAYYVADRS-LPANEVRSTLSQELPAYM 723
Cdd:PRK09088  376 FFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVgMADAQWGEVGYLAIVPADGApLDLERIRSHLSTRLAKYK 455
                         490       500
                  ....*....|....*....|....
gi 386647928  724 LPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK09088  456 VPKHLRLVDALPRTASGKLQKARL 479
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1323-1795 2.84e-32

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 135.54  E-value: 2.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAqGVKPNQLVGILADRSADLLVGALAVWKAGgaYVPLDPDYPS--DRIQFMLEDSAASVLLT 1400
Cdd:cd05909     8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKLAGIKTVLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1401 QTHLQERAQQWGQTLQAVLClddEAAYAEDASN--------------------------VANVnEPHDLAYVIYTSGTTG 1454
Cdd:cd05909    85 SKQFIEKLKLHHLFDVEYDA---RIVYLEDLRAkiskadkckaflagkfppkwllrifgVAPV-QPDDPAVILFTSGSEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1455 RPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASF-SFDvFVGDIARTLYNGGTMVICPkddriDParLHY-----W 1528
Cdd:cd05909   161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFhSFG-LTGCLWLPLLSGIKVVFHP-----NP--LDYkkipeL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1529 ISEEKITIFESTPAliipFMDYVAE--HGLDMSSMELLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAidsslyd 1606
Cdd:cd05909   233 IYDKKATILLGTPT----FLRGYARaaHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG--IRILEGYGTTECS------- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1607 ePLAKL--PEAGNVP--IGKAALNAKFYIVD-AHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfveGERLY 1681
Cdd:cd05909   300 -PVISVntPQSPNKEgtVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-------GDGWY 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1682 RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVR-EDA-KGQKVLCAYFTaeSELKLSEL 1759
Cdd:cd05909   372 DTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSvPDGrKGEKIVLLTTT--TDTDPSSL 449
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 1760 RSSLSQ-ELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05909   450 NDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1307-1795 2.88e-32

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 136.71  E-value: 2.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 1386
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QFMLEDSAASVLLTQTHLQERAQQ-WGQT-LQAVLC------------------LDDEAAYAEDASNV------------ 1434
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAPVVEQvRAETsLRHVIVtsladvlpaeptlplpdsLRAPRLAAAGAIDLlpalractapvp 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1435 ANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR-EYRLDQFPVRLLQLASF-----SFDVFVgdiarTLYNG 1508
Cdd:PRK06178  203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAvAVVGGEDSVFLSFLPEFwiageNFGLLF-----PLFSG 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1509 GTMVICpkdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVT-DYR---------V 1578
Cdd:PRK06178  278 ATLVLL---ARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSFVKKLNpDYRqrwraltgsV 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1579 LQErfgsqfriiNAYGVTEA-----------AIDSSLYDEPL-AKLPeagnVPigkaalNAKFYIVDAHLN-PVPVGVLG 1645
Cdd:PRK06178  355 LAE---------AAWGMTEThtcdtftagfqDDDFDLLSQPVfVGLP----VP------GTEFKICDFETGeLLPLGAEG 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1646 ELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAE 1725
Cdd:PRK06178  416 EIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 1726 GVREAVVVVREDA-KGQkVLCAYFT--AESELKLSELRSSLSQELPGYMIPSYFVqLEQLPLTANGKIDRKAL 1795
Cdd:PRK06178  489 AVLGSAVVGRPDPdKGQ-VPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
7470-7886 4.84e-32

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 134.41  E-value: 4.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7470 TQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLT 7549
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7550 QRHlqecvsfdgkviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDR 7629
Cdd:cd17640    84 END--------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDR 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7630 VVQFASL--SFDASCwEIFKALFFGATLY--IPA-KDTILDYP---------LFESYmnENGITAAI--LPPT----YAI 7689
Cdd:cd17640   132 FLSILPIwhSYERSA-EYFIFACGCSQAYtsIRTlKDDLKRVKphyivsvprLWESL--YSGIQKQVskSSPIkqflFLF 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7690 YLSPDRlpsLKKLITGGSAasvefVQQWKDK------VRYFNAYGPTEASIVTSvwAASPDGLDLRSVpiGRPIANHQIF 7763
Cdd:cd17640   209 FLSGGI---FKFGISGGGA-----LPPHVDTffeaigIEVLNGYGLTETSPVVS--ARRLKCNVRGSV--GRPLPGTEIK 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7764 IVDSQ-NHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRI-DHQVKIR 7841
Cdd:cd17640   277 IVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWF------NTGDLGWLTCGGELVLTGRAkDTIVLSN 350
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 7842 GYRIELGEIEEQLLKIASVQETIVIargdanGQQQ--LCAYFVADRE 7886
Cdd:cd17640   351 GENVEPQPIEEALMRSPFIEQIMVV------GQDQkrLGALIVPNFE 391
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
7443-7923 5.36e-32

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 135.68  E-value: 5.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7443 AREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQA-DQPVGLMIERSlEMIVGAFAIMKAGG 7521
Cdd:PRK07786   14 ARRQNWVNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7522 AYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQ-------ECVSFDGKVI----AADD-----EQAYGEDGSNLEPVVGP 7585
Cdd:PRK07786   93 IAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALApvatavrDIVPLLSTVVvaggSSDDsvlgyEDLLAEAGPAHAPVDIP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7586 NHL-AYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFD-ASCWEIFKALFFGATLYIpakdti 7663
Cdd:PRK07786  173 NDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVI------ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7664 ldYPL--FE-----SYMNENGITAAILPPT--YAIYLSPDRLP---SLKKLITGGSAASVEFVQQWKD---KVRYFNAYG 7728
Cdd:PRK07786  247 --YPLgaFDpgqllDVLEAEKVTGIFLVPAqwQAVCAEQQARPrdlALRVLSWGAAPASDTLLRQMAAtfpEAQILAAFG 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7729 PTEASIVTSVWaaspDGLD-LRSV-PIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNP 7806
Cdd:PRK07786  325 QTEMSPVTCML----LGEDaIRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGW 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7807 FlagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV---A 7883
Cdd:PRK07786  401 F-------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnD 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 386647928 7884 DRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:PRK07786  474 DAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
2362-2828 5.37e-32

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 133.76  E-value: 5.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2362 PAVVFEGQQLTYRELNERANRLARTLQ-ALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLED 2440
Cdd:cd05958     2 TCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2441 SSAQVLLAqrrlqervsfAGTVVTVDDeqayagdgsnlesavgpndLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFA-N 2519
Cdd:cd05958    82 ARITVALC----------AHALTASDD-------------------ICILAFTSGTTGAPKATMHFHRDPLASADRYAvN 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2520 TLQINAQDRVVQFASLSFdascwevfqTLFFGATLYIP---TKETILdyqwFERYMSDNGITTA---------TLPPTYA 2587
Cdd:cd05958   133 VLRLREDDRFVGSPPLAF---------TFGLGGVLLFPfgvGASGVL----LEEATPDLLLSAIarykptvlfTAPTAYR 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2588 --VYLNPDHMPD---FKRLIAAGSASSLELLQQWKDkvkyfnAYG-PTEDSICTT----IWTPSTEDISQLKSVpiGGPI 2657
Cdd:cd05958   200 amLAHPDAAGPDlssLRKCVSAGEALPAALHRAWKE------ATGiPIIDGIGSTemfhIFISARPGDARPGAT--GKPV 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2658 VNHRIYIVDAHYQPVPVGVAGELCIAGvglARGYLNRPDLTAEKFVDnpfepGERMYrTGDLAKWLPDGTIEYLGRIDHQ 2737
Cdd:cd05958   272 PGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQ-----GGWNI-TGDTYSRDPDGYFRHQGRSDDM 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2738 VKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVG-----ELRGELSGELPGYMIPAHFVQL 2812
Cdd:cd05958   343 IVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlarELQDHAKAHIAPYKYPRAIEFV 422
                         490
                  ....*....|....*.
gi 386647928 2813 ERMPLTPNGKIDRKAL 2828
Cdd:cd05958   423 TELPRTATGKLQRFAL 438
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1316-1792 5.46e-32

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 134.11  E-value: 5.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1316 VVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAA 1395
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1396 SVLLtqthlqeraqqwgqtlqavlclddeaayaedasnvanVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR 1475
Cdd:cd05914    81 KAIF-------------------------------------VSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1476 EYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICpkdDRIDPARLhywiseEKITIFESTPALIIPFMdYVAEHG 1555
Cdd:cd05914   124 VVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL---DKIPSAKI------IALAFAQVTPTLGVPVP-LVIEKI 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1556 LDMSSMELLITS-----------SDSCSVTDYRVLQERFGSQFRII-----------------------NAYGVTEAAid 1601
Cdd:cd05914   194 FKMDIIPKLTLKkfkfklakkinNRKIRKLAFKKVHEAFGGNIKEFviggakinpdveeflrtigfpytIGYGMTETA-- 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1602 sslydePLAklpeAGNVP-------IGKAALNAKFYIVDahlnPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspf 1674
Cdd:cd05914   272 ------PII----SYSPPnrirlgsAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK--- 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1675 vegERLYRTGDLARWMPDGNVDFIGRIDNQAKI-RGYRIETGEIETQLLKAEgVREAVVVVREDAKGQKVLCAYFTAESE 1753
Cdd:cd05914   335 ---DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMP-FVLESLVVVQEKKLVALAYIDPDFLDV 410
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 1754 LKLS----------ELRSSLSQELPGY-MIPSYFVQLEQLPLTANGKIDR 1792
Cdd:cd05914   411 KALKqrniidaikwEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1306-1795 5.62e-32

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 135.65  E-value: 5.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1306 QAERTPEVAAVVYEND-RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSD 1384
Cdd:PRK06087   32 TARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1385 RIQFMLEDSAASVLLTQTHLQERA--------QQWGQTLQAVLCLDDEA-AYAEDA-SNVANVNEP---------HDLAY 1445
Cdd:PRK06087  112 ELVWVLNKCQAKMFFAPTLFKQTRpvdlilplQNQLPQLQQIVGVDKLApATSSLSlSQIIADYEPlttaitthgDELAA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1446 VIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL---DQF--PVRLLQLASFsfdvFVGDIARTLYnGGTMVIcpkDDRI 1520
Cdd:PRK06087  192 VLFTSGTEGLPKGVMLTHNNILASERAYCARLNLtwqDVFmmPAPLGHATGF----LHGVTAPFLI-GARSVL---LDIF 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1521 DPARLHYWISEEKIT-IFESTPaLIIPFMDYVAEHGLDMSSMELLITSSdscSVTDYRVLQERFGSQFRIINAYGVTEAA 1599
Cdd:PRK06087  264 TPDACLALLEQQRCTcMLGATP-FIYDLLNLLEKQPADLSALRFFLCGG---TTIPKKVARECQQRGIKLLSVYGSTESS 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1600 IDSSLydePLAK-LPEAGNVPiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegE 1678
Cdd:PRK06087  340 PHAVV---NLDDpLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------E 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1679 RLYRTGDLARWMPDGNVDFIGRiDNQAKIR-GYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFT---AESEL 1754
Cdd:PRK06087  410 GWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlkaPHHSL 488
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928 1755 KLSELRSSLS-QELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK06087  489 TLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2484-2825 6.81e-32

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 130.86  E-value: 6.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2484 PNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRV---VQF-----------ASLSFDASCweVFQTLF 2549
Cdd:cd05917     1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipVPLfhcfgsvlgvlACLTHGATM--VFPSPS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2550 FGAtlyIPTKETILDyqwfERYMSDNGIttatlPPTYAVYLNPDHMP--DFKRL---IAAGSASSLELLqqwKDKVKYFN 2624
Cdd:cd05917    79 FDP---LAVLEAIEK----EKCTALHGV-----PTMFIAELEHPDFDkfDLSSLrtgIMAGAPCPPELM---KRVIEVMN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2625 ------AYGPTEDSICTTIWTPSTEDISQLKSVpigGPIVNH-RIYIVDAHYQPVP-VGVAGELCIAGVGLARGYLNRPD 2696
Cdd:cd05917   144 mkdvtiAYGMTETSPVSTQTRTDDSIEKRVNTV---GRIMPHtEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2697 LTAEKfvdnpfEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVkIRG-YRIELGEIEEQLLKVASVQEAIVIA-HDDASGQ 2774
Cdd:cd05917   221 KTAEA------IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGvPDERYGE 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2775 kQLCAYFV--ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDR 2825
Cdd:cd05917   294 -EVCAWIRlkEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
2343-2828 7.07e-32

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 135.27  E-value: 7.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2343 ADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAY 2422
Cdd:PRK06155   19 SERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2423 VPIDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFA-------------GTVVTVDDEQAY------AGDGSNLESAVG 2483
Cdd:PRK06155   99 VPINTALRGPQLEHILRNSGARLLVVEAALLAALEAAdpgdlplpavwllDAPASVSVPAGWstaplpPLDAPAPAAAVQ 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2484 PNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDrvVQFASLS-FDASCWEVF-QTLFFGATLYIPTKET 2561
Cdd:PRK06155  179 PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD--VLYTTLPlFHTNALNAFfQALLAGATYVLEPRFS 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2562 ILDYqWFEryMSDNGITT-----ATLPPTYAVYLNPDHMPDFKRlIAAGSASSLELLQQWKDK--VKYFNAYGPTEdsic 2634
Cdd:PRK06155  257 ASGF-WPA--VRRHGATVtyllgAMVSILLSQPARESDRAHRVR-VALGPGVPAALHAAFRERfgVDLLDGYGSTE---- 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2635 ttiwtpstedisqlKSVPIGGPIVNHR------------IYIVDAHYQPVPVGVAGELCIAG---VGLARGYLNRPDLTA 2699
Cdd:PRK06155  329 --------------TNFVIAVTHGSQRpgsmgrlapgfeARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTV 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2700 EKFVDNPFEPGERMYRTgdlakwlPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCA 2779
Cdd:PRK06155  395 EAWRNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMA 467
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928 2780 YFVADRTMTVG--ELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK06155  468 AVVLRDGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
PRK09088 PRK09088
acyl-CoA synthetase; Validated
3863-4337 7.39e-32

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 134.16  E-value: 7.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3863 QALRNPDAVAVVFEKSQL--TYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPE 3940
Cdd:PRK09088    4 HARLQPQRLAAVDLALGRrwTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3941 DRIRYMLEDSGAQALLTQRHLR----ERVSFAGTFVAVDdeqayhADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEH 4016
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVAagrtDVEDLAAFIASAD------ALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4017 HGLCSLKLMFANTlqmteqDRVVQFASLSFDASCWEIF-------KALFFGATLYI-----PTSTT--ILDYPLfesymn 4082
Cdd:PRK09088  158 RNLQQTAHNFGVL------GRVDAHSSFLCDAPMFHIIglitsvrPVLAVGGSILVsngfePKRTLgrLGDPAL------ 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4083 enGITATILPPTYAAYL------NPDRMPSLKKLITGGSAASVEFVQQWKDK-VLYFNAYGPTEASIVTSIWDEASdsLG 4155
Cdd:PRK09088  226 --GITHYFCVPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWLDDgIPMVDGFGMSEAGTVFGMSVDCD--VI 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4156 DRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVdnpfepGERMYRTGDLVRWLPDG 4235
Cdd:PRK09088  302 RAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGWFRTGDIARRDADG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4236 NLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAngQQQLVAY-FVAQRELTA---AELRATMSQELPN 4311
Cdd:PRK09088  376 FFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADA--QWGEVGYlAIVPADGAPldlERIRSHLSTRLAK 453
                         490       500
                  ....*....|....*....|....*.
gi 386647928 4312 YMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK09088  454 YKVPKHLRLVDALPRTASGKLQKARL 479
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
7445-7928 7.62e-32

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 134.81  E-value: 7.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7445 EQTIHGLFEEQAERMPEKAAVVFEN-----TQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKA 7519
Cdd:PRK08008    6 GQHLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7520 GGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQ-------RHLQECVSFDGKVIAADDEQAYGEDGS--------------N 7578
Cdd:PRK08008   86 GAIMVPINARLLREESAWILQNSQASLLVTSaqfypmyRQIQQEDATPLRHICLTRVALPADDGVssftqlkaqqpatlC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7579 LEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQ-FASLSFDASCWEIFKALFFGATLYI 7657
Cdd:PRK08008  166 YAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTvMPAFHIDCQCTAAMAAFSAGATFVL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7658 PAK-------DTILDYplfesymnENGITAAILPPTYAIYLSP----DRLPSLKKLITGGSAASVE---FVQQWKdkVRY 7723
Cdd:PRK08008  246 LEKysarafwGQVCKY--------RATITECIPMMIRTLMVQPpsanDRQHCLREVMFYLNLSDQEkdaFEERFG--VRL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7724 FNAYGPTEasivTSVWAASPDGLDLRSVP-IGRPIANHQIFIVDSQNHMLPVGVAGELCISG-AG--LARGYLNRPELTA 7799
Cdd:PRK08008  316 LTSYGMTE----TIVGIIGDRPGDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYYLDPKATA 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7800 EKFVDNPFLagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCA 7879
Cdd:PRK08008  392 KVLEADGWL------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKA 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928 7880 Y--FVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK08008  466 FvvLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1323-1721 7.69e-32

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 133.49  E-value: 7.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 1402
Cdd:cd05907     6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 hlqeraqqwgqtlqavlclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQF 1482
Cdd:cd05907    86 -------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1483 PVRL--LQLASfsfdVF--VGDIARTLYNGGTMVICPKDDRIDPArlhywISEEKITIFESTPALIIPF---MDYVAEHG 1555
Cdd:cd05907   129 DRHLsfLPLAH----VFerRAGLYVPLLAGARIYFASSAETLLDD-----LSEVRPTVFLAVPRVWEKVyaaIKVKAVPG 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1556 LDMSSMELLITSSdscsvTDYRV-----LQERFGSQFR-----IINAYGVTE--AAIDSSLYDEplaklPEAGNVpiGKA 1623
Cdd:cd05907   200 LKRKLFDLAVGGR-----LRFAAsggapLPAELLHFFRalgipVYEGYGLTEtsAVVTLNPPGD-----NRIGTV--GKP 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1624 ALNAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRIDN 1703
Cdd:cd05907   268 LPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKD 331
                         410
                  ....*....|....*....
gi 386647928 1704 QAKIR-GYRIETGEIETQL 1721
Cdd:cd05907   332 LIITSgGKNISPEPIENAL 350
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
7456-7925 8.94e-32

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 134.93  E-value: 8.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVF-----ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:cd05970    27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLLT----------QRHLQECVSFDGKVIAADDEQ----AYGEDGSNLEPVVGPNH--------- 7587
Cdd:cd05970   107 TAKDIVYRIESADIKMIVAiaednipeeiEKAAPECPSKPKLVWVGDPVPegwiDFRKLIKNASPDFERPTansypcged 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7588 LAYVIYTSGTTGKPKgvMVEHHGLCSL----KLMFAETLRitEEDRVVQFASLSFDASCW-EIFKALFFGATLYIpakdt 7662
Cdd:cd05970   187 ILLVYFSSGTTGMPK--MVEHDFTYPLghivTAKYWQNVR--EGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFV----- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7663 iLDYPLFE-----SYMNENGITAAILPPTyaIY-------LSPDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYG 7728
Cdd:cd05970   258 -YDYDKFDpkallEKLSKYGVTTFCAPPT--IYrfliredLSRYDLSSLRYCTTAGEALNPEVFNTFKEKtgIKLMEGFG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7729 PTEasivTSVWAASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGA-----GLARGYLNRPELTAEKFV 7803
Cdd:cd05970   335 QTE----TTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWH 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7804 DNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA 7883
Cdd:cd05970   411 DG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVL 483
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 7884 DRELTVSElrgTLSQELPG--------YMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd05970   484 AKGYEPSE---ELKKELQDhvkkvtapYKYPRIVEFVDELPKTISGKIRR 530
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
257-685 8.94e-32

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 134.28  E-value: 8.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  257 PRDTTIHRLFEEQAERRPDAVA----VTfeDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILK 332
Cdd:cd05904     2 PTDLPLDSVSFLFASAHPSRPAlidaAT--GRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  333 AGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWIRLDDEEAYHEDGSNLESVNGPEHLTYVI------ 406
Cdd:cd05904    80 LGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVvikqdd 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  407 -----YTSGTTGKPKGNLTTHRNII--------RVVKNTNYIDVTgqdkLLQLSSYSFDGSTFDIFGALLNGAKLVLVPK 473
Cdd:cd05904   160 vaallYSSGTTGRSKGVMLTHRNLIamvaqfvaGEGSNSDSEDVF----LCVLPMFHIYGLSSFALGLLRLGATVVVMPR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  474 etvLDVAKLAGLIEKQQISVMFITTAffnVLVDM--NPDC----LRHARAILFGGERVSVSH---VRKALGHLgpgKIKH 544
Cdd:cd05904   236 ---FDLEELLAAIERYKVTHLPVVPP---IVLALvkSPIVdkydLSSLRQIMSGAAPLGKELieaFRAKFPNV---DLGQ 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  545 VYGPTESTVFATSYDVHEvEEGAVSIPIGGPISNTAIYIVN-AQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFAD 623
Cdd:cd05904   307 GYGMTESTGVVAMCFAPE-KDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK 385
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  624 npfapgERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV 685
Cdd:cd05904   386 ------EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
5935-6420 9.26e-32

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 135.16  E-value: 9.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5935 KTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVP 6014
Cdd:PRK06710   24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6015 IDPDYPEDRIRYMLEDSGAKLLLVQGHLLDRAS---------------FADKL-------------------VNLNDDGA 6060
Cdd:PRK06710  104 TNPLYTERELEYQLHDSGAKVILCLDLVFPRVTnvqsatkiehvivtrIADFLpfpknllypfvqkkqsnlvVKVSESET 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6061 YH-------EDGSNLEPVNGPEH-LTYVIYTSGTTGRPKGVMVEHRNvvrLVKNT--------NYVELNEqthiLQTGAV 6124
Cdd:PRK06710  184 IHlwnsvekEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKN---LVSNTlmgvqwlyNCKEGEE----VVLGVL 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6125 VFdastFEIWG-------ALLNGGRLYVVRN---ETILDAVSLKNAIQQYGINTMW---LTAPLynqLSQQDsgmFAGLK 6191
Cdd:PRK06710  257 PF----FHVYGmtavmnlSIMQGYKMVLIPKfdmKMVFEAIKKHKVTLFPGAPTIYialLNSPL---LKEYD---ISSIR 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6192 TLIVGGDVLSVpHINRVLREHAGLSIVNGYGPTENTtfSTTHT-IVGEQKEAVPIGKPINNSTAYIVDSKL-SLLPVGVW 6269
Cdd:PRK06710  327 ACISGSAPLPV-EVQEKFETVTGGKLVEGYGLTESS--PVTHSnFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEI 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6270 GELIVGGDGVARGYLNRPELTAeKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKV 6349
Cdd:PRK06710  404 GEIVVKGPQIMKGYWNKPEETA-AVLQDGWL------HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 6350 ASVKEATVIVREDESGQKQLCAYFVAER--ELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK06710  477 EKVQEVVTIGVPDPYRGETVKAFVVLKEgtECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
4913-5385 1.04e-31

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 133.61  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAqGVKPNQLVGILADRSADLLVGALAVWKAGgaYVPLDPDYPS--DRIQFMLEDSAASVLLT 4990
Cdd:cd05909     8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKLAGIKTVLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4991 QTHLQERAQQWGQTLQAALClddEAAYAEDASN--------------------------VANVnEPHDLAYVIYTSGTTG 5044
Cdd:cd05909    85 SKQFIEKLKLHHLFDVEYDA---RIVYLEDLRAkiskadkckaflagkfppkwllrifgVAPV-QPDDPAVILFTSGSEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5045 RPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASF-SFDvFVGDIARTLYNGGTMVICPkddriDParLHY-----W 5118
Cdd:cd05909   161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFhSFG-LTGCLWLPLLSGIKVVFHP-----NP--LDYkkipeL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5119 ISEEKITIFESTPAliipFMDYVAE--HGLDMSSMVLLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAidsslyd 5196
Cdd:cd05909   233 IYDKKATILLGTPT----FLRGYARaaHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG--IRILEGYGTTECS------- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5197 ePLAKL--PEAGNVP--IGKAALNAKFYIVD-AHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfveGERLY 5271
Cdd:cd05909   300 -PVISVntPQSPNKEgtVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-------GDGWY 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5272 RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVR-EDA-KGQKVLCAHFTaeSELKLSEL 5349
Cdd:cd05909   372 DTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSvPDGrKGEKIVLLTTT--TDTDPSSL 449
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 5350 RSSLSQ-ELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05909   450 NDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1291-1795 1.04e-31

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 134.72  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1291 PDAPENEVFHALFE--KQAERTPEVAAVVYEND-----RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVG 1363
Cdd:cd05906     1 PLHRPEGAPRTLLEllLRAAERGPTKGITYIDAdgseeFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1364 ALAVWKAGGAYVPLDP----DYPSDRIQF------MLEDSaasVLLT----QTHLQERAQQWGQTLQAVLCLDDEAAYAE 1429
Cdd:cd05906    81 FWACVLAGFVPAPLTVpptyDEPNARLRKlrhiwqLLGSP---VVLTdaelVAEFAGLETLSGLPGIRVLSIEELLDTAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1430 DAsnVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLAsfsFDvFVGDIA----RTL 1505
Cdd:cd05906   158 DH--DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP---LD-HVGGLVelhlRAV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1506 YNGGTMVICPKDDRI-DPARLHYWISEEKITIFEStP----ALIIPFMDYVAEHGLDMSSMELLITSSDSCSV-TDYRVL 1579
Cdd:cd05906   232 YLGCQQVHVPTEEILaDPLRWLDLIDRYRVTITWA-PnfafALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAkTIRRLL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1580 Q--ERFGSQ-FRIINAYGVTE----AAIDSSLYDEPLAKLPEAgnVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGI 1652
Cdd:cd05906   311 RllEPYGLPpDAIRPAFGMTEtcsgVIYSRSFPTYDHSQALEF--VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1653 GVARGYLNRPELTEEKFVDSPFvegerlYRTGDLArWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVRE--A 1730
Cdd:cd05906   389 VVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfT 461
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 1731 VVVVREDAK-GQKVLCAYFTAESELK------LSELRSSLSQEL---PGYMIPsyfVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05906   462 AAFAVRDPGaETEELAIFFVPEYDLQdalsetLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
4912-5385 1.07e-31

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 134.30  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 4991
Cdd:cd12119    25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 THLQER-AQQWGQ--TLQAALCLDDEAAYAED------------ASNVANVNEP----HDLAYVIYTSGTTGRPKGVMIE 5052
Cdd:cd12119   105 RDFLPLlEAIAPRlpTVEHVVVMTDDAAMPEPagvgvlayeellAAESPEYDWPdfdeNTAAAICYTSGTTGNPKGVVYS 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5053 HRSLVntaagyrreyrldqfpvrLLQLASFSFDVF---VGDIA----------------RTLYNGGTMVIcPkDDRIDPA 5113
Cdd:cd12119   185 HRSLV------------------LHAMAALLTDGLglsESDVVlpvvpmfhvnawglpyAAAMVGAKLVL-P-GPYLDPA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5114 RLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSvtdyRVLQERFGSQF-RIINAYGVTEAA--I 5190
Cdd:cd12119   245 SLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVP----RSLIEAFEERGvRVIHAWGMTETSplG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5191 DSSLYDEPLAKLPEAGNVPI----GKAALNAKFYIVDAHLNPVPV--GVLGELCIGGIGVARGYLNRPELTEEKFVDSPF 5264
Cdd:cd12119   321 TVARPPSEHSNLSEDEQLALrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5265 vegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQK--VLCAHFTAES 5342
Cdd:cd12119   401 -------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErpLAVVVLKEGA 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 386647928 5343 ELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd12119   474 TVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
4891-5382 1.11e-31

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 134.90  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4891 ALFEKQAECTPEAAAVVYEND--RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 4968
Cdd:PRK12583   22 DAFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNIN 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4969 PDYPSDRIQFMLEDSAASVLLT---------QTHLQERAQQWGQT------------LQAALCLDDEA-----AYAE--- 5019
Cdd:PRK12583  102 PAYRASELEYALGQSGVRWVICadafktsdyHAMLQELLPGLAEGqpgalacerlpeLRGVVSLAPAPppgflAWHElqa 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5020 --DASNVANVNE------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ-----FPVRLLQlasfSFDV 5086
Cdd:PRK12583  182 rgETVSREALAErqasldRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEhdrlcVPVPLYH----CFGM 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5087 FVGDIArTLYNGGTMVIcpKDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDY 5166
Cdd:PRK12583  258 VLANLG-CMTVGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVM 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5167 -RVLQERFGSQFRIinAYGVTEAA--IDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIG 5243
Cdd:PRK12583  335 rRVMDEMHMAEVQI--AYGMTETSpvSLQTTAADDLERRVET----VGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYS 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5244 VARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVV 5323
Cdd:PRK12583  409 VMKGYWNNPEATAES------IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 5324 VREDAKGQKVLCAHFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 5382
Cdd:PRK12583  483 GVPDEKYGEEIVAWVRLHPGHAASeeELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
255-747 1.21e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 134.70  E-value: 1.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  255 DYPRdTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKA 333
Cdd:PRK08314    6 TLPE-TSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  334 GGAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERV---------------SFSGT-----------WIR-------L 380
Cdd:PRK08314   85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaQYSDYlpaepeiavpaWLRaepplqaL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  381 DDEEAYH-----EDGSNLESVN-GPEHLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDKLLQ-LSSYSFD 452
Cdd:PRK08314  165 APGGVVAwkealAAGLAPPPHTaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMaNAVGSVLWSNSTPESVVLAvLPLFHVT 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  453 GSTFDIFGALLNGAKLVLVP---KETVLDvaklagLIEKQQISVMfitTAFFNVLVD--MNPD----CLRHARAILFGGE 523
Cdd:PRK08314  245 GMVHSMNAPIYAGATVVLMPrwdREAAAR------LIERYRVTHW---TNIPTMVVDflASPGlaerDLSSLRYIGGGGA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  524 RVSVSHVRKALGHLGpgkIKHV--YGPTESTVFATSYDVHEVEEGAVSIpiggPISNTAIYIVNAQNkLQ--PIGVAGEL 599
Cdd:PRK08314  316 AMPEAVAERLKELTG---LDYVegYGLTETMAQTHSNPPDRPKLQCLGI----PTFGVDARVIDPET-LEelPPGEVGEI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  600 CVAGDGLARGYLNRPDLTAEKFADnpfAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAI 679
Cdd:PRK08314  388 VVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  680 EKATVV-VRESANGE--KQLCAYYVADRSLP-ANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK08314  465 QEACVIaTPDPRRGEtvKAVVVLRPEARGKTtEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
5945-6417 1.35e-31

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 134.16  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTF-----EDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDY 6019
Cdd:cd05970    27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6020 PEDRIRYMLEDSGAKLLLV--QGHLLDRASFA-------DKLVNLND---DG--AYHEDGSNLEPVNGPEH--------- 6076
Cdd:cd05970   107 TAKDIVYRIESADIKMIVAiaEDNIPEEIEKAapecpskPKLVWVGDpvpEGwiDFRKLIKNASPDFERPTansypcged 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6077 LTYVIYTSGTTGRPKgvMVEHRNVVRL---VKNTNYVELNEQT-H--ILQTGAVvfDASTFEIWGALLNGGRLYVVRNET 6150
Cdd:cd05970   187 ILLVYFSSGTTGMPK--MVEHDFTYPLghiVTAKYWQNVREGGlHltVADTGWG--KAVWGKIYGQWIAGAAVFVYDYDK 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6151 iLDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGM--FAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTENTT 6228
Cdd:cd05970   263 -FDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRydLSSLRYCTTAGEALN-PEVFNTFKEKTGIKLMEGFGQTETTL 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6229 fsTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGD-----GVARGYLNRPELTAEKFVESsflpge 6303
Cdd:cd05970   341 --TIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG------ 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6304 rCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGE 6383
Cdd:cd05970   413 -YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSE 491
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928 6384 lraALSQELPN--------YMIPSHFVPLERMPLTPNGKIDR 6417
Cdd:cd05970   492 ---ELKKELQDhvkkvtapYKYPRIVEFVDELPKTISGKIRR 530
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
3820-4339 1.44e-31

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 133.97  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3820 SPNAPVSMLELVTEAekaeiihvfnntaaeYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDA 3899
Cdd:PRK13383   16 NPPSPRAVLRLLREA---------------SRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3900 GVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVDDEQA 3979
Cdd:PRK13383   81 GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3980 YHADGSNLEPVVGPNHlAYVIYTSGTTGKPKGVMVEHHglcsLKLMFANTLQMTEQDRVVQFASLSFDAScweIFKALFF 4059
Cdd:PRK13383  161 AGAEESGGRPAVAAPG-RIVLLTSGTTGKPKGVPRAPQ----LRSAVGVWVTILDRTRLRTGSRISVAMP---MFHGLGL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4060 GA-TLYIPTSTTILDYPLFE--------SYMNENGITAtiLPPTYAAYLN-PDR------MPSLKKLITGGSAASVEFVQ 4123
Cdd:PRK13383  233 GMlMLTIALGGTVLTHRHFDaeaalaqaSLHRADAFTA--VPVVLARILElPPRvrarnpLPQLRVVMSSGDRLDPTLGQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4124 QWKD---KVLYfNAYGPTEASIvtsiwdEASDSLGDRKSVP--IGRPLANHRIYVVDSHNRmlPVG--VAGELCISGvgl 4196
Cdd:PRK13383  311 RFMDtygDILY-NGYGSTEVGI------GALATPADLRDAPetVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGG--- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4197 argylnrpELTAEKFVDNPFEPG-ERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVL 4275
Cdd:PRK13383  379 --------ELAGTRYTDGGGKAVvDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVI 450
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 4276 AREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:PRK13383  451 GVPDERFGHRLAAFVVLHpgSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
4913-5311 1.44e-31

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 132.72  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 4992
Cdd:cd05907     6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 hlqeraqqwgqtlqaalclddeaayaedasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQF 5072
Cdd:cd05907    86 -------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5073 PVRL--LQLASfsfdVF--VGDIARTLYNGGTMVICPKDDRIDPArlhywISEEKITIFESTPALIIPF---MDYVAEHG 5145
Cdd:cd05907   129 DRHLsfLPLAH----VFerRAGLYVPLLAGARIYFASSAETLLDD-----LSEVRPTVFLAVPRVWEKVyaaIKVKAVPG 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5146 LDMssMVLLITSSDSCsvtdyRV-------LQERFGSQFR-----IINAYGVTE--AAIDSSLYDEplaklPEAGNVpiG 5211
Cdd:cd05907   200 LKR--KLFDLAVGGRL-----RFaasggapLPAELLHFFRalgipVYEGYGLTEtsAVVTLNPPGD-----NRIGTV--G 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5212 KAALNAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRI 5291
Cdd:cd05907   266 KPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRK 329
                         410       420
                  ....*....|....*....|.
gi 386647928 5292 DNQAKIR-GYRIETGEIETQL 5311
Cdd:cd05907   330 KDLIITSgGKNISPEPIENAL 350
PRK07787 PRK07787
acyl-CoA synthetase; Validated
2362-2831 1.45e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 132.81  E-value: 1.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2362 PAVVFEGQQLTYRELNERANRLARTLQALGvktdqPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDS 2441
Cdd:PRK07787   17 DAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2442 SAQVLLAQRRLQERvsfAGTVVTVDdeqaYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTL 2521
Cdd:PRK07787   92 GAQAWLGPAPDDPA---GLPHVPVR----LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2522 QINAQD--------------------------RVVQFASLSFDAscweVFQTLFFGATLY--IPTketildyQWfERYMS 2573
Cdd:PRK07787  165 QWTADDvlvhglplfhvhglvlgvlgplrignRFVHTGRPTPEA----YAQALSEGGTLYfgVPT-------VW-SRIAA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2574 DNGIT------------TATLPptyavylnpdhMPDFKRLIAAGSASSLEllqqwkdkvkyfnAYGPTEdsictTIWTPS 2641
Cdd:PRK07787  233 DPEAAralrgarllvsgSAALP-----------VPVFDRLAALTGHRPVE-------------RYGMTE-----TLITLS 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2642 TEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVA--GELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDL 2719
Cdd:PRK07787  284 TRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDV 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2720 AKWLPDGTIEYLGR--IDhQVKIRGYRIELGEIEEQLLKVASVQEAIVI-AHDDASGQkQLCAYFVADRTMTVGELRGEL 2796
Cdd:PRK07787  358 AVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVgVPDDDLGQ-RIVAYVVGADDVAADELIDFV 435
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 386647928 2797 SGELPGYMIPAHFVQLERMPLTPNGKIDRKALPAP 2831
Cdd:PRK07787  436 AQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
4906-5382 1.46e-31

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 132.95  E-value: 1.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4906 VVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAA 4985
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4986 SVLLtqthlqeraqqwgqtlqaalclddeaayaedasnvanVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR 5065
Cdd:cd05914    81 KAIF-------------------------------------VSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5066 EYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICpkdDRIDPARLhywiseEKITIFESTPALIIPFMdYVAEH- 5144
Cdd:cd05914   124 VVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL---DKIPSAKI------IALAFAQVTPTLGVPVP-LVIEKi 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5145 -------GLDMSSMVLLITS---SDSCSVTDYRVLQERFGSQFRII-----------------------NAYGVTEAAid 5191
Cdd:cd05914   194 fkmdiipKLTLKKFKFKLAKkinNRKIRKLAFKKVHEAFGGNIKEFviggakinpdveeflrtigfpytIGYGMTETA-- 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5192 sslydePLAklpeAGNVP-------IGKAALNAKFYIVDahlnPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspf 5264
Cdd:cd05914   272 ------PII----SYSPPnrirlgsAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK--- 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5265 vegERLYRTGDLARWMPDGNVDFIGRIDNQAKI-RGYRIETGEIETQLLKAEgVREAVVVVREDAKGQKVLCAHFTAESE 5343
Cdd:cd05914   335 ---DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMP-FVLESLVVVQEKKLVALAYIDPDFLDV 410
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 5344 LKLS----------ELRSSLSQELPGY-MIPSYFVQLEQLPLTANGKIDR 5382
Cdd:cd05914   411 KALKqrniidaikwEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1307-1795 1.82e-31

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 133.09  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 1386
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QFMLEDSAASVLLTQTHLQERAQQwgQTLQAVLcldDEAAYAE--------DASNVANVNEPHDLAYVIYTSGTTGRPKG 1458
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVAL--ETPKIVI---DAAAQADsrrlaqggLEIPPQAAVAPTDLVRLMYTSGTTDRPKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1459 VMIEH-----RSLVNTAA-GYRREYRL----DQFPVRLLQLASFSfdvfvgdiarTLYNGGTMVIcpkDDRIDPARLHYW 1528
Cdd:PRK06145  167 VMHSYgnlhwKSIDHVIAlGLTASERLlvvgPLYHVGAFDLPGIA----------VLWVGGTLRI---HREFDPEAVLAA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1529 ISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTEAAIDSSLYdEP 1608
Cdd:PRK06145  234 IERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVF-TRARYIDAYGLTETCSGDTLM-EA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1609 LAKLPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLAR 1688
Cdd:PRK06145  312 GREIEKIGST--GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGY 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1689 WMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAYFTAE-SELKLSELRSSLSQE 1766
Cdd:PRK06145  383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPgATLTLEALDRHCRQR 462
                         490       500
                  ....*....|....*....|....*....
gi 386647928 1767 LPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK06145  463 LASFKVPRQLKVRDELPRNPSGKVLKRVL 491
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
3861-4332 2.00e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 133.75  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3861 EEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGV-RPDQLVGLMVERSlEMVVGIMAIMKAGGAYIPIDPEYP 3939
Cdd:PRK07786   24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVgFGDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFRLT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3940 EDRIRYMLEDSGAQALLTQRHL-------RERVSFAGTFVAVDD---------EQAYHADGSNLEPVVGPNHL-AYVIYT 4002
Cdd:PRK07786  103 PPEIAFLVSDCGAHVVVTEAALapvatavRDIVPLLSTVVVAGGssddsvlgyEDLLAEAGPAHAPVDIPNDSpALIMYT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4003 SGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFD-ASCWEIFKALFFGATLYI-PTS----TTILDypl 4076
Cdd:PRK07786  183 SGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIyPLGafdpGQLLD--- 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4077 fesYMNENGITATILPPTY-----AAYLNPDRMPSLKKLITGGSAASVEFVQQWKD---KVLYFNAYGPTEASIVTSIWD 4148
Cdd:PRK07786  260 ---VLEAEKVTGIFLVPAQwqavcAEQQARPRDLALRVLSWGAAPASDTLLRQMAAtfpEAQILAAFGQTEMSPVTCMLL 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4149 eASDSLGDRKSVpiGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEpgermyrTGDL 4228
Cdd:PRK07786  337 -GEDAIRKLGSV--GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------SGDL 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4229 VRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV---AQRELTAAELRATM 4305
Cdd:PRK07786  407 VRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnDDAALTLEDLAEFL 486
                         490       500
                  ....*....|....*....|....*..
gi 386647928 4306 SQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK07786  487 TDRLARYKHPKALEIVDALPRNPAGKV 513
PRK08315 PRK08315
AMP-binding domain protein; Validated
1301-1790 2.18e-31

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 134.17  E-value: 2.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1301 ALFEKQAERTPEVAAVVY--ENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 1378
Cdd:PRK08315   20 QLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1379 PDYPSDRIQFMLEDSAASVLLTQTH---------LQE-----RAQQWGQ-------TLQAVLCLDDEA-----AYAEDAS 1432
Cdd:PRK08315  100 PAYRLSELEYALNQSGCKALIAADGfkdsdyvamLYElapelATCEPGQlqsarlpELRRVIFLGDEKhpgmlNFDELLA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1433 NVANVNE-----------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA------GYRREYRLdQFPVRLLQlasfSFD 1495
Cdd:PRK08315  180 LGRAVDDaelaarqatldPDDPINIQYTSGTTGFPKGATLTHRNILNNGYfigeamKLTEEDRL-CIPVPLYH----CFG 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1496 VFVGDIArTLYNGGTMVIcPKDdRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTD 1575
Cdd:PRK08315  255 MVLGNLA-CVTHGATMVY-PGE-GFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIEV 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1576 YRVLQERFG-SQFRIinAYGVTEAA--IDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLN-PVPVGVLGELCIGG 1651
Cdd:PRK08315  332 MKRVIDKMHmSEVTI--AYGMTETSpvSTQTRTDDPLEKRVTT----VGRALPHLEVKIVDPETGeTVPRGEQGELCTRG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1652 IGVARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIdnqaK---IRG----Y-RietgEIETQLLK 1723
Cdd:PRK08315  406 YSVMKGYWNDPEKTAEA------IDADGWMHTGDLAVMDEEGYVNIVGRI----KdmiIRGgeniYpR----EIEEFLYT 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 1724 AEGVREAVVVVREDAKGQKVLCAYFTAE--SELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:PRK08315  472 HPKIQDVQVVGVPDEKYGEEVCAWIILRpgATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
PRK06188 PRK06188
acyl-CoA synthetase; Validated
5946-6423 2.25e-31

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 133.57  E-value: 2.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5946 ERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIR 6025
Cdd:PRK06188   23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6026 YMLEDSGAKLLLVQ--------GHLLDRASFADKLVNLND--------DGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGR 6089
Cdd:PRK06188  103 YVLEDAGISTLIVDpapfveraLALLARVPSLKHVLTLGPvpdgvdllAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6090 PKGVMVEHRNVVRLvknTNYV----ELNEQTHILQTGAVVFDASTFeIWGALLNGGRLYVVRNetiLDAVSLKNAIQQYG 6165
Cdd:PRK06188  183 PKGVMGTHRSIATM---AQIQlaewEWPADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVLAK---FDPAEVLRAIEEQR 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6166 IN-TMWLTAPLYNQLSQQDSGM--FAGLKTLIVGGDVLS----VPHINRVlrehaGLSIVNGYGPTEN----TTFSTTHT 6234
Cdd:PRK06188  256 ITaTFLVPTMIYALLDHPDLRTrdLSSLETVYYGASPMSpvrlAEAIERF-----GPIFAQYYGQTEApmviTYLRKRDH 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6235 IVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFvESSFLpgercyRTGDLARW 6314
Cdd:PRK06188  331 DPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWL------HTGDVARE 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6315 LPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFV--AERELTIGELRAALSQEL 6392
Cdd:PRK06188  404 DEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVlrPGAAVDAAELQAHVKERK 483
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 6393 PNYMIPSHFVPLERMPLTPNGKIDRRALPAP 6423
Cdd:PRK06188  484 GSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
7472-7925 2.42e-31

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 132.18  E-value: 2.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTqr 7551
Cdd:cd05914     8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 hlqecvsfdgkviaADDEQaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVV 7631
Cdd:cd05914    86 --------------SDEDD-----------------VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKIL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7632 QFASLSFDASC-WEIFKALFFGATLY----IPAKDTILD--------------YPLFESYMNE--NGITAAILPPTYAIY 7690
Cdd:cd05914   135 SILPLHHIYPLtFTLLLPLLNGAHVVfldkIPSAKIIALafaqvtptlgvpvpLVIEKIFKMDiiPKLTLKKFKFKLAKK 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7691 LSPDRLPSL-------------KKLITGGSAASVEFVQQWKD-KVRYFNAYGPTEAS--IVTSVWAaspdglDLRSVPIG 7754
Cdd:cd05914   215 INNRKIRKLafkkvheafggniKEFVIGGAKINPDVEEFLRTiGFPYTIGYGMTETApiISYSPPN------RIRLGSAG 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7755 RPIANHQIFIVDSQnhmlPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRI 7834
Cdd:cd05914   289 KVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWF------HTGDLGKIDAEGYLYIRGRK 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7835 DHQ-VKIRGYRIELGEIEEQLLKIASVQETIVIARgdaNGQQQLCAYFVADRELTVS------------ELRGTLSQELP 7901
Cdd:cd05914   359 KEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQ---EKKLVALAYIDPDFLDVKAlkqrniidaikwEVRDKVNQKVP 435
                         490       500
                  ....*....|....*....|....*
gi 386647928 7902 GY-MIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd05914   436 NYkKISKVKIVKEEFEKTPKGKIKR 460
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
5930-6420 2.73e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 133.74  E-value: 2.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5930 KYPSdktIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRN-AGVQPDQMVGLMVERSLEMVVGMIAILKA 6008
Cdd:PRK05677   22 EYPN---IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6009 GGAYVPIDPDYPEDRIRYMLEDSGAKLLLV---QGHLLDR------------ASFADKL--------------------- 6052
Cdd:PRK05677   99 GLIVVNTNPLYTAREMEHQFNDSGAKALVClanMAHLAEKvlpktgvkhvivTEVADMLpplkrllinavvkhvkkmvpa 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6053 ------VNLND---DGAyhedGSNLEPVN-GPEHLTYVIYTSGTTGRPKGVMVEHRNVVR---LVKNTNYVELNEQTHIL 6119
Cdd:PRK05677  179 yhlpqaVKFNDalaKGA----GQPVTEANpQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCRALMGSNLNEGCEIL 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6120 QTGAVVFD--ASTFEIWGALLNGGRLYVVRNETILDAVSLKNAIQQY----GINTmwltapLYNQLSQQDSGM---FAGL 6190
Cdd:PRK05677  255 IAPLPLYHiyAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFsgfvGLNT------LFVALCNNEAFRkldFSAL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6191 KTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAvpIGKPINNSTAYIVDSKLSLLPVGVWG 6270
Cdd:PRK05677  329 KLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGT--IGIPVPSTLCKVIDDDGNELPLGEVG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6271 ELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVA 6350
Cdd:PRK05677  406 ELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALP 479
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 6351 SVKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK05677  480 GVLQCAAIGVPDEKSGEAIKVFVVVKpgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
270-746 3.22e-31

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 133.13  E-value: 3.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPDAVAVTF------EDRQLTYGELNERANRLARTLRNAGVQADqLVGLMVERSLEMIVGIMGILKAGGAYVPI-DP 342
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  343 EYPE--ERIRYMLEDSGTQVLLSQ--------GHLQERVSFSGTWIRLDDeeAYHEDGSNLESVNGPEH--LTYVIYTSG 410
Cdd:cd05931    82 TPGRhaERLAAILADAGPRVVLTTaaalaavrAFAASRPAAGTPRLLVVD--LLPDTSAADWPPPSPDPddIAYLQYTSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  411 TTGKPKGNLTTHRNIIRVVkntnyidvtgqdKLLQLSSYSFDGSTF--------D------IFGALLNGAKLVLVPKET- 475
Cdd:cd05931   160 STGTPKGVVVTHRNLLANV------------RQIRRAYGLDPGDVVvswlplyhDmgliggLLTPLYSGGPSVLMSPAAf 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  476 VLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDC------LRHARAILFGGERVSVSHVRK------ALGhLGPGKIK 543
Cdd:cd05931   228 LRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEdlegldLSSWRVALNGAEPVRPATLRRfaeafaPFG-FRPEAFR 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  544 HVYGPTESTVFATS-----------YDVHEVEEGAVSIPIGG-----------PISNTAIYIVNAQ-NKLQPIGVAGELC 600
Cdd:cd05931   307 PSYGLAEATLFVSGgppgtgpvvlrVDRDALAGRAVAVAADDpaarelvscgrPLPDQEVRIVDPEtGRELPDGEVGEIW 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  601 VAGDGLARGYLNRPDLTAEKFADNPFAPGERMYRTGDLARwLPDGTIEYVGRIDDQVKIRGfR------IE--LGEIEAH 672
Cdd:cd05931   387 VRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRG-RnhypqdIEatAEEAHPA 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  673 LLKL---------EAIEKATVVVRESANGEKqlcayyVADRSLpANEVRSTLSQE--LPAYMLpsYFVQLEQMPLTTNGK 741
Cdd:cd05931   465 LRPGcvaafsvpdDGEERLVVVAEVERGADP------ADLAAI-AAAIRAAVAREhgVAPADV--VLVRPGSIPRTSSGK 535

                  ....*
gi 386647928  742 VDRRA 746
Cdd:cd05931   536 IQRRA 540
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
7454-7928 3.84e-31

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 132.79  E-value: 3.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7454 EQAERMPEKAAVVFENTQ-----LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGG--AYVPI 7526
Cdd:cd05906    17 LRAAERGPTKGITYIDADgseefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFvpAPLTV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7527 DPEYPEDR--------IRYMLED-------SGAQVLLTQRHLQECVSFDgkVIAADDEQAYGEDgSNLePVVGPNHLAYV 7591
Cdd:cd05906    97 PPTYDEPNarlrklrhIWQLLGSpvvltdaELVAEFAGLETLSGLPGIR--VLSIEELLDTAAD-HDL-PQSRPDDLALL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7592 IYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDrvVQFASLSFD--ASCWEI-FKALFFGA-TLYIPAkDTILDYP 7667
Cdd:cd05906   173 MLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQD--VFLNWVPLDhvGGLVELhLRAVYLGCqQVHVPT-EEILADP 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7668 L-FESYMNENGITAAiLPPTYAIYLSPDRLP----------SLKKLITGG----SAASVEFVQQWK------DKVRyfNA 7726
Cdd:cd05906   250 LrWLDLIDRYRVTIT-WAPNFAFALLNDLLEeiedgtwdlsSLRYLVNAGeavvAKTIRRLLRLLEpyglppDAIR--PA 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7727 YGPTEAS---IVTSVWAASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFV 7803
Cdd:cd05906   327 FGMTETCsgvIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFT 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7804 DNPFlagermYRTGDLArWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIA---RGDANGQQQLCAY 7880
Cdd:cd05906   407 EDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAfavRDPGAETEELAIF 479
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 7881 FV------ADRELTVSELRGTLSQEL---PGYMIPsyfVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05906   480 FVpeydlqDALSETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
7446-7932 3.97e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 133.23  E-value: 3.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7446 QTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVP 7525
Cdd:PRK06710   24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7526 IDPEYPEDRIRYMLEDSGAQVLLTQ-------RHLQECVSFDGKVIA----------------------------ADDEQ 7570
Cdd:PRK06710  104 TNPLYTERELEYQLHDSGAKVILCLdlvfprvTNVQSATKIEHVIVTriadflpfpknllypfvqkkqsnlvvkvSESET 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7571 AY------GEDGSNLEPVVGP-NHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSF----- 7638
Cdd:PRK06710  184 IHlwnsveKEVNTGVEVPCDPeNDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFfhvyg 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7639 -----DASCWEIFKALFfgatlyIPAKDTILdypLFESyMNENGITaaILPPTYAIYLSPDRLPSLKKL--------ITG 7705
Cdd:PRK06710  264 mtavmNLSIMQGYKMVL------IPKFDMKM---VFEA-IKKHKVT--LFPGAPTIYIALLNSPLLKEYdissiracISG 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7706 GSAASVEfVQQWKDKV---RYFNAYGPTEASIVTS---VWAASPDGldlrsvPIGRPIANHQIFIVDSQN-HMLPVGVAG 7778
Cdd:PRK06710  332 SAPLPVE-VQEKFETVtggKLVEGYGLTESSPVTHsnfLWEKRVPG------SIGVPWPDTEAMIMSLETgEALPPGEIG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7779 ELCISGAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIA 7858
Cdd:PRK06710  405 EIVVKGPQIMKGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 7859 SVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAPE 7932
Cdd:PRK06710  478 KVQEVVTIGVPDPYRGETVKAFVVlkEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
5933-6417 4.37e-31

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 132.97  E-value: 4.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5933 SDKTIHQLFEEQAERIPDHLAVTF--EDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGG 6010
Cdd:PRK12583   16 LTQTIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6011 AYVPIDPDYPEDRIRYMLEDSGAKLLLvqghLLDRASFAD----------KLVNLNDDGAYHEDGSNLEPV-----NGPE 6075
Cdd:PRK12583   96 ILVNINPAYRASELEYALGQSGVRWVI----CADAFKTSDyhamlqellpGLAEGQPGALACERLPELRGVvslapAPPP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTY------------------------------VIYTSGTTGRPKGVMVEHRNVVrlvkNTNYVeLNEQTHILQTGAVV 6125
Cdd:PRK12583  172 GFLAwhelqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNIL----NNGYF-VAESLGLTEHDRLC 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6126 FDASTFEIWGALLNG------GRLYVVRNE-----TILDAVSLKNAIQQYGINTMWLTaplynQLSQQDSGMF--AGLKT 6192
Cdd:PRK12583  247 VPVPLYHCFGMVLANlgcmtvGACLVYPNEafdplATLQAVEEERCTALYGVPTMFIA-----ELDHPQRGNFdlSSLRT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6193 LIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGE-QKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGE 6271
Cdd:PRK12583  322 GIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDlERRVETVGRTQPHLEVKVVDPDGATVPRGEIGE 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6272 LIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVAS 6351
Cdd:PRK12583  402 LCTRGYSVMKGYWNNPEATAESIDEDGWM------HTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPA 475
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 6352 VKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDR 6417
Cdd:PRK12583  476 VADVQVFGVPDEKYGEEIVAWVRLHpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
3859-4337 5.15e-31

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 132.32  E-value: 5.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVF--EKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDP 3936
Cdd:PRK05852   21 LVEVAATRLPEAPALVVtaDRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3937 EYPEDRIRYMLEDSGAQALLTQR---HLRERVSFAGTFVAVDDEQAYHADGSNLEPVVG----PNHL-----------AY 3998
Cdd:PRK05852  101 ALPIAEQRVRSQAAGARVVLIDAdgpHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDaatePTPAtstpeglrpddAM 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3999 VIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASL----SFDAScweIFKALFFGATLYIPTSTTILDY 4074
Cdd:PRK05852  181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLyhghGLIAA---LLATLASGGAVLLPARGRFSAH 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4075 PLFESYMNENGITATILPPTYAAYLN-PDRMPSLKK-----LITGGSAA-SVEFVQQWKDKVL--YFNAYGPTEAS--IV 4143
Cdd:PRK05852  258 TFWDDIKAVGATWYTAVPTIHQILLErAATEPSGRKpaalrFIRSCSAPlTAETAQALQTEFAapVVCAFGMTEAThqVT 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4144 TSIWDEASDSLGDRKSV-PIGRPLANhRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgerm 4222
Cdd:PRK05852  338 TTQIEGIGQTENPVVSTgLVGRSTGA-QIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL------ 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4223 yRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV--AQRELTAAE 4300
Cdd:PRK05852  411 -RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVprESAPPTAEE 489
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 4301 LRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK05852  490 LVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
3851-4315 5.61e-31

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 133.46  E-value: 5.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3851 QQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGA 3930
Cdd:PRK08279   34 DSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3931 YIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVDDEQAYHADGSNLEPV-------------------- 3990
Cdd:PRK08279  114 VALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEgyedlaaaaagapttnpasr 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3991 --VGPNHLAYVIYTSGTTGKPKGVMVEHH-GLCSLKlMFANTLQMTEQDR-------------VVQFASL---------- 4044
Cdd:PRK08279  194 sgVTAKDTAFYIYTSGTTGLPKAAVMSHMrWLKAMG-GFGGLLRLTPDDVlycclplyhntggTVAWSSVlaagatlalr 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4045 -SFDASC-WEIFKAlfFGATL--YI----------PTSTTILDYPLfeSYMNENGITATILPptyaaylnpdrmpslkkl 4110
Cdd:PRK08279  273 rKFSASRfWDDVRR--YRATAfqYIgelcryllnqPPKPTDRDHRL--RLMIGNGLRPDIWD------------------ 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4111 itggsaasvEFVQQWK-DKVLYFnaYGPTEASIVTSIWDEASDSLGdrkSVPiGRPLANHRI---------YVVDSHNRM 4180
Cdd:PRK08279  331 ---------EFQQRFGiPRILEF--YAASEGNVGFINVFNFDGTVG---RVP-LWLAHPYAIvkydvdtgePVRDADGRC 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4181 LPVGvAGE--LCISGVGLAR---GYlNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIE 4255
Cdd:PRK08279  396 IKVK-PGEvgLLIGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVA 473
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 4256 LGEVETQLAKIDAVQEAIVLARE--DANGQQQLVAYFVAQ-RELTAAELRATMSQELPNYMIP 4315
Cdd:PRK08279  474 TTEVENALSGFPGVEEAVVYGVEvpGTDGRAGMAAIVLADgAEFDLAALAAHLYERLPAYAVP 536
PRK07514 PRK07514
malonyl-CoA synthase; Validated
4889-5311 6.67e-31

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 131.54  E-value: 6.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4889 FHALFEKQAEctPEAAAV-VYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPL 4967
Cdd:PRK07514    6 FDALRAAFAD--RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4968 DPDYPSDRIQFMLEDSAASVLLtqthLQERAQQWGQTLQAA------LCLDD-------EAAYAEDASNVANVNEPHDLA 5034
Cdd:PRK07514   84 NTAYTLAELDYFIGDAEPALVV----CDPANFAWLSKIAAAagaphvETLDAdgtgsllEAAAAAPDDFETVPRGADDLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5035 YVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASF-SFDVFVGdIARTLYNGGTMVICPKddrIDPA 5113
Cdd:PRK07514  160 AILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFhTHGLFVA-TNVALLAGASMIFLPK---FDPD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5114 RLHYWIseEKITIFESTPALiipfmdYV---AEHGLD---MSSMVLLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTE 5187
Cdd:PRK07514  236 AVLALM--PRATVMMGVPTF------YTrllQEPRLTreaAAHMRLFISGSAPLLAETHREFQERTG--HAILERYGMTE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5188 AAIDSSlydEPLAKLPEAGNVpiGKAALNAKFYIVDAHLN-PVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFve 5266
Cdd:PRK07514  306 TNMNTS---NPYDGERRAGTV--GFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-- 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 5267 gerlYRTGDLARWMPDGNVDFIGRidnqAK---IR-GYRIETGEIETQL 5311
Cdd:PRK07514  379 ----FITGDLGKIDERGYVHIVGR----GKdliISgGYNVYPKEVEGEI 419
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
257-747 7.17e-31

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 132.19  E-value: 7.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  257 PRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGA 336
Cdd:PRK06155   18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  337 YVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERV--------SFSGTWIrLDDEEAYHED-----------GSNLESVN 397
Cdd:PRK06155   98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALeaadpgdlPLPAVWL-LDAPASVSVPagwstaplpplDAPAPAAA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  398 -GPEHLTYVIYTSGTTGKPKGNLTTH-------RNIIRVvkntnyIDVTGQDKLLqlssysfdgSTFDIF---------G 460
Cdd:PRK06155  177 vQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAED------LEIGADDVLY---------TTLPLFhtnalnaffQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  461 ALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPdclrharailfgGERVSVSHVRKALGHLGPG 540
Cdd:PRK06155  242 ALLAGATYVLEPR---FSASGFWPAVRRHGATVTYLLGAMVSILLSQPA------------RESDRAHRVRVALGPGVPA 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  541 KIkHV-------------YGPTESTVfatsydvheveegavsiPIGGPISNT------------AIYIVNAQNKLQPIGV 595
Cdd:PRK06155  307 AL-HAafrerfgvdlldgYGSTETNF-----------------VIAVTHGSQrpgsmgrlapgfEARVVDEHDQELPDGE 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  596 AGELCVAGD---GLARGYLNRPDLTAEKFADNPFAPGERMYRTgdlarwlPDGTIEYVGRIDDQVKIRGFRIELGEIEAH 672
Cdd:PRK06155  369 PGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQV 441
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  673 LLKLEAIEKATVVVRESANGEKQLCAYYVAD--RSL-PANEVRSTLSQeLPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK06155  442 LLSHPAVAAAAVFPVPSELGEDEVMAAVVLRdgTALePVALVRHCEPR-LAYFAVPRYVEFVAALPKTENGKVQKFVL 518
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
7473-7928 8.61e-31

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 129.91  E-value: 8.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7473 TYRELNERANRLARTLRAEGVQA-DQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTqr 7551
Cdd:cd05958    12 TYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC-- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 hlqecvsfDGKVIAADDeqaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMvehHGLCSLKLMF----AETLRITEE 7627
Cdd:cd05958    90 --------AHALTASDD-------------------ICILAFTSGTTGAPKATM---HFHRDPLASAdryaVNVLRLRED 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7628 DRVVQFASLSFD-ASCWEIFKALFFGATLYIPAKDTIldyPLFESYMNENGITAAILPPT--YAIYLSPDR----LPSLK 7700
Cdd:cd05958   140 DRFVGSPPLAFTfGLGGVLLFPFGVGASGVLLEEATP---DLLLSAIARYKPTVLFTAPTayRAMLAHPDAagpdLSSLR 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7701 KLITGGSAASVEFVQQWKDK--VRYFNAYGPTEA-SIVTSvwaASPDglDLRSVPIGRPIANHQIFIVDSQNHMLPVGVA 7777
Cdd:cd05958   217 KCVSAGEALPAALHRAWKEAtgIPIIDGIGSTEMfHIFIS---ARPG--DARPGATGKPVPGYEAKVVDDEGNPVPDGTI 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7778 GELCISGAglaRGYLNRPELTAEKFVDNPFLAgermyrTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKI 7857
Cdd:cd05958   292 GRLAVRGP---TGCRYLADKRQRTYVQGGWNI------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQH 362
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 7858 ASVQETIVIARGDANGQQQLCAYFV-----ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05958   363 PAVAECAVVGHPDESRGVVVKAFVVlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
PRK06178 PRK06178
acyl-CoA synthetase; Validated
4897-5385 8.93e-31

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 132.09  E-value: 8.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4897 AECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 4976
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4977 QFMLEDSAASVLLTQTHLQERAQQ-WGQT-------------------------LQAALCLDDEAA---YAEDASNVANV 5027
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAPVVEQvRAETslrhvivtsladvlpaeptlplpdsLRAPRLAAAGAIdllPALRACTAPVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5028 NEPHDL---AYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR-EYRLDQFPVRLLQLASF-----SFDVFVgdiarTLYNG 5098
Cdd:PRK06178  203 LPPPALdalAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAvAVVGGEDSVFLSFLPEFwiageNFGLLF-----PLFSG 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5099 GTMVICpkdDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVT-DYR---------V 5168
Cdd:PRK06178  278 ATLVLL---ARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSFVKKLNpDYRqrwraltgsV 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5169 LQErfgsqfriiNAYGVTEA-----------AIDSSLYDEPL-AKLPeagnVPigkaalNAKFYIVDAHLN-PVPVGVLG 5235
Cdd:PRK06178  355 LAE---------AAWGMTEThtcdtftagfqDDDFDLLSQPVfVGLP----VP------GTEFKICDFETGeLLPLGAEG 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5236 ELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAE 5315
Cdd:PRK06178  416 EIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 5316 GVREAVVVVREDA-KGQ-KVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVqLEQLPLTANGKIDRKAL 5385
Cdd:PRK06178  489 AVLGSAVVGRPDPdKGQvPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
3868-4337 1.08e-30

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 131.46  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVF-----EKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDR 3942
Cdd:cd05970    31 PDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3943 IRYMLEDSGAQALLT------QRHLRERVSFAGT---FVAVDDEQ-----AYHADGSNLEPVVGPNH---------LAYV 3999
Cdd:cd05970   111 IVYRIESADIKMIVAiaedniPEEIEKAAPECPSkpkLVWVGDPVpegwiDFRKLIKNASPDFERPTansypcgedILLV 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4000 IYTSGTTGKPKgvMVEHHGLCSL-KLMFANTLQ-MTEQDRVVQFASLSFDASCW-EIFKALFFGATLYIptsttiLDYPL 4076
Cdd:cd05970   191 YFSSGTTGMPK--MVEHDFTYPLgHIVTAKYWQnVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFV------YDYDK 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4077 FE-----SYMNENGITATILPPTYAAYLNPDRM-----PSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEA--SI 4142
Cdd:cd05970   263 FDpkallEKLSKYGVTTFCAPPTIYRFLIREDLsrydlSSLRYCTTAGEALNPEVFNTFKEKtgIKLMEGFGQTETtlTI 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4143 VTSIWDEAsdslgdrKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCIS-----GVGLARGYLNRPELTAEKFVDNpfe 4217
Cdd:cd05970   343 ATFPWMEP-------KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTAEVWHDG--- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4218 pgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELT 4297
Cdd:cd05970   413 ----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYE 488
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 4298 AAElraTMSQELPN--------YMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05970   489 PSE---ELKKELQDhvkkvtapYKYPRIVEFVDELPKTISGKIRRVEI 533
PRK09088 PRK09088
acyl-CoA synthetase; Validated
2354-2828 1.10e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 130.70  E-value: 1.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2354 QAERIPDHPAVV--FEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPE 2431
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2432 DRISYMLEDSSAQVLLAQRRLQervsfAGT--VVTVDDEQAYA-GDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHH 2508
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVA-----AGRtdVEDLAAFIASAdALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2509 GLCSLKQMFANTLQINAQDRVV----QFASLSFDAScweVFQTLFFGATlyiptketILDYQWFE-----RYMSDN--GI 2577
Cdd:PRK09088  159 NLQQTAHNFGVLGRVDAHSSFLcdapMFHIIGLITS---VRPVLAVGGS--------ILVSNGFEpkrtlGRLGDPalGI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2578 TTATLPPTYAVYLNpdHMPDF-----KRLIA---AGSASSLELLQQWKDK-VKYFNAYGPTEDSicTTIWTPSTEDI--S 2646
Cdd:PRK09088  228 THYFCVPQMAQAFR--AQPGFdaaalRHLTAlftGGAPHAAEDILGWLDDgIPMVDGFGMSEAG--TVFGMSVDCDVirA 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2647 QLKSVPIGGPIVNHRIyiVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVdnpfepGERMYRTGDLAKWLPDG 2726
Cdd:PRK09088  304 KAGAAGIPTPTVQTRV--VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGWFRTGDIARRDADG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2727 TIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDAS-GQKQLCAYFVADRTMT-VGELRGELSGELPGYM 2804
Cdd:PRK09088  376 FFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLAIVPADGAPLdLERIRSHLSTRLAKYK 455
                         490       500
                  ....*....|....*....|....
gi 386647928 2805 IPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK09088  456 VPKHLRLVDALPRTASGKLQKARL 479
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
4886-5385 1.16e-30

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 131.71  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4886 NEAFHALFEKQAECTPEAAAVVYEND------RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWK 4959
Cdd:PRK13295   23 DRTINDDLDACVASCPDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4960 AGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTH------------LQERAQQWGQTLQ---------AALCLDDEAAYA 5018
Cdd:PRK13295  103 IGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfdhaamarrLRPELPALRHVVVvggdgadsfEALLITPAWEQE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5019 EDASNV--ANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLL-----QLASFSFDVFVgdi 5091
Cdd:PRK13295  183 PDAPAIlaRLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMaspmaHQTGFMYGLMM--- 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5092 arTLYNGGTMVIcpkDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQE 5171
Cdd:PRK13295  260 --PVMLGATAVL---QDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARA 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5172 RFGSqfRIINAYGVTE-AAIDSSLYDEPLAKLPEAGNVPIGKAALNakfyIVDAHLNPVPVGVLGELCIGGIGVARGYLN 5250
Cdd:PRK13295  335 ALGA--KIVSAWGMTEnGAVTLTKLDDPDERASTTDGCPLPGVEVR----VVDADGAPLPAGQIGRLQVRGCSNFGGYLK 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5251 RPELTEekfvdspfVEGERLYRTGDLARWMPDGNVdfigRIDNQAK---IRG-YRIETGEIETQLLKAEGVREAVVVVRE 5326
Cdd:PRK13295  409 RPQLNG--------TDADGWFDTGDLARIDADGYI----RISGRSKdviIRGgENIPVVEIEALLYRHPAIAQVAIVAYP 476
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 5327 DAKGQKVLCAHFT--AESELKLSELRSSL-SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK13295  477 DERLGERACAFVVprPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
PRK07638 PRK07638
acyl-CoA synthetase; Validated
3867-4337 1.20e-30

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 130.67  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3867 NPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQlVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYM 3946
Cdd:PRK07638   14 QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3947 LEDSGAQALLTQRHLRERVSFAGTFVAVDDE-----QAYHADGSNLEPVvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCS 4021
Cdd:PRK07638   93 LAISNADMIVTERYKLNDLPDEEGRVIEIDEwkrmiEKYLPTYAPIENV--QNAPFYMGFTSGSTGKPKAFLRAQQSWLH 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4022 LKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDypLFESYMNENGITATILPPTYAAYLNP 4101
Cdd:PRK07638  171 SFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRKFIPNQ--VLDKLETENISVMYTVPTMLESLYKE 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4102 DRMPSLK-KLITGGSAASVEFVQQWKDKVLY---FNAYGPTEASIVTSIWDEASDslgdRKSVPIGRPLANHRIYVVDSh 4177
Cdd:PRK07638  249 NRVIENKmKIISSGAKWEAEAKEKIKNIFPYaklYEFYGASELSFVTALVDEESE----RRPNSVGRPFHNVQVRICNE- 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4178 nrmlpvgvAGELCISG-VGlaRGYLNRPELTAEKFVD--NPFEPGERMYRTGDLVRWL-PDGNLEYLGRIDHQVKIRGYR 4253
Cdd:PRK07638  324 --------AGEEVQKGeIG--TVYVKSPQFFMGYIIGgvLARELNADGWMTVRDVGYEdEEGFIYIVGREKNMILFGGIN 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4254 IELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYfVAQRElTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:PRK07638  394 IFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAI-IKGSA-TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIA 471

                  ....
gi 386647928 4334 RKAL 4337
Cdd:PRK07638  472 RMEA 475
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1288-1795 1.35e-30

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 131.40  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1288 PAAPDAPENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAV 1367
Cdd:PRK06164    1 TPHDAAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1368 WKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTH---------LQERAQQWGQTLQAVLCLDDEAAYAED-------- 1430
Cdd:PRK06164   81 ARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidfaaiLAAVPPDALPPLRAIAVVDDAADATPApapgarvq 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1431 ----------ASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQL---ASFSFDVF 1497
Cdd:PRK06164  161 lfalpdpappAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALpfcGVFGFSTL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1498 VGDIARtlynGGTMVICPKDDRIDPARLhywISEEKIT-IFESTPALIIPFmDYVAEHGlDMSSMELLITSSDSCSVTDY 1576
Cdd:PRK06164  241 LGALAG----GAPLVCEPVFDAARTARA---LRRHRVThTFGNDEMLRRIL-DTAGERA-DFPSARLFGFASFAPALGEL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1577 RVLQERFGsqFRIINAYGVTEAAIDSSLYD--EPLAKLPEAGNVPIGKAalnAKFYIVDAHLNPV-PVGVLGELCIGGIG 1653
Cdd:PRK06164  312 AALARARG--VPLTGLYGSSEVQALVALQPatDPVSVRIEGGGRPASPE---ARVRARDPQDGALlPDGESGEIEIRAPS 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1654 VARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIEtQLLKAEGVREAVVV 1733
Cdd:PRK06164  387 LMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE-HALEALPGVAAAQV 459
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1734 VREDAKGQKVLCAYFTAESELKLSE--LRSSLSQELPGYMIPSYFVQLEQLPLT--ANG-KIDRKAL 1795
Cdd:PRK06164  460 VGATRDGKTVPVAFVIPTDGASPDEagLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
4911-5385 1.36e-30

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 131.25  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4911 DRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDP----DYPSDRIQF------ML 4980
Cdd:cd05906    38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARLRKlrhiwqLL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSaasVLLT----QTHLQERAQQWGQTLQAALCLDDEAAYAEDAsnVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSL 5056
Cdd:cd05906   118 GSP---VVLTdaelVAEFAGLETLSGLPGIRVLSIEELLDTAADH--DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5057 VNTAAGYRREYRLDQFPVRLLQLAsfsFDvFVGDIA----RTLYNGGTMVICPKDDRI-DPARLHYWISEEKITIFEStP 5131
Cdd:cd05906   193 LARSAGKIQHNGLTPQDVFLNWVP---LD-HVGGLVelhlRAVYLGCQQVHVPTEEILaDPLRWLDLIDRYRVTITWA-P 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 ----ALIIPFMDYVAEHGLDMSSMVLLITSSDSCSV-TDYRVLQ--ERFGSQ-FRIINAYGVTE----AAIDSSLYDEPL 5199
Cdd:cd05906   268 nfafALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAkTIRRLLRllEPYGLPpDAIRPAFGMTEtcsgVIYSRSFPTYDH 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5200 AKLPEAgnVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLArW 5279
Cdd:cd05906   348 SQALEF--VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-F 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5280 MPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVreavvvvredAKGQKVLCAHFTAESELK-------------- 5345
Cdd:cd05906   419 LDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV----------EPSFTAAFAVRDPGAETEelaiffvpeydlqd 488
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 5346 -----LSELRSSLSQEL---PGYMIPsyfVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05906   489 alsetLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
2355-2774 1.47e-30

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 130.43  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVV--FEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPED 2432
Cdd:cd05904    15 ASAHPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2433 RISYMLEDSSAQVLLAQRRLQERV-SFAGTVVTVDDE----------QAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPK 2501
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTAELAEKLaSLALPVVLLDSAefdslsfsdlLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2502 GVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFdascWEVFQTLFF-------GATLYIPTK---ETILDYqwFERY 2571
Cdd:cd05904   175 GVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPM----FHIYGLSSFalgllrlGATVVVMPRfdlEELLAA--IERY 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2572 msdnGITTATLPPTYAVYLNPDHMP---DFKRL--IAAGSAS-SLELLQQWKDK---VKYFNAYGPTEDSICTTIwTPST 2642
Cdd:cd05904   249 ----KVTHLPVVPPIVLALVKSPIVdkyDLSSLrqIMSGAAPlGKELIEAFRAKfpnVDLGQGYGMTESTGVVAM-CFAP 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2643 EDiSQLKSVPIGGPIVNHRIYIVD-AHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfepgERMYRTGDLAK 2721
Cdd:cd05904   324 EK-DRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK------EGWLHTGDLCY 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2722 WLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVI-AHDDASGQ 2774
Cdd:cd05904   397 IDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIpYPDEEAGE 450
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
5930-6420 1.99e-30

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 130.91  E-value: 1.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5930 KYPSdktIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAG 6009
Cdd:PRK07059   21 QYPS---LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6010 GAYVPIDPDYPEDRIRYMLEDSGAKLLLV--------QgHLLDR--------ASFADKL------VNL------------ 6055
Cdd:PRK07059   98 YVVVNVNPLYTPRELEHQLKDSGAEAIVVlenfattvQ-QVLAKtavkhvvvASMGDLLgfkghiVNFvvrrvkkmvpaw 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6056 --------ND---DGAyhedGSNLEPVN-GPEHLTYVIYTSGTTGRPKGVMVEHRNVV-RLVKNTNYVE--LNEQTHILQ 6120
Cdd:PRK07059  177 slpghvrfNDalaEGA----RQTFKPVKlGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQMEAWLQpaFEKKPRPDQ 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6121 TGAV-------VFdASTFEIWGALLNGGRLYVVRNEtiLDAVSLKNAIQQYGINTMWLTAPLYNQL------SQQDsgmF 6187
Cdd:PRK07059  253 LNFVcalplyhIF-ALTVCGLLGMRTGGRNILIPNP--RDIPGFIKELKKYQVHIFPAVNTLYNALlnnpdfDKLD---F 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6188 AGLKTLIVGGDVLSVPHINRVLrEHAGLSIVNGYG-----------PTENTTFSTThtivgeqkeavpIGKPINNSTAYI 6256
Cdd:PRK07059  327 SKLIVANGGGMAVQRPVAERWL-EMTGCPITEGYGlsetspvatcnPVDATEFSGT------------IGLPLPSTEVSI 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6257 VDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGDLARWLPDGTLEYKGRIDEQVKIRGYR 6336
Cdd:PRK07059  394 RDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFN 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6337 IELGEIEEQLLKVASVKEATVI-VREDESGqkQLCAYFVAER--ELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNG 6413
Cdd:PRK07059  468 VYPNEIEEVVASHPGVLEVAAVgVPDEHSG--EAVKLFVVKKdpALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVG 545

                  ....*..
gi 386647928 6414 KIDRRAL 6420
Cdd:PRK07059  546 KILRREL 552
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
4896-5385 2.44e-30

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 130.64  E-value: 2.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4896 QAECTPEAAAVVYEND-RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSD 4974
Cdd:PRK06087   32 TARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4975 RIQFMLEDSAASVLLTQTHLQERA--------QQWGQTLQAALCLDDEA-AYAEDA-SNVANVNEP---------HDLAY 5035
Cdd:PRK06087  112 ELVWVLNKCQAKMFFAPTLFKQTRpvdlilplQNQLPQLQQIVGVDKLApATSSLSlSQIIADYEPlttaitthgDELAA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5036 VIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL---DQF--PVRLLQLASFsfdvFVGDIARTLYnGGTMVIcpkDDRI 5110
Cdd:PRK06087  192 VLFTSGTEGLPKGVMLTHNNILASERAYCARLNLtwqDVFmmPAPLGHATGF----LHGVTAPFLI-GARSVL---LDIF 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5111 DPARLHYWISEEKIT-IFESTPaLIIPFMDYVAEHGLDMSSMVLLITSSdscSVTDYRVLQERFGSQFRIINAYGVTEAA 5189
Cdd:PRK06087  264 TPDACLALLEQQRCTcMLGATP-FIYDLLNLLEKQPADLSALRFFLCGG---TTIPKKVARECQQRGIKLLSVYGSTESS 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5190 IDSSLydePLAK-LPEAGNVPiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegE 5268
Cdd:PRK06087  340 PHAVV---NLDDpLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------E 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5269 RLYRTGDLARWMPDGNVDFIGRiDNQAKIR-GYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFT---AESEL 5344
Cdd:PRK06087  410 GWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlkaPHHSL 488
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928 5345 KLSELRSSLS-QELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK06087  489 TLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK09088 PRK09088
acyl-CoA synthetase; Validated
5944-6420 3.02e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 129.54  E-value: 3.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5944 QAERIPDHLAVT--FEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPE 6021
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6022 DRIRYMLEDSGAKLLLVQGHL-------LDRASFADKLvnlndDGAyhedGSNLEPVNGPEHLTYVIYTSGTTGRPKGVM 6094
Cdd:PRK09088   84 SELDALLQDAEPRLLLGDDAVaagrtdvEDLAAFIASA-----DAL----EPADTPSIPPERVSLILFTSGTSGQPKGVM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6095 VEHRNVVRLVKNtnyveLNEQTHILQTGAVVFDASTFEIWG-------ALLNGGRLYVvrNETILDAVSLKN-AIQQYGI 6166
Cdd:PRK09088  155 LSERNLQQTAHN-----FGVLGRVDAHSSFLCDAPMFHIIGlitsvrpVLAVGGSILV--SNGFEPKRTLGRlGDPALGI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6167 nTMWLTAPlynQLSQQ-------DSGMFAGLKTLIVGGdvlsVPHINRVLRE--HAGLSIVNGYGPTEnttfstTHTIVG 6237
Cdd:PRK09088  228 -THYFCVP---QMAQAfraqpgfDAAALRHLTALFTGG----APHAAEDILGwlDDGIPMVDGFGMSE------AGTVFG 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6238 EQKEAVPI-------GKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGD 6310
Cdd:PRK09088  294 MSVDCDVIrakagaaGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGD 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6311 LARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQKQLCAYFVAER-ELTIGELRAAL 6388
Cdd:PRK09088  368 IARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVgMADAQWGEVGYLAIVPADGaPLDLERIRSHL 447
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 6389 SQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK09088  448 STRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
PRK07529 PRK07529
AMP-binding domain protein; Validated
5936-6462 3.10e-30

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 131.23  E-value: 3.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTF--------EDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILK 6007
Cdd:PRK07529   26 STYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6008 AGGAyVPIDPDYPEDRIRYMLEDSGAKLL---------------------------LVQGHLLDR----ASFADKLVNLN 6056
Cdd:PRK07529  106 AGIA-NPINPLLEPEQIAELLRAAGAKVLvtlgpfpgtdiwqkvaevlaalpelrtVVEVDLARYlpgpKRLAVPLIRRK 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6057 DDGAYH--------EDGSNLE--PVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVrlvknTNYVELNEQTHILQTGAVVF 6126
Cdd:PRK07529  185 AHARILdfdaelarQPGDRLFsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEV-----ANAWLGALLLGLGPGDTVFC 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6127 DASTFEIWGALLNG------GRLYVV------RNETILDavSLKNAIQQYGINTMWLTAPLYNQLSQQ--DSGMFAGLKT 6192
Cdd:PRK07529  260 GLPLFHVNALLVTGlaplarGAHVVLatpqgyRGPGVIA--NFWKIVERYRINFLSGVPTVYAALLQVpvDGHDISSLRY 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6193 LIVGGDVLSVPHINRvLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAvPIGKPI----------NNSTAYIVDSkls 6262
Cdd:PRK07529  338 ALCGAAPLPVEVFRR-FEAATGVRIVEGYGLTEATCVSSVNPPDGERRIG-SVGLRLpyqrvrvvilDDAGRYLRDC--- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6263 llPVGVWGELIVGGDGVARGYLNrpeltAEKfvESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVkIR-GYRIELGE 6341
Cdd:PRK07529  413 --AVDEVGVLCIAGPNVFSGYLE-----AAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAA 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVIVREDESGQKQLCAY--FVAERELTIGELRAALSQELPN-YMIPSHFVPLERMPLTPNGKIDRR 6418
Cdd:PRK07529  483 IEEALLRHPAVALAAAVGRPDAHAGELPVAYvqLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKP 562
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 386647928 6419 ALPApqgnapvgaeyVAPRTEQEKALAavwQAVLGAERVGVTDH 6462
Cdd:PRK07529  563 ALRR-----------DAIRRVLRAALR---DAGVEAEVVDVVED 592
PRK06164 PRK06164
acyl-CoA synthetase; Validated
3853-4337 4.19e-30

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 129.86  E-value: 4.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3853 EQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYI 3932
Cdd:PRK06164    9 ADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3933 PIDPEYPEDRIRYMLEDSGAQALLTQRHLReRVSFAGTFVAVDDE------QAYHADGSN-------------------- 3986
Cdd:PRK06164   89 AVNTRYRSHEVAHILGRGRARWLVVWPGFK-GIDFAAILAAVPPDalpplrAIAVVDDAAdatpapapgarvqlfalpdp 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3987 ------LEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVqfASLSFDAScweifkalfFG 4060
Cdd:PRK06164  168 appaaaGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLL--AALPFCGV---------FG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4061 -ATL--YIPTSTTILDYPLFES-----YMNENGITATI-----LPPTYAAYLNPDRMPSLKKL----ITGGSAASVEFVQ 4123
Cdd:PRK06164  237 fSTLlgALAGGAPLVCEPVFDAartarALRRHRVTHTFgndemLRRILDTAGERADFPSARLFgfasFAPALGELAALAR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4124 QwKDKVLYfNAYGPTEASIVTSIWDeASDSLGDRKsVPIGRPL-ANHRIYVVDSHN-RMLPVGVAGELCISGVGLARGYL 4201
Cdd:PRK06164  317 A-RGVPLT-GLYGSSEVQALVALQP-ATDPVSVRI-EGGGRPAsPEARVRARDPQDgALLPDGESGEIEIRAPSLMRGYL 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4202 NRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREdAN 4281
Cdd:PRK06164  393 DNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-RD 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 4282 GQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLT--PNG-KIDRKAL 4337
Cdd:PRK06164  466 GKTVPVAFVIPTdgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
6079-6418 4.72e-30

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 125.96  E-value: 4.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6079 YVIYTSGTTGRPKGVMVEH----------RNVVRLVKNTNYVEL-----NEQTHILQTGAVVFDASTFEIWGALLNGGRL 6143
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTPSEDAHkaaaaAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6144 YVVRNEtiLDAVSLKNAIQQYGINTMWLT-----APLYNQLSQQDSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIV 6218
Cdd:cd05924    87 VLPDDR--FDPEEVWRTIEKHKVTSMTIVgdamaRPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6219 NGYGPTEnTTFSTTHTIVGEQKEAVPIGKPinNSTAYIVDSKLSLLPVGVWGELIVGGDG-VARGYLNRPELTAEKFVEs 6297
Cdd:cd05924   165 DAFGSSE-TGFTGSGHSAGSGPETGPFTRA--NPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAETFPE- 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6298 sfLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDES-GQKqlCAYFVAE 6376
Cdd:cd05924   241 --VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERwGQE--VVAVVQL 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 6377 RE---LTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRR 6418
Cdd:cd05924   317 REgagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
PRK07470 PRK07470
acyl-CoA synthetase; Validated
269-747 4.88e-30

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 129.39  E-value: 4.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  269 QAERR-PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEE 347
Cdd:PRK07470   15 QAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  348 RIRYMLEDSGTQVLLSQG--------------HLQERVSFSGTWIRLDDEEAYHEDGSNLESVNGPEHLT--YVIYTSGT 411
Cdd:PRK07470   95 EVAYLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDDpcWFFFTSGT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  412 TGKPKGNLTTHRNIIRVVknTNYI-----DVTGQDKLLQLSSYSFDGSTFdifgALLN---GAKLVLVPKETvLDVAKLA 483
Cdd:PRK07470  175 TGRPKAAVLTHGQMAFVI--TNHLadlmpGTTEQDASLVVAPLSHGAGIH----QLCQvarGAATVLLPSER-FDPAEVW 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  484 GLIEKQQISVMFITTAFFNVLVDmNPDCLRH----ARAILFGGERVSVSHVRKALGHLGPgKIKHVYGPTESTVFATSYD 559
Cdd:PRK07470  248 ALVERHRVTNLFTVPTILKMLVE-HPAVDRYdhssLRYVIYAGAPMYRADQKRALAKLGK-VLVQYFGLGEVTGNITVLP 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  560 --VHEVEEG-AVSI-PIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRT 635
Cdd:PRK07470  326 paLHDAEDGpDARIgTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  636 GDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAI-EKATVVVRESANGEKQLcAYYVA--DRSLPANEVR 712
Cdd:PRK07470  399 GDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVsEVAVLGVPDPVWGEVGV-AVCVArdGAPVDEAELL 477
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 386647928  713 STLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK07470  478 AWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
2345-2828 5.84e-30

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 129.32  E-value: 5.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2345 KTIHQLFEEQAERIPD----HPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGG 2420
Cdd:cd05906    10 RTLLELLLRAAERGPTkgitYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2421 --AYVPIDPEYPEDR--------ISYMLEdsSAQVLLAQRRLQErvsFAG----------TVVTVDDEQAYAGDgSNLEs 2480
Cdd:cd05906    90 vpAPLTVPPTYDEPNarlrklrhIWQLLG--SPVVLTDAELVAE---FAGletlsglpgiRVLSIEELLDTAAD-HDLP- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2481 AVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSlkqMFANTLQIN-AQDRVVQFASLSFD--ASCWEV-FQTLFFGA-TLY 2555
Cdd:cd05906   163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILA---RSAGKIQHNgLTPQDVFLNWVPLDhvGGLVELhLRAVYLGCqQVH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2556 IPTKETI------LDyqWFERYMsdngiTTATLPPTYAVYLNPDHMPDF----------KRLIAAGSASS-------LEL 2612
Cdd:cd05906   240 VPTEEILadplrwLD--LIDRYR-----VTITWAPNFAFALLNDLLEEIedgtwdlsslRYLVNAGEAVVaktirrlLRL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2613 LQQWK---DKVKyfNAYGPTED-SICTTIWTPSTEDISQ-LKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGL 2687
Cdd:cd05906   313 LEPYGlppDAIR--PAFGMTETcSGVIYSRSFPTYDHSQaLEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVV 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2688 ARGYLNRPDLTAEKFVDNPFepgermYRTGDLAkWLPDGTIEYLGRIDHQVKIRGYRIELGEIE---EQLLKVASVQEAI 2764
Cdd:cd05906   391 TKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEaavEEVPGVEPSFTAA 463
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2765 VIAHDDASGQKQLCAYFV------ADRTMTVGELRGELSGEL---PGYMIPahfVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05906   464 FAVRDPGAETEELAIFFVpeydlqDALSETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK06164 PRK06164
acyl-CoA synthetase; Validated
257-740 6.35e-30

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 129.09  E-value: 6.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  257 PRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGA 336
Cdd:PRK06164    7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  337 YVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQeRVSFSGTWIRLDDEE-------------------------------A 385
Cdd:PRK06164   87 VIAVNTRYRSHEVAHILGRGRARWLVVWPGFK-GIDFAAILAAVPPDAlpplraiavvddaadatpapapgarvqlfalP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  386 YHEDGSNLESVNGPEHLTYVIYT-SGTTGKPKgnLTTHRNIIRVVKNTNYIDVTGQD---KLLQLSSYS--FDGSTfdIF 459
Cdd:PRK06164  166 DPAPPAAAGERAADPDAGALLFTtSGTTSGPK--LVLHRQATLLRHARAIARAYGYDpgaVLLAALPFCgvFGFST--LL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  460 GALLNGAKLVLVPketVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRHARAILFG--------GERVSVSHVR 531
Cdd:PRK06164  242 GALAGGAPLVCEP---VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGfasfapalGELAALARAR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  532 KAlghlgpgKIKHVYGPTEstVFA------TSYDVHEVEEGAvsipiGGPISNTA-IYIVNAQN-KLQPIGVAGELCVAG 603
Cdd:PRK06164  319 GV-------PLTGLYGSSE--VQAlvalqpATDPVSVRIEGG-----GRPASPEArVRARDPQDgALLPDGESGEIEIRA 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  604 DGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKAT 683
Cdd:PRK06164  385 PSLMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928  684 VVVRESaNGEKQLCAYYVADRSLPANE--VRSTLSQELPAYMLPSYFVQLEQMPLTTNG 740
Cdd:PRK06164  459 VVGATR-DGKTVPVAFVIPTDGASPDEagLMAACREALAGFKVPARVQVVEAFPVTESA 516
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
261-742 6.52e-30

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 130.00  E-value: 6.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFED------RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAG 334
Cdd:cd17634    54 LAANALDRHLRENGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  335 GAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQER-------------VSFSGTWIR-----------LDDEEAYHEDG 390
Cdd:cd17634   134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAgrsvplkknvddaLNPNVTSVEhvivlkrtgsdIDWQEGRDLWW 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  391 SNLESVNGPEHLT---------YVIYTSGTTGKPKGNLTTHRN-IIRVVKNTNYI-DVTGQDKLLQLSSYSF-DGSTFDI 458
Cdd:cd17634   214 RDLIAKASPEHQPeamnaedplFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVfDYGPGDIYWCTADVGWvTGHSYLL 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  459 FGALLNGAKLVL---VPKETvlDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCL-RHARA---ILFG-GERVSVSHV 530
Cdd:cd17634   294 YGPLACGATTLLyegVPNWP--TPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIeGTDRSslrILGSvGEPINPEAY 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  531 RKALGHLGPGKIKHV--YGPTESTVFATSY--DVHEVEEGAVSIPIGGpisnTAIYIVNAQNKLQPIGVAGELcVAGD-- 604
Cdd:cd17634   372 EWYWKKIGKEKCPVVdtWWQTETGGFMITPlpGAIELKAGSATRPVFG----VQPAVVDNEGHPQPGGTEGNL-VITDpw 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  605 -GLARGYLNRPDltaeKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAI-EKA 682
Cdd:cd17634   447 pGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVaEAA 522
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  683 TVVVRESANGEKQLCayYVADRS--LP----ANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKV 742
Cdd:cd17634   523 VVGIPHAIKGQAPYA--YVVLNHgvEPspelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
286-749 6.70e-30

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 130.92  E-value: 6.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQG 365
Cdd:PRK06060   31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  366 HLQERVSfSGTWIRLDD--EEAYHEDGSNLESVNGpEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNT--NYIDVTGQD 441
Cdd:PRK06060  111 ALRDRFQ-PSRVAEAAElmSEAARVAPGGYEPMGG-DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrKALRLTPED 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  442 klLQLSS---YSFDGSTFDIFGALLNGAKLVLVPKETVLDVAklAGLIEKQQISVMFITTAFFNVLVDM-NPDCLRHARA 517
Cdd:PRK06060  189 --TGLCSarmYFAYGLGNSVWFPLATGGSAVINSAPVTPEAA--AILSARFGPSVLYGVPNFFARVIDScSPDSFRSLRC 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  518 ILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAvsipIGGPISNTAIYIVNAQNKLQPIGVAG 597
Cdd:PRK06060  265 VVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGT----LGRVLPPYEIRVVAPDGTTAGPGVEG 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  598 ELCVAGDGLARGYLNRPDltaekfadnPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLE 677
Cdd:PRK06060  341 DLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDE 411
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  678 AIEKATVVVRESANGEKQLCAYYVA------DRSLPANEVRSTLSQeLPAYMLPSYFVQLEQMPLTTNGKVDRRALPA 749
Cdd:PRK06060  412 AVAEAAVVAVRESTGASTLQAFLVAtsgatiDGSVMRDLHRGLLNR-LSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
3854-4341 7.86e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 129.38  E-value: 7.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3854 QTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIP 3933
Cdd:PRK06710   24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3934 IDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGT----------------------------------FVAVDDEQA 3979
Cdd:PRK06710  104 TNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSatkiehvivtriadflpfpknllypfvqkkqsnlVVKVSESET 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3980 YHADGS-------NLEPVVGP-NHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFdascw 4051
Cdd:PRK06710  184 IHLWNSvekevntGVEVPCDPeNDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPF----- 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4052 eiFKAlfFGAT----LYIPTSTTILDYPLFESYMNENGI---TATILP--PT-YAAYLNPDRM-----PSLKKLITGGSA 4116
Cdd:PRK06710  259 --FHV--YGMTavmnLSIMQGYKMVLIPKFDMKMVFEAIkkhKVTLFPgaPTiYIALLNSPLLkeydiSSIRACISGSAP 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4117 ASVEfVQQWKDKVL---YFNAYGPTEASIVTS---IWDeasdslgdrKSVP--IGRPLANHRIYVVD-SHNRMLPVGVAG 4187
Cdd:PRK06710  335 LPVE-VQEKFETVTggkLVEGYGLTESSPVTHsnfLWE---------KRVPgsIGVPWPDTEAMIMSlETGEALPPGEIG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4188 ELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDgnleylgRIDHQVKIRGYRIELGEVETQLAKID 4267
Cdd:PRK06710  405 EIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKD-------RKKDMIVASGFNVYPREVEEVLYEHE 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 4268 AVQEAIVLAREDANGQQQLVAYFVAQR--ELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPE 4341
Cdd:PRK06710  478 KVQEVVTIGVPDPYRGETVKAFVVLKEgtECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
5942-6415 8.63e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 128.74  E-value: 8.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5942 EEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQ-PDQMVGLMVERSlEMVVGMIAILKAGGAYVPIDPDYP 6020
Cdd:PRK07786   24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGfGDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFRLT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6021 EDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVN----------------LNDDGAYHEDGSNLEPVNGPEHLTYVI-YT 6083
Cdd:PRK07786  103 PPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPllstvvvaggssddsvLGYEDLLAEAGPAHAPVDIPNDSPALImYT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6084 SGTTGRPKGVMVEHRNVVRLVKN---TNYVELNEQT--------HILQTGAVVFdastfeiwGALLngGRLYVVRNETIL 6152
Cdd:PRK07786  183 SGTTGRPKGAVLTHANLTGQAMTclrTNGADINSDVgfvgvplfHIAGIGSMLP--------GLLL--GAPTVIYPLGAF 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6153 DAVSLKNAIQQYGINTMWLTAPLYNQL--SQQDSGMFAGLKTLIVGgdvlSVPHINRVLREHA----GLSIVNGYGPTEN 6226
Cdd:PRK07786  253 DPGQLLDVLEAEKVTGIFLVPAQWQAVcaEQQARPRDLALRVLSWG----AAPASDTLLRQMAatfpEAQILAAFGQTEM 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6227 TTFstthTIVGEQKEAV----PIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpg 6302
Cdd:PRK07786  329 SPV----TCMLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF--- 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6303 ercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFV---AEREL 6379
Cdd:PRK07786  402 ----HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnDDAAL 477
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 6380 TIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:PRK07786  478 TLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
PRK07638 PRK07638
acyl-CoA synthetase; Validated
7456-7928 9.54e-30

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 127.97  E-value: 9.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAegvQADQP--VGLMIERSLEMI-VGAFAIMkAGGAYVPIDPEYPE 7532
Cdd:PRK07638   11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNE---KESKNktIAILLENRIEFLqLFAGAAM-AGWTCVPLDIKWKQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7533 DRIRYMLEDSGAQVLLTQRH-LQECVSFDGKVIAAD----DEQAYGEDGSNLEPVvgPNHLAYVIYTSGTTGKPKGVMVE 7607
Cdd:PRK07638   87 DELKERLAISNADMIVTERYkLNDLPDEEGRVIEIDewkrMIEKYLPTYAPIENV--QNAPFYMGFTSGSTGKPKAFLRA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7608 HHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDypLFESYMNENGITAAILPPTY 7687
Cdd:PRK07638  165 QQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRKFIPNQ--VLDKLETENISVMYTVPTML 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7688 AIYLSPDRLPSLK-KLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTSVwaaSPDGLDLRSVPIGRPIANHQIF 7763
Cdd:PRK07638  243 ESLYKENRVIENKmKIISSGAKWEAEAKEKIKNIfpyAKLYEFYGASELSFVTAL---VDEESERRPNSVGRPFHNVQVR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7764 IVDSqnhmlpvgvAGELCISGAgLARGYLNRPELTAEkfvdnpFLAGERMYRTGDLARWLPDGNIEYL---------GRI 7834
Cdd:PRK07638  320 ICNE---------AGEEVQKGE-IGTVYVKSPQFFMG------YIIGGVLARELNADGWMTVRDVGYEdeegfiyivGRE 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7835 DHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFvaDRELTVSELRGTLSQELPGYMIPSYFVQLEQ 7914
Cdd:PRK07638  384 KNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLKSFCLQRLSSFKIPKEWHFVDE 461
                         490
                  ....*....|....
gi 386647928 7915 MPLTPNGKIDRNAL 7928
Cdd:PRK07638  462 IPYTNSGKIARMEA 475
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
3864-4337 9.94e-30

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 126.82  E-value: 9.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDavavvfekSQLTYGELNERANRLARTLRDAGV-RPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPeypedr 3942
Cdd:cd05958     3 CLRSPE--------REWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3943 irymledsgaqaLLTQRHLRERVSFAGTFVAVDDEQAYHADgsnlepvvgpnHLAYVIYTSGTTGKPKGVMvehHGLCSL 4022
Cdd:cd05958    69 ------------LLRPKELAYILDKARITVALCAHALTASD-----------DICILAFTSGTTGAPKATM---HFHRDP 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4023 KLMF----ANTLQMTEQDRVVQFASLSFD-ASCWEIFKALFFGA-TLYIPTSTTildyPLFESYMNENGITATILPPT-Y 4095
Cdd:cd05958   123 LASAdryaVNVLRLREDDRFVGSPPLAFTfGLGGVLLFPFGVGAsGVLLEEATP----DLLLSAIARYKPTVLFTAPTaY 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4096 AAYL------NPDrMPSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTsiwdeASDSLGDRKSVPIGRPLA 4167
Cdd:cd05958   199 RAMLahpdaaGPD-LSSLRKCVSAGEALPAALHRAWKEAtgIPIIDGIGSTEMFHIF-----ISARPGDARPGATGKPVP 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4168 NHRIYVVDSHNRMLPVGVAGELCISGvglARGYLNRPELTAEKFVDnpfepGERMYrTGDLVRWLPDGNLEYLGRIDHQV 4247
Cdd:cd05958   273 GYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQ-----GGWNI-TGDTYSRDPDGYFRHQGRSDDMI 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4248 KIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ-----RELTAAELRATMSQELPNYMIPSYFVQLA 4322
Cdd:cd05958   344 VSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipGPVLARELQDHAKAHIAPYKYPRAIEFVT 423
                         490
                  ....*....|....*
gi 386647928 4323 QMPLTPNGKIDRKAL 4337
Cdd:cd05958   424 ELPRTATGKLQRFAL 438
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
5953-6420 1.32e-29

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 128.03  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5953 AVTFEDkqLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSG 6032
Cdd:cd17642    39 AHTGVN--YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6033 AKLLLVQGHLLDRA-------SFADKLVNLN---DDGAYHED----GSNLEP-----------VNGPEHLTYVIYTSGTT 6087
Cdd:cd17642   117 PTIVFCSKKGLQKVlnvqkklKIIKTIIILDskeDYKGYQCLytfiTQNLPPgfneydfkppsFDRDEQVALIMNSSGST 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6088 GRPKGVMVEHRN-VVRLVKNTNYV---ELNEQTHILQTGAVVFDASTFEIWGALLNGGR---LYVVRNETILdavslkNA 6160
Cdd:cd17642   197 GLPKGVQLTHKNiVARFSHARDPIfgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRvvlMYKFEEELFL------RS 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6161 IQQYGINTMWLTAPLYNQLSQQ---DSGMFAGLKTLIVGGDVLSvPHINRVLREHAGLSIV-NGYGPTEnttfSTTHTIV 6236
Cdd:cd17642   271 LQDYKVQSALLVPTLFAFFAKStlvDKYDLSNLHEIASGGAPLS-KEVGEAVAKRFKLPGIrQGYGLTE----TTSAILI 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6237 GEQKEAVP--IGKPINNSTAYIVDSKL-SLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLAR 6313
Cdd:cd17642   346 TPEGDDKPgaVGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWL------HSGDIAY 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6314 WLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGElraalsQELP 6393
Cdd:cd17642   420 YDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTE------KEVM 493
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 6394 NYmIPSHFVPLERM----------PLTPNGKIDRRAL 6420
Cdd:cd17642   494 DY-VASQVSTAKRLrggvkfvdevPKGLTGKIDRRKI 529
PRK06145 PRK06145
acyl-CoA synthetase; Validated
4888-5385 1.37e-29

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 127.69  E-value: 1.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4888 AFHAlfekqaECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPL 4967
Cdd:PRK06145    9 AFHA------RRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4968 DPDYPSDRIQFMLEDSAASVLLTQTHLQERAqqwgqTLQAALCLDDEAAYAE--------DASNVANVNEPHDLAYVIYT 5039
Cdd:PRK06145   83 NYRLAADEVAYILGDAGAKLLLVDEEFDAIV-----ALETPKIVIDAAAQADsrrlaqggLEIPPQAAVAPTDLVRLMYT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5040 SGTTGRPKGVMIEH-----RSLVNTAA-GYRREYRL----DQFPVRLLQLASFSfdvfvgdiarTLYNGGTMVIcpkDDR 5109
Cdd:PRK06145  158 SGTTDRPKGVMHSYgnlhwKSIDHVIAlGLTASERLlvvgPLYHVGAFDLPGIA----------VLWVGGTLRI---HRE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5110 IDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTEAA 5189
Cdd:PRK06145  225 FDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVF-TRARYIDAYGLTETC 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5190 IDSSLYdEPLAKLPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFveger 5269
Cdd:PRK06145  304 SGDTLM-EAGREIEKIGST--GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF----- 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5270 lyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAHFTAE-SELKLS 5347
Cdd:PRK06145  376 --RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPgATLTLE 453
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 386647928 5348 ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK06145  454 ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2639-2921 1.42e-29

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 122.94  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2639 TPSTEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGElcIAGVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGD 2718
Cdd:COG3433     6 PPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGE--GGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQAD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2719 LAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAH----DDASGQKQLCAYFVADRTMTVGELRG 2794
Cdd:COG3433    84 DLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaalrGAGVGLLLIVGAVAALDGLAAAAALA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2795 ELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALPAPQGNASAGADYVAPRSEE---EKVLADVWQAVLG--AERVGATD 2869
Cdd:COG3433   164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETaltEEELRADVAELLGvdPEEIDPDD 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 2870 HFFELGGDSIKSIQVSSRLHQAGYKLEIRDLFKYPTVAQLSKHIRPVARMAD 2921
Cdd:COG3433   244 NLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK08315 PRK08315
AMP-binding domain protein; Validated
3853-4332 1.60e-29

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 128.39  E-value: 1.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3853 EQTIHGLFEEQALRNPDAVAVVFEKSQL--TYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGA 3930
Cdd:PRK08315   15 EQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3931 YIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRErVSFAGTFVAVDDEQAYHADGsNLEPVVGPnHLAYVI---------- 4000
Cdd:PRK08315   95 LVTINPAYRLSELEYALNQSGCKALIAADGFKD-SDYVAMLYELAPELATCEPG-QLQSARLP-ELRRVIflgdekhpgm 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4001 ----------------------------------YTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRV---VQF-- 4041
Cdd:PRK08315  172 lnfdellalgravddaelaarqatldpddpiniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLcipVPLyh 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4042 ---------ASLS-----------FDA----------SCweifKALFFGATLYIptstTILDYPLFESYmnengitatil 4091
Cdd:PRK08315  252 cfgmvlgnlACVThgatmvypgegFDPlatlaaveeeRC----TALYGVPTMFI----AELDHPDFARF----------- 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4092 pptyaaylnpDrMPSLKKLITGGSAASVEFVQQWKDKvLYFN----AYGPTEASIVtSIWDEASDSLgDRKSVPIGRPLA 4167
Cdd:PRK08315  313 ----------D-LSSLRTGIMAGSPCPIEVMKRVIDK-MHMSevtiAYGMTETSPV-STQTRTDDPL-EKRVTTVGRALP 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4168 NHRIYVVD-SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKfVDnpfepGERMYRTGDLVRWLPDGNLEYLGRIDHQ 4246
Cdd:PRK08315  379 HLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-ID-----ADGWMHTGDLAVMDEEGYVNIVGRIKDM 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4247 VkIRG----Y-RielgEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAELRATMSQELPNYMIPSYFV 4319
Cdd:PRK08315  453 I-IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRpgATLTEEDVRDFCRGKIAHYKIPRYIR 527
                         570
                  ....*....|...
gi 386647928 4320 QLAQMPLTPNGKI 4332
Cdd:PRK08315  528 FVDEFPMTVTGKI 540
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
8034-8446 1.67e-29

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 125.10  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8034 YPVSSAQKRLFIL--HQlEGA---QQSYnipgfaTIEGPLDRDRFEAVFRQLIERHETLRTGF-EMANGEPVQRVYSDVE 8107
Cdd:cd19545     2 YPCTPLQEGLMALtaRQ-PGAyvgQRVF------ELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8108 FAVEYSkADREEAVEIAQRfvRPFDLrKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAGEELPPlR 8187
Cdd:cd19545    75 ISWTES-TSLDEYLEEDRA--APMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-P 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8188 IQYKDYAAWQRseayAKRVKQQEGYWLQTLAGELPVI--ELP-TDYERTSTRSFEgaelefeadealTQRLNELAARHES 8264
Cdd:cd19545   150 PPFSRFVKYLR----QLDDEAAAEFWRSYLAGLDPAVfpPLPsSRYQPRPDATLE------------HSISLPSSASSGV 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8265 TLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTH--ADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTlgafeHQ 8342
Cdd:cd19545   214 TLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDL-----LD 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8343 DYPFEEL----VERLNvkRDASRNPVFDTMFVLQ-NTEDRGIEADAFSLTPFVFDQTVAAQFDLTLSVAEDDGAIRGSFQ 8417
Cdd:cd19545   289 MIPFEHTglqnIRRLG--PDARAACNFQTLLVVQpALPSSTSESLELGIEEESEDLEDFSSYGLTLECQLSGSGLRVRAR 366
                         410       420
                  ....*....|....*....|....*....
gi 386647928 8418 YAAKLFKATMIRKMSKDLLAVLEQICGNP 8446
Cdd:cd19545   367 YDSSVISEEQVERLLDQFEHVLQQLASAP 395
PRK06164 PRK06164
acyl-CoA synthetase; Validated
4878-5385 1.86e-29

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 127.94  E-value: 1.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4878 PAAPDAPENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAV 4957
Cdd:PRK06164    1 TPHDAAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4958 WKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTH---------LQERAQQWGQTLQAALCLDDEAAYAED-------- 5020
Cdd:PRK06164   81 ARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidfaaiLAAVPPDALPPLRAIAVVDDAADATPApapgarvq 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5021 ----------ASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQL---ASFSFDVF 5087
Cdd:PRK06164  161 lfalpdpappAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALpfcGVFGFSTL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5088 VGDIARtlynGGTMVICPKDDRIDPARLhywISEEKIT-IFESTPALIIPFmDYVAEHGlDMSSMVLLITSSDSCSVTDY 5166
Cdd:PRK06164  241 LGALAG----GAPLVCEPVFDAARTARA---LRRHRVThTFGNDEMLRRIL-DTAGERA-DFPSARLFGFASFAPALGEL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5167 RVLQERFGsqFRIINAYGVTEAAIDSSLYD--EPLAKLPEAGNVPIGKAalnAKFYIVDAHLNPV-PVGVLGELCIGGIG 5243
Cdd:PRK06164  312 AALARARG--VPLTGLYGSSEVQALVALQPatDPVSVRIEGGGRPASPE---ARVRARDPQDGALlPDGESGEIEIRAPS 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5244 VARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIEtQLLKAEGVREAVVV 5323
Cdd:PRK06164  387 LMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE-HALEALPGVAAAQV 459
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 5324 VREDAKGQKVLCAHFTAESELKLSE--LRSSLSQELPGYMIPSYFVQLEQLPLT--ANG-KIDRKAL 5385
Cdd:PRK06164  460 VGATRDGKTVPVAFVIPTDGASPDEagLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
5958-6420 2.12e-29

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 125.67  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5958 DKQLTYGELNERANRLARTLRNAGV-QPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLL 6036
Cdd:cd05958     8 EREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6037 LvqghLLDRASFADKLVNLNddgayhedgsnlepvngpehltyviYTSGTTGRPKGVMVEHRNVVRLVK--NTNYVELNE 6114
Cdd:cd05958    88 L----CAHALTASDDICILA-------------------------FTSGTTGAPKATMHFHRDPLASADryAVNVLRLRE 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6115 QTHILQTGAVVFdasTFEIWGALL---NGGRLYVVRNETILDavSLKNAIQQYGInTMWLTAP-LYNQL------SQQDS 6184
Cdd:cd05958   139 DDRFVGSPPLAF---TFGLGGVLLfpfGVGASGVLLEEATPD--LLLSAIARYKP-TVLFTAPtAYRAMlahpdaAGPDL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6185 GmfaGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTENTtfsttHT-IVGEQKEAVP--IGKPINNSTAYIVDSKL 6261
Cdd:cd05958   213 S---SLRKCVSAGEALP-AALHRAWKEATGIPIIDGIGSTEMF-----HIfISARPGDARPgaTGKPVPGYEAKVVDDEG 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6262 SLLPVGVWGELIVGGDgvaRGYLNRPELTAEKFVESSFLPgercyrTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGE 6341
Cdd:cd05958   284 NPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNI------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQE-----LPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:cd05958   355 VEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDhakahIAPYKYPRAIEFVTELPRTATGKLQ 434

                  ....
gi 386647928 6417 RRAL 6420
Cdd:cd05958   435 RFAL 438
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
2355-2828 2.23e-29

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 127.61  E-value: 2.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVF-----EGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEY 2429
Cdd:cd05970    27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2430 PEDRISYMLE--DSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYAGDG------------SNL---------ESAVGPND 2486
Cdd:cd05970   107 TAKDIVYRIEsaDIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPvpegwidfrkliKNAspdferptaNSYPCGED 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2487 LAYIIYTSGTTGKPKgvMVEHHGLCSLKQMFANTLQINAQD--RVVQFASLSFDASCW-EVFQTLFFGATLYIptketiL 2563
Cdd:cd05970   187 ILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQNVREggLHLTVADTGWGKAVWgKIYGQWIAGAAVFV------Y 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2564 DYQWFE-----RYMSDNGITTATLPPTYAVYLNPDHMPDF-----KRLIAAGSASSLELLQQWKDK--VKYFNAYGPTED 2631
Cdd:cd05970   259 DYDKFDpkallEKLSKYGVTTFCAPPTIYRFLIREDLSRYdlsslRYCTTAGEALNPEVFNTFKEKtgIKLMEGFGQTET 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2632 SICTtiwtpSTEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCI-----AGVGLARGYLNRPDLTAEKFVDNp 2706
Cdd:cd05970   339 TLTI-----ATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgKPVGLFGGYYKDAEKTAEVWHDG- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2707 fepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRT 2786
Cdd:cd05970   413 ------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKG 486
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 2787 MTVGElrgELSGELPG--------YMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05970   487 YEPSE---ELKKELQDhvkkvtapYKYPRIVEFVDELPKTISGKIRRVEI 533
PRK07529 PRK07529
AMP-binding domain protein; Validated
2314-2828 2.26e-29

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 128.53  E-value: 2.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2314 APIAGLEMLTAAEQTQLHHVFNATaadyeadkTIHQLFEEQAERIPDHPAVVF--------EGQQLTYRELNERANRLAR 2385
Cdd:PRK07529    2 PAFATLADIEAIEAVPLAARDLPA--------STYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTAN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2386 TLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAyVPIDPEYPEDRISYMLEDSSAQVLLAQR---------RLQERV 2456
Cdd:PRK07529   74 LLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVTLGpfpgtdiwqKVAEVL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2457 SFAG---TVVTVD---------------------------DEQAYAGDGSNLESA--VGPNDLAYIIYTSGTTGKPKGVM 2504
Cdd:PRK07529  153 AALPelrTVVEVDlarylpgpkrlavplirrkaharildfDAELARQPGDRLFSGrpIGPDDVAAYFHTGGTTGMPKLAQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2505 VEHHGlcslkqMFANTLQINAQDRVVQFASLSFDASCWEVF-------QTLFFGATLYIPT-----KETILDYQW--FER 2570
Cdd:PRK07529  233 HTHGN------EVANAWLGALLLGLGPGDTVFCGLPLFHVNallvtglAPLARGAHVVLATpqgyrGPGVIANFWkiVER 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2571 YmsdnGITT-ATLPPTYAVYLN-PDHMPDFKRL-IAAGSASSL--ELLQQWKDK--VKYFNAYGPTEDSICTTIWTPSTE 2643
Cdd:PRK07529  307 Y----RINFlSGVPTVYAALLQvPVDGHDISSLrYALCGAAPLpvEVFRRFEAAtgVRIVEGYGLTEATCVSSVNPPDGE 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2644 diSQLKSVPIGGPIVNHRIYIVDA--HY-QPVPVGVAGELCIAGVGLARGYLNrpdltAEKfvDNPFEPGERMYRTGDLA 2720
Cdd:PRK07529  383 --RRIGSVGLRLPYQRVRVVILDDagRYlRDCAVDEVGVLCIAGPNVFSGYLE-----AAH--NKGLWLEDGWLNTGDLG 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2721 KWLPDGTIEYLGRidhqVK---IR-GYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAY--FVADRTMTVGELRG 2794
Cdd:PRK07529  454 RIDADGYFWLTGR----AKdliIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYvqLKPGASATEAELLA 529
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 386647928 2795 ELSGELPG-YMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK07529  530 FARDHIAErAAVPKHVRILDALPKTAVGKIFKPAL 564
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
2486-2828 2.31e-29

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 122.82  E-value: 2.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2486 DLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDR------VVQFASLSFdascweVFQTLFFGATLYIPTK 2559
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSwllslpLYHVGGLAI------LVRSLLAGAELVLLER 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2560 EtildyQWFERYMSDNGITTATLPPTYAVYL-----NPDHMPDFKRLIAAGSASSLELLQQWKDK-VKYFNAYGPTEDSI 2633
Cdd:cd17630    75 N-----QALAEDLAPPGVTHVSLVPTQLQRLldsgqGPAALKSLRAVLLGGAPIPPELLERAADRgIPLYTTYGMTETAS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2634 CTTIWTPSTEDISQLksvpigGPIVNHR-IYIVDAhyqpvpvgvaGELCIAGVGLARGYLNRPdltaekFVDNPFEPGer 2712
Cdd:cd17630   150 QVATKRPDGFGRGGV------GVLLPGReLRIVED----------GEIWVGGASLAMGYLRGQ------LVPEFNEDG-- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2713 MYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDAS-GQKqLCAYFVADRTMTVGE 2791
Cdd:cd17630   206 WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElGQR-PVAVIVGRGPADPAE 284
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 386647928 2792 LRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd17630   285 LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
3868-4332 2.35e-29

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 126.64  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQRhlrervSFAG-TFVAVDDeqayhaDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG--LCSLkl 4024
Cdd:cd12118    98 RHSEAKVLFVDR------EFEYeDLLAEGD------PDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGayLNAL-- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4025 mfANTLQMTEQDRVVQFASLS-FDASCWEIFKALF-FGATLYIPTSttiLDYPLFESYMNENGIT----AtilPPTYAAY 4098
Cdd:cd12118   164 --ANILEWEMKQHPVYLWTLPmFHCNGWCFPWTVAaVGGTNVCLRK---VDAKAIYDLIEKHKVThfcgA---PTVLNML 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4099 LNPdrMPSLKK-------LITGGS---AASVEFVQQWKDKVLYfnAYGPTEAS--IVTSIWDEASDSLGD--------RK 4158
Cdd:cd12118   236 ANA--PPSDARplphrvhVMTAGApppAAVLAKMEELGFDVTH--VYGLTETYgpATVCAWKPEWDELPTeerarlkaRQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4159 SVPIgrpLANHRIYVVDSHNrMLPV---GV-AGELCISGVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPD 4234
Cdd:cd12118   312 GVRY---VGLEEVDVLDPET-MKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGG-------WFHSGDLAVIHPD 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4235 GNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAyFVAQRE---LTAAELRATMSQELPN 4311
Cdd:cd12118   381 GYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA-FVELKEgakVTEEEIIAFCREHLAG 459
                         490       500
                  ....*....|....*....|.
gi 386647928 4312 YMIPSYFVqLAQMPLTPNGKI 4332
Cdd:cd12118   460 FMVPKTVV-FGELPKTSTGKI 479
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
8066-8446 2.57e-29

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 125.12  E-value: 2.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8066 GPLDRDRFEAVFRQLIERHETLRTGFEMAN-GEPVQRVYSDVE---FAVEYSKADREEAVEIAQRFVRP-----FDLRKP 8136
Cdd:cd19547    34 GGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAppwALLDWSGEDPDRRAELLERLLADdraagLSLADC 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8137 PLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYA----GEE--LPPLRiQYKDYAAWQRseAYAKRVKQQE 8210
Cdd:cd19547   114 PLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEelahGREpqLSPCR-PYRDYVRWIR--ARTAQSEESE 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8211 GYWLQTLAgEL---PVIELPTDYERTstrsFEGAELEFEadEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDI 8287
Cdd:cd19547   191 RFWREYLR-DLtpsPFSTAPADREGE----FDTVVHEFP--EQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDV 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8288 IVGTPVAGRTH--ADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELV-----ERLNVKRdas 8360
Cdd:cd19547   264 VHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLAQIKswasgERLSGGR--- 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8361 rnpVFDTMFVLQNTEDRGIEADAFSLTPFVFDQTVAAQFDLTLSVAEDDgAIRGSFQYAAKLFKATMIRKMSKDLLAVLE 8440
Cdd:cd19547   341 ---VFDNLVAFENYPEDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQ-KLAFHFNYDTTHFTRAQVDRFIEVFRLLTE 416

                  ....*.
gi 386647928 8441 QICGNP 8446
Cdd:cd19547   417 QLCRRP 422
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
5921-6420 3.11e-29

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 130.43  E-value: 3.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5921 QRVFN----ATEAKYPSDKTIHQLFEEQAERIPDHLAVTfeD---KQLTYGELNERANRLARTLRNaGVQPDQMVGLMVE 5993
Cdd:PRK08633  597 QAVFElsfdSWKSRKEALPPLAEAWIDTAKRNWSRLAVA--DstgGELSYGKALTGALALARLLKR-ELKDEENVGILLP 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5994 RSlemVVGMI---AILKAGgaYVPIDPDYP--EDRIRYMLEDSGAKlllvqgHLLDRASFADKLVNLNDDGA-------- 6060
Cdd:PRK08633  674 PS---VAGALanlALLLAG--KVPVNLNYTasEAALKSAIEQAQIK------TVITSRKFLEKLKNKGFDLElpenvkvi 742
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6061 YHED--------------------------GSNLEPVNgPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYV-ELN 6113
Cdd:PRK08633  743 YLEDlkakiskvdkltallaarllparllkRLYGPTFK-PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVfNLR 821
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6114 EQTHILqtGAVVFDAS---TFEIWGALLNGgrLYVVRNETILDAVSLKNAIQQYGInTMWLTAP----LYNQLSQQDSGM 6186
Cdd:PRK08633  822 NDDVIL--SSLPFFHSfglTVTLWLPLLEG--IKVVYHPDPTDALGIAKLVAKHRA-TILLGTPtflrLYLRNKKLHPLM 896
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6187 FAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTENT---TFSTTHTIVGE------QKEAvPIGKPINNSTAYIV 6257
Cdd:PRK08633  897 FASLRLVVAGAEKLK-PEVADAFEEKFGIRILEGYGATETSpvaSVNLPDVLAADfkrqtgSKEG-SVGMPLPGVAVRIV 974
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6258 D-SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVEssfLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYR 6336
Cdd:PRK08633  975 DpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEM 1051
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6337 IELGEIEEQLLKV---ASVKEATVIVREDESGQKqlCAYFVAERELTIGELRAALSQ-ELPNYMIPSHFVPLERMPLTPN 6412
Cdd:PRK08633 1052 VPLGAVEEELAKAlggEEVVFAVTAVPDEKKGEK--LVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGS 1129

                  ....*...
gi 386647928 6413 GKIDRRAL 6420
Cdd:PRK08633 1130 GKLDLKGL 1137
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
8064-8446 3.19e-29

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 124.91  E-value: 3.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8064 IEGP-LDRDRFEAVFRQLIERHETLRTGFEmANGEpvQRVYSDV---EFAV----EYSKADREEA-VEIAQRF-VRPFDL 8133
Cdd:cd19535    32 FDGEdLDPDRLERAWNKLIARHPMLRAVFL-DDGT--QQILPEVpwyGITVhdlrGLSEEEAEAAlEELRERLsHRVLDV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8134 RKPPLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYA--GEELPPLRIQYKDYAAWQRSEAYAKRVKQQEg 8211
Cdd:cd19535   109 ERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEdpGEPLPPLELSFRDYLLAEQALRETAYERARA- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8212 YWLQTLAgELPV-IELPT--DYERTSTRSFegAELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDII 8288
Cdd:cd19535   188 YWQERLP-TLPPaPQLPLakDPEEIKEPRF--TRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFL 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8289 VGTPVAGR--THADVEPIIGMFVNT--LAIRnyPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNP- 8363
Cdd:cd19535   265 LNLTLFNRlpLHPDVNDVVGDFTSLllLEVD--GSEGQSFLERARRLQQQLWEDLDHSSYSGVVVVRRLLRRRGGQPVLa 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8364 --VF----DTMFVLQNTEDR------GIeadafSLTPFVFdqtvaaqfdLTLSVAEDDGAIRGSFQYAAKLFKATMIRKM 8431
Cdd:cd19535   343 pvVFtsnlGLPLLDEEVREVlgelvyMI-----SQTPQVW---------LDHQVYEEDGGLLLNWDAVDELFPEGMLDDM 408
                         410
                  ....*....|....*
gi 386647928 8432 SKDLLAVLEQICGNP 8446
Cdd:cd19535   409 FDAYVRLLERLADDD 423
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
2334-2828 3.65e-29

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 130.04  E-value: 3.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2334 FNATAADYEADKTIHQLFEEQAERIPDHPAVV-FEGQQLTYRELNERANRLARTLQALgVKTDQPVGLMLERSlemVVGM 2412
Cdd:PRK08633  604 FDSWKSRKEALPPLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALARLLKRE-LKDEENVGILLPPS---VAGA 679
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2413 F---AVLKAGgaYVPIDPEYP--EDRISYMLEDSSAQVLLAQRRLQERVSFAG---------TVVTVDD--EQAYAGDG- 2475
Cdd:PRK08633  680 LanlALLLAG--KVPVNLNYTasEAALKSAIEQAQIKTVITSRKFLEKLKNKGfdlelpenvKVIYLEDlkAKISKVDKl 757
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2476 -----------SNLESAVGPN----DLAYIIYTSGTTGKPKGVMVEHHGLCS-LKQMfANTLQINAQDRVVqfASLSFda 2539
Cdd:PRK08633  758 tallaarllpaRLLKRLYGPTfkpdDTATIIFSSGSEGEPKGVMLSHHNILSnIEQI-SDVFNLRNDDVIL--SSLPF-- 832
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2540 scwevFQTLFFGATLYIPTKETI--------LDY----QWFERYMSDNGITTATLPPTYA--VYLNPDhmpDFK--RLIA 2603
Cdd:PRK08633  833 -----FHSFGLTVTLWLPLLEGIkvvyhpdpTDAlgiaKLVAKHRATILLGTPTFLRLYLrnKKLHPL---MFAslRLVV 904
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2604 AGsASSL--ELLQQWKDK--VKYFNAYGPTEDSICTTIWTPSTED---ISQLKSVP--IGGPIVNHRIYIVDAH-YQPVP 2673
Cdd:PRK08633  905 AG-AEKLkpEVADAFEEKfgIRILEGYGATETSPVASVNLPDVLAadfKRQTGSKEgsVGMPLPGVAVRIVDPEtFEELP 983
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2674 VGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQ 2753
Cdd:PRK08633  984 PGEDGLILIGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEE 1060
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 2754 LLKV--ASVQEAIVIAHDDASGQKQLCAYFVADrTMTVGELRGELS-GELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK08633 1061 LAKAlgGEEVVFAVTAVPDEKKGEKLVVLHTCG-AEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK08316 PRK08316
acyl-CoA synthetase; Validated
257-747 3.82e-29

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 126.59  E-value: 3.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  257 PRDTTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGA 336
Cdd:PRK08316    8 ARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  337 YVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERV---------------------SFSGTWIRLDDEEAYHEDGSNLES 395
Cdd:PRK08316   88 HVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAeaalallpvdtlilslvlggrEAPGGWLDFADWAEAGSVAEPDVE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  396 VNGpEHLTYVIYTSGTTGKPKGNLTTHRNIIrvvknTNYI------DVTGQDKLL---------QLssysfdgstfDIF- 459
Cdd:PRK08316  168 LAD-DDLAQILYTSGTESLPKGAMLTHRALI-----AEYVscivagDMSADDIPLhalplyhcaQL----------DVFl 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  460 -GALLNGAKLVLVPK---ETVLDvaklagLIEKQQIsvmfitTAFF---NVLVDMnpdcLRHAraiLFggERVSVSHVRK 532
Cdd:PRK08316  232 gPYLYVGATNVILDApdpELILR------TIEAERI------TSFFappTVWISL----LRHP---DF--DTRDLSSLRK 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  533 A--------------LGHLGPG-KIKHVYGPTESTVFATSYDVHEVEEGAVSipIGGPISNTAIYIVNAQNKLQPIGVAG 597
Cdd:PRK08316  291 GyygasimpvevlkeLRERLPGlRFYNCYGQTEIAPLATVLGPEEHLRRPGS--AGRPVLNVETRVVDDDGNDVAPGEVG 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  598 ELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLE 677
Cdd:PRK08316  369 EIVHRSPQLMLGYWDDPEKTAEAFRGGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHP 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  678 AIEK----------------ATVVVRESAngekqlcayyvadrSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGK 741
Cdd:PRK08316  442 AVAEvaviglpdpkwieavtAVVVPKAGA--------------TVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGK 507

                  ....*.
gi 386647928  742 VDRRAL 747
Cdd:PRK08316  508 ILKREL 513
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
2345-2828 4.45e-29

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 126.34  E-value: 4.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2345 KTIHQLFEEQAERIPDHPAVVFEG-----QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAG 2419
Cdd:PRK08008    7 QHLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2420 GAYVPIDPEYPEDRISYMLEDSSAQVLLAQ-------RRLQERVSFAGTVVTVDDEQAYAGDGS------------NLES 2480
Cdd:PRK08008   87 AIMVPINARLLREESAWILQNSQASLLVTSaqfypmyRQIQQEDATPLRHICLTRVALPADDGVssftqlkaqqpaTLCY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2481 AV--GPNDLAYIIYTSGTTGKPKGVMVEHHGLcslkqMFAN-----TLQINAQDRVVQ-FASLSFDASCWEVFQTLFFGA 2552
Cdd:PRK08008  167 APplSTDDTAEILFTSGTTSRPKGVVITHYNL-----RFAGyysawQCALRDDDVYLTvMPAFHIDCQCTAAMAAFSAGA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2553 TLYIPTK-------ETILDYQwferymsdngittATLppTYAvylnpdhMPDFKRLIAAGSASS-------------LEL 2612
Cdd:PRK08008  242 TFVLLEKysarafwGQVCKYR-------------ATI--TEC-------IPMMIRTLMVQPPSAndrqhclrevmfyLNL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2613 LQQWKD------KVKYFNAYGPTEdsicTTIW----TPSTEdisqlKSVP-IGGPIVNHRIYIVDAHYQPVPVGVAGELC 2681
Cdd:PRK08008  300 SDQEKDafeerfGVRLLTSYGMTE----TIVGiigdRPGDK-----RRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEIC 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2682 IAGV---GLARGYLNRPDLTAEKfvdnpFEPGERMYrTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVA 2758
Cdd:PRK08008  371 IKGVpgkTIFKEYYLDPKATAKV-----LEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHP 444
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2759 SVQEAIVIAHDDASGQKQLCAY--FVADRTMTVGELRGELSGELPGYMIPAhFVQL-ERMPLTPNGKIDRKAL 2828
Cdd:PRK08008  445 KIQDIVVVGIKDSIRDEAIKAFvvLNEGETLSEEEFFAFCEQNMAKFKVPS-YLEIrKDLPRNCSGKIIKKNL 516
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1288-1804 4.78e-29

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 126.41  E-value: 4.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1288 PAAPDAPENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAV 1367
Cdd:PRK06155   12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1368 WKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQER---AQQWGQTLQAVLCLDDEAAYAEDAS------------ 1432
Cdd:PRK06155   92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAAleaADPGDLPLPAVWLLDAPASVSVPAGwstaplppldap 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1433 -NVANVnEPHDLAYVIYTSGTTGRPKGVMIEHRSL----VNTAAGY---RREYRLDQFPV-RLLQLASFSfdvfvgdiaR 1503
Cdd:PRK06155  172 aPAAAV-QPGDTAAILYTSGTTGPSKGVCCPHAQFywwgRNSAEDLeigADDVLYTTLPLfHTNALNAFF---------Q 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1504 TLYNGGTMVICPKddridparlhywiseekitiFESTpaliiPFMDYVAEHGL-------DMSSMELLITSSDSCSVTDY 1576
Cdd:PRK06155  242 ALLAGATYVLEPR--------------------FSAS-----GFWPAVRRHGAtvtyllgAMVSILLSQPARESDRAHRV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1577 RV-------------LQERFGsqFRIINAYGVTEAaiDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLNPVPVGV 1643
Cdd:PRK06155  297 RValgpgvpaalhaaFRERFG--VDLLDGYGSTET--NFVIAVTHGSQRPGS----MGRLAPGFEARVVDEHDQELPDGE 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1644 LGELCIGG---IGVARGYLNRPELTEEKFVDSPFVEGERLYRTgdlarwmPDGNVDFIGRIDNQAKIRGYRIETGEIETQ 1720
Cdd:PRK06155  369 PGELLLRAdepFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQV 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1721 LLKAEGVREavvvvredakgqkvlCAYFTAESELKLSE------LRSSLSQE-----------LPGYMIPSYFVQLEQLP 1783
Cdd:PRK06155  442 LLSHPAVAA---------------AAVFPVPSELGEDEvmaavvLRDGTALEpvalvrhceprLAYFAVPRYVEFVAALP 506
                         570       580
                  ....*....|....*....|.
gi 386647928 1784 LTANGKIDRKALPAPDASMQT 1804
Cdd:PRK06155  507 KTENGKVQKFVLREQGVTADT 527
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
286-747 4.82e-29

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 125.91  E-value: 4.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNaGVQADQLVGLMVERSLEMIVGIMGILKAGgaYVPIDPEYP--EERIRYMLEDSGTQVLLS 363
Cdd:cd05909     8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIKTVLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  364 QGHLQER--------VSFSGTWIRLDDEEA----------------YHEDGSNLESVNG--PEHLTYVIYTSGTTGKPKG 417
Cdd:cd05909    85 SKQFIEKlklhhlfdVEYDARIVYLEDLRAkiskadkckaflagkfPPKWLLRIFGVAPvqPDDPAVILFTSGSEGLPKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  418 NLTTHRNIIRVVKN-TNYIDVTGQDKLLQ----LSSYSFDGStfdIFGALLNGAKLVLVPKEtvLDVAKLAGLIEKQQIS 492
Cdd:cd05909   165 VVLSHKNLLANVEQiTAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVVFHPNP--LDYKKIPELIYDKKAT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  493 VMFITTAFFNVLVD-MNPDCLRHARAILFGGERVSVSHVRKALGHLGPgKIKHVYGPTE-STVFATSYDVHEVEEGAVsi 570
Cdd:cd05909   240 ILLGTPTFLRGYARaAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGI-RILEGYGTTEcSPVISVNTPQSPNKEGTV-- 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  571 piGGPISNTAIYIVNAQNKLQ-PIGVAGELCVAGDGLARGYLNRPDLTAekfadnpFAPGERMYRTGDLARWLPDGTIEY 649
Cdd:cd05909   317 --GRPLPGMEVKIVSVETHEEvPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFLTI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  650 VGRIDDQVKIRGFRIELGEIEAHLLKLEAIEK--ATVVVRESANGEK-QLCayyVADRSLPANEVRSTLSQ-ELPAYMLP 725
Cdd:cd05909   388 TGRLSRFAKIAGEMVSLEAIEDILSEILPEDNevAVVSVPDGRKGEKiVLL---TTTTDTDPSSLNDILKNaGISNLAKP 464
                         490       500
                  ....*....|....*....|..
gi 386647928  726 SYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05909   465 SYIHQVEEIPLLGTGKPDYVTL 486
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
2352-2849 5.22e-29

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 126.43  E-value: 5.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2352 EEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVK-TDQPVGLMLERSlEMVVGMFAVLKAGGAYVPIDPEYP 2430
Cdd:PRK07786   24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGfGDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFRLT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2431 EDRISYMLEDSSAQVLLAQRRLQ-------ERVSFAGTVVTVDD---------EQAYAGDGSNLESAVGPNDL-AYIIYT 2493
Cdd:PRK07786  103 PPEIAFLVSDCGAHVVVTEAALApvatavrDIVPLLSTVVVAGGssddsvlgyEDLLAEAGPAHAPVDIPNDSpALIMYT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2494 SGTTGKPKGVMVEHHGLC--SLKQMFANTLQINAQdrvVQFASLSF--DASCWEVFQTLFFGATLYI-PTKE----TILD 2564
Cdd:PRK07786  183 SGTTGRPKGAVLTHANLTgqAMTCLRTNGADINSD---VGFVGVPLfhIAGIGSMLPGLLLGAPTVIyPLGAfdpgQLLD 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2565 YQWFERymsdngITTATLPPT--YAVYLNPDHMP-DFK-RLIAAGSA-SSLELLQQWKD---KVKYFNAYGPTEDSICTT 2636
Cdd:PRK07786  260 VLEAEK------VTGIFLVPAqwQAVCAEQQARPrDLAlRVLSWGAApASDTLLRQMAAtfpEAQILAAFGQTEMSPVTC 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2637 IWtpSTED-ISQLKSVpiGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEpgermyr 2715
Cdd:PRK07786  334 ML--LGEDaIRKLGSV--GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH------- 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2716 TGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV---ADRTMTVGEL 2792
Cdd:PRK07786  403 SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnDDAALTLEDL 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 2793 RGELSGELPGYMIPAHFVQLERMPLTPNGKID----RKALPAPqGNASAGADYVAPRSEEE 2849
Cdd:PRK07786  483 AEFLTDRLARYKHPKALEIVDALPRNPAGKVLktelRERYGAC-VNVERRSASAGFTERRE 542
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
7591-7925 6.73e-29

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 121.98  E-value: 6.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7591 VIYTSGTTGKPKGVMVEHhglcslKLMFAET-------LRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIpAKDTI 7663
Cdd:cd17635     6 VIFTSGTTGEPKAVLLAN------KTFFAVPdilqkegLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT-GGENT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7664 LDYPLFESyMNENGITAAILPPT---YAIYLSPDRL---PSLKKLITGGS---AASVEFVQqWKDKVRYFNAYGPTEASI 7734
Cdd:cd17635    79 TYKSLFKI-LTTNAVTTTCLVPTllsKLVSELKSANatvPSLRLIGYGGSraiAADVRFIE-ATGLTNTAQVYGLSETGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7735 VTSVwaasPDGLDLRSV-PIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagerm 7813
Cdd:cd17635   157 ALCL----PTDDDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV------ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7814 yRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELR 7893
Cdd:cd17635   227 -NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIR 305
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 386647928 7894 G---TLSQELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd17635   306 AlkhTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
285-704 7.27e-29

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 124.78  E-value: 7.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  285 QLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQ 364
Cdd:cd17640     5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  365 ghlqervsfsgtwirlddeeayhedgsnlesvNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTN-YIDVTGQDKL 443
Cdd:cd17640    85 --------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSdIVPPQPGDRF 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  444 LQL--SSYSFDGStFDIFGALLNGAKLVLVPKETVLDVAKLaglieKQQ--ISVMFITTAFFN----VLVDMNPDCLRHA 515
Cdd:cd17640   133 LSIlpIWHSYERS-AEYFIFACGCSQAYTSIRTLKDDLKRV-----KPHyiVSVPRLWESLYSgiqkQVSKSSPIKQFLF 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  516 RAILFGGE-RVSVS-------HVRKALGHLGPgKIKHVYGPTESTVFATSYDVHEVEEGAVsipiGGPISNTAIYIVNAQ 587
Cdd:cd17640   207 LFFLSGGIfKFGISgggalppHVDTFFEAIGI-EVLNGYGLTETSPVVSARRLKCNVRGSV----GRPLPGTEIKIVDPE 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  588 -NKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVKIR-GFRIE 665
Cdd:cd17640   282 gNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVE 355
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 386647928  666 LGEIEAHLLKLEAIEKATVVVREsangEKQLCAYYVADR 704
Cdd:cd17640   356 PQPIEEALMRSPFIEQIMVVGQD----QKRLGALIVPNF 390
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
7456-7930 8.62e-29

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 125.49  E-value: 8.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:PRK13383   45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHlAYVIYTSGTTGKPKGVMVEHHglcsLK 7615
Cdd:PRK13383  125 AAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG-RIVLLTSGTTGKPKGVPRAPQ----LR 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7616 LMFAETLRITEEDRVVQFASLSFDAScweIFKALFFGA-TLYIPAKDTILDYPLFE--------SYMNENGITAaiLPPT 7686
Cdd:PRK13383  200 SAVGVWVTILDRTRLRTGSRISVAMP---MFHGLGLGMlMLTIALGGTVLTHRHFDaeaalaqaSLHRADAFTA--VPVV 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7687 YAIYLS-PDR------LPSLKKLITGGSAASVEFVQQWKDKVR--YFNAYGPTEASIVTsvwAASPdgLDLRSVP--IGR 7755
Cdd:PRK13383  275 LARILElPPRvrarnpLPQLRVVMSSGDRLDPTLGQRFMDTYGdiLYNGYGSTEVGIGA---LATP--ADLRDAPetVGK 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7756 PIANHQIFIVDSQNHmlPVG--VAGELCISGaglargylnrpELTAEKFVDNPFLAG-ERMYRTGDLARWLPDGNIEYLG 7832
Cdd:PRK13383  350 PVAGCPVRILDRNNR--PVGprVTGRIFVGG-----------ELAGTRYTDGGGKAVvDGMTSTGDMGYLDNAGRLFIVG 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7833 RIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA--DRELTVSELRGTLSQELPGYMIPSYFV 7910
Cdd:PRK13383  417 REDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLhpGSGVDAAQLRDYLKDRVSRFEQPRDIN 496
                         490       500
                  ....*....|....*....|
gi 386647928 7911 QLEQMPLTPNGKIDRNALPA 7930
Cdd:PRK13383  497 IVSSIPRNPTGKVLRKELPG 516
PRK07638 PRK07638
acyl-CoA synthetase; Validated
2346-2828 8.65e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 124.89  E-value: 8.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLArtlQALGVKTDQP--VGLMLERSLEMVVGMFAVLKAGGAYV 2423
Cdd:PRK07638    2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVA---NWLNEKESKNktIAILLENRIEFLQLFAGAAMAGWTCV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2424 PIDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDE-----QAYAGDGSNLESAvgPNDLAYIIYTSGTTG 2498
Cdd:PRK07638   79 PLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEwkrmiEKYLPTYAPIENV--QNAPFYMGFTSGSTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2499 KPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIptKETILDYQWFERYMSDNGIT 2578
Cdd:PRK07638  157 KPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL--MRKFIPNQVLDKLETENISV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2579 TATLPPTYAVYLNPDHMPDFK-RLIAAG---SASSLELLQQWKDKVKYFNAYGPTEDSICTTIwtpSTEDiSQLKSVPIG 2654
Cdd:PRK07638  235 MYTVPTMLESLYKENRVIENKmKIISSGakwEAEAKEKIKNIFPYAKLYEFYGASELSFVTAL---VDEE-SERRPNSVG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2655 GPIVNHRIYIVDAhyqpvpvgvAGELCIAG-VGlaRGYLNRPDLTAEKFVD--NPFEPGERMYRTGDLAKWL-PDGTIEY 2730
Cdd:PRK07638  311 RPFHNVQVRICNE---------AGEEVQKGeIG--TVYVKSPQFFMGYIIGgvLARELNADGWMTVRDVGYEdEEGFIYI 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2731 LGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFvaDRTMTVGELRGELSGELPGYMIPAHFV 2810
Cdd:PRK07638  380 VGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLKSFCLQRLSSFKIPKEWH 457
                         490
                  ....*....|....*...
gi 386647928 2811 QLERMPLTPNGKIDRKAL 2828
Cdd:PRK07638  458 FVDEIPYTNSGKIARMEA 475
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
2346-2828 8.75e-29

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 125.90  E-value: 8.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI 2425
Cdd:PRK07059   24 SLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2426 DPEYPEDRISYMLEDSSA--------------QVL-------------------------LAQRRLQERV---SFAGTVv 2463
Cdd:PRK07059  104 NPLYTPRELEHQLKDSGAeaivvlenfattvqQVLaktavkhvvvasmgdllgfkghivnFVVRRVKKMVpawSLPGHV- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2464 TVDDEQAyAGDGSNLESA-VGPNDLAYIIYTSGTTGKPKGVMVEHHGLcslkqmFANTLQINA--------QDRVVQFAS 2534
Cdd:PRK07059  183 RFNDALA-EGARQTFKPVkLGPDDVAFLQYTGGTTGVSKGATLLHRNI------VANVLQMEAwlqpafekKPRPDQLNF 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2535 LsfdasC----WEVFQ-TLFF-------GATLYIPTKETILDY-QWFERYMSDNGITTATLpptYAVYLN-PD-HMPDFK 2599
Cdd:PRK07059  256 V-----CalplYHIFAlTVCGllgmrtgGRNILIPNPRDIPGFiKELKKYQVHIFPAVNTL---YNALLNnPDfDKLDFS 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2600 RLIAA---GSASSLELLQQWKDKVKYF--NAYGPTEDSICTTIWTPSTEDISQlksvPIGGPIVNHRIYIVDAHYQPVPV 2674
Cdd:PRK07059  328 KLIVAnggGMAVQRPVAERWLEMTGCPitEGYGLSETSPVATCNPVDATEFSG----TIGLPLPSTEVSIRDDDGNDLPL 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2675 GVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQL 2754
Cdd:PRK07059  404 GEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 2755 LKVASVQEAIVIA-HDDASGqkQLCAYFVA--DRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK07059  478 ASHPGVLEVAAVGvPDEHSG--EAVKLFVVkkDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
3880-4334 9.14e-29

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 124.48  E-value: 9.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALltqr 3959
Cdd:cd05914     8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 hlrervsfagtFVAVDDEqayhadgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVV 4039
Cdd:cd05914    84 -----------FVSDEDD------------------VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKIL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4040 QFASLSFDASC-WEIFKALFFGATLY----IPTSTTILD--------------YPLFESYMNE--NGITATILPPTYAAY 4098
Cdd:cd05914   135 SILPLHHIYPLtFTLLLPLLNGAHVVfldkIPSAKIIALafaqvtptlgvpvpLVIEKIFKMDiiPKLTLKKFKFKLAKK 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4099 LNPDRMPSL-------------KKLITGGSAASVEFVQQWKD-KVLYFNAYGPTEAS--IVTSIWDEAsdslgdrKSVPI 4162
Cdd:cd05914   215 INNRKIRKLafkkvheafggniKEFVIGGAKINPDVEEFLRTiGFPYTIGYGMTETApiISYSPPNRI-------RLGSA 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4163 GRPLANHRIYVVDSHnrmlPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGR 4242
Cdd:cd05914   288 GKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAEGYLYIRGR 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4243 IDHQ-VKIRGYRIELGEVETQLAKIDAVQEAIVLAREDaNGQQQLVAYFVA-------QRELTAA---ELRATMSQELPN 4311
Cdd:cd05914   358 KKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK-KLVALAYIDPDFldvkalkQRNIIDAikwEVRDKVNQKVPN 436
                         490       500
                  ....*....|....*....|....
gi 386647928 4312 Y-MIPSYFVQLAQMPLTPNGKIDR 4334
Cdd:cd05914   437 YkKISKVKIVKEEFEKTPKGKIKR 460
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
2364-2825 9.74e-29

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 124.48  E-value: 9.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2364 VVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSA 2443
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2444 QVLlaqrrlqervsfagtvvtvddeqaYAGDgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQI 2523
Cdd:cd05914    81 KAI------------------------FVSD---------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2524 NAQDRVVQFASLSFDASCWEVFQT-LFFGATLYIPTKET--ILDYQWFERYMSDNGIT----------TATLPPT----- 2585
Cdd:cd05914   128 GKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPsaKIIALAFAQVTPTLGVPvplviekifkMDIIPKLtlkkf 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2586 -YAVYLNPDHMP---------------DFKRLIAAGSASSLELLQQWKD-KVKYFNAYGPTEDS--ICTTIWtpstediS 2646
Cdd:cd05914   208 kFKLAKKINNRKirklafkkvheafggNIKEFVIGGAKINPDVEEFLRTiGFPYTIGYGMTETApiISYSPP-------N 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2647 QLKSVPIGGPIVNHRIYIvdahYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDG 2726
Cdd:cd05914   281 RIRLGSAGKVIDGVEVRI----DSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAEG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2727 TIEYLGRIDHQ-VKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASgqkQLCAYFVADRTMTVG------------ELR 2793
Cdd:cd05914   351 YLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL---VALAYIDPDFLDVKAlkqrniidaikwEVR 427
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 2794 GELSGELPGYMIPAHF-VQLERMPLTPNGKIDR 2825
Cdd:cd05914   428 DKVNQKVPNYKKISKVkIVKEEFEKTPKGKIKR 460
PRK08315 PRK08315
AMP-binding domain protein; Validated
4891-5380 1.16e-28

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 125.69  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4891 ALFEKQAECTPEAAAVVY--ENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 4968
Cdd:PRK08315   20 QLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4969 PDYPSDRIQFMLEDSAASVLLTQTH---------LQE-----RAQQWGQtLQAA--------LCLDDEA-----AYAEDA 5021
Cdd:PRK08315  100 PAYRLSELEYALNQSGCKALIAADGfkdsdyvamLYElapelATCEPGQ-LQSArlpelrrvIFLGDEKhpgmlNFDELL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5022 SNVANVNE-----------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA------GYRREYRLdQFPVRLLQlasfSF 5084
Cdd:PRK08315  179 ALGRAVDDaelaarqatldPDDPINIQYTSGTTGFPKGATLTHRNILNNGYfigeamKLTEEDRL-CIPVPLYH----CF 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5085 DVFVGDIArTLYNGGTMVIcPKDdRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVT 5164
Cdd:PRK08315  254 GMVLGNLA-CVTHGATMVY-PGE-GFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIE 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5165 DYRVLQERFG-SQFRIinAYGVTEAA--IDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLN-PVPVGVLGELCIG 5240
Cdd:PRK08315  331 VMKRVIDKMHmSEVTI--AYGMTETSpvSTQTRTDDPLEKRVTT----VGRALPHLEVKIVDPETGeTVPRGEQGELCTR 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5241 GIGVARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIdnqaK---IRG----Y-RietgEIETQLL 5312
Cdd:PRK08315  405 GYSVMKGYWNDPEKTAEA------IDADGWMHTGDLAVMDEEGYVNIVGRI----KdmiIRGgeniYpR----EIEEFLY 470
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5313 KAEGVREAVVVVREDAKGQKVLCA--HFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:PRK08315  471 THPKIQDVQVVGVPDEKYGEEVCAwiILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
PRK07529 PRK07529
AMP-binding domain protein; Validated
7446-7928 1.16e-28

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 126.61  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7446 QTIHGLFEEQAERMPEKAAVVF--------ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIM 7517
Cdd:PRK07529   25 ASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7518 KAGGAyVPIDPEYPEDRIRYMLEDSGAQVLLTQR-------------------HLQECVSFDG----------------- 7561
Cdd:PRK07529  105 AAGIA-NPINPLLEPEQIAELLRAAGAKVLVTLGpfpgtdiwqkvaevlaalpELRTVVEVDLarylpgpkrlavplirr 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7562 ----KVIAADDEQAyGEDGSNLE--PVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDrvVQFAS 7635
Cdd:PRK07529  184 kahaRILDFDAELA-RQPGDRLFsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGD--TVFCG 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7636 LSF---DASCWEIFKALFFGATLYIPakdTILDY----------PLFESYmnenGITAAILPPT-YAIYLS--PDR--LP 7697
Cdd:PRK07529  261 LPLfhvNALLVTGLAPLARGAHVVLA---TPQGYrgpgvianfwKIVERY----RINFLSGVPTvYAALLQvpVDGhdIS 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7698 SLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEASIVTSVwaASPDGlDLRSVPIGRPIANHQIFIV--DSQNHML- 7772
Cdd:PRK07529  334 SLRYALCGAAPLPVEVFRRFEAAtgVRIVEGYGLTEATCVSSV--NPPDG-ERRIGSVGLRLPYQRVRVVilDDAGRYLr 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7773 --PVGVAGELCISGAGLARGYLNrpeltAEKfvDNPFLAGERMYRTGDLARWLPDGNIEYLGRidhqVK---IR-GYRIE 7846
Cdd:PRK07529  411 dcAVDEVGVLCIAGPNVFSGYLE-----AAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGR----AKdliIRgGHNID 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7847 LGEIEEQLLKIASVQETIVIARGDANGQQQLCAY--FVADRELTVSELRGTLSQELPG-YMIPSYFVQLEQMPLTPNGKI 7923
Cdd:PRK07529  480 PAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYvqLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKI 559

                  ....*
gi 386647928 7924 DRNAL 7928
Cdd:PRK07529  560 FKPAL 564
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
3856-4339 1.37e-28

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 126.07  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3856 IHGLFEEQALRNPDAVAVVFEKSQ-----LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGA 3930
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3931 YIPIDPEYPEDRIRYMLEDSGAQALLTQ--------------------------------RHLRERVSFA-GTFVAVDDE 3977
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkeeadkacaqcptvekvvvvRHLGNDFTPAkGRDLSYDEE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3978 QAYHADGSNLepvVGPNHLAYVIYTSGTTGKPKGVmVEHHGLCSLKLMF--ANTLQMTEQDRVVQFASLSFDASCWEIFK 4055
Cdd:cd05968   223 KETAGDGAER---TESEDPLMIIYTSGTTGKPKGT-VHVHAGFPLKAAQdmYFQFDLKPGDLLTWFTDLGWMMGPWLIFG 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4056 ALFFGATLYIPTSTTILDYPLFESYMNEN------GITATI---LPPTYAAYLNPDRMPSLKKLITGGSAASVE-----F 4121
Cdd:cd05968   299 GLILGATMVLYDGAPDHPKADRLWRMVEDheithlGLSPTLiraLKPRGDAPVNAHDLSSLRVLGSTGEPWNPEpwnwlF 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4122 VQQWKDKVLYFNAYGPTEASivtsiwdeaSDSLGDRKSVPI-----GRPLANHRIYVVDSHNRMLPVGVaGELCISG--V 4194
Cdd:cd05968   379 ETVGKGRNPIINYSGGTEIS---------GGILGNVLIKPIkpssfNGPVPGMKADVLDESGKPARPEV-GELVLLApwP 448
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4195 GLARGYLNRPeltaEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIV 4274
Cdd:cd05968   449 GMTRGFWRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAA 524
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4275 LAREDANGQQQLVAYFV-----AQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:cd05968   525 IGVPHPVKGEAIVCFVVlkpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
2368-2828 1.45e-28

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 124.95  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2368 GQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLL 2447
Cdd:cd17642    42 GVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVF 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2448 AQRR-------LQERVSFAGTVVTVD---DEQAYAGDGSNLESAVGPN---------------DLAYIIYTSGTTGKPKG 2502
Cdd:cd17642   122 CSKKglqkvlnVQKKLKIIKTIIILDskeDYKGYQCLYTFITQNLPPGfneydfkppsfdrdeQVALIMNSSGSTGLPKG 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2503 VMVEHHGLCS-----LKQMFANtlQINAQDRVVQFASLSFDASCWEVFQTLFFGATL-YIPTKETILdyqwFERYMSDNG 2576
Cdd:cd17642   202 VQLTHKNIVArfshaRDPIFGN--QIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVvLMYKFEEEL----FLRSLQDYK 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2577 ITTATLPPTYAVYLNPDHMPDFKRL-----IAAGSAS-SLELLQQWKDKVKY---FNAYGPTEDSICTTIwTPSTEDisq 2647
Cdd:cd17642   276 VQSALLVPTLFAFFAKSTLVDKYDLsnlheIASGGAPlSKEVGEAVAKRFKLpgiRQGYGLTETTSAILI-TPEGDD--- 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2648 lKSVPIGGPIVNHRIYIVDAHY-QPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDG 2726
Cdd:cd17642   352 -KPGAVGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGW------LHSGDIAYYDEDG 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2727 TIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA-HDDASGqkQLCAYFV---ADRTMTVGELRGELSGEL-P 2801
Cdd:cd17642   425 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGiPDEDAG--ELPAAVVvleAGKTMTEKEVMDYVASQVsT 502
                         490       500
                  ....*....|....*....|....*..
gi 386647928 2802 GYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd17642   503 AKRLRGGVKFVDEVPKGLTGKIDRRKI 529
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
3845-4339 1.71e-28

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 126.68  E-value: 1.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3845 NTAAEYQQEQTIHGLFEEQALRNPDAVavvfeksqlTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAI 3924
Cdd:PRK06060    5 NLAGLLAEQASEAGWYDRPAFYAADVV---------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLAC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3925 MKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFAGTFVAVD-DEQAYHADGSNLEPVVGpNHLAYVIYTS 4003
Cdd:PRK06060   76 LARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAElMSEAARVAPGGYEPMGG-DALAYATYTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4004 GTTGKPKGVMVEHHGLCS-LKLMFANTLQMTEQDRVVQFASLSFdascweifkALFFGATLYIP--TSTTILDYPLFESY 4080
Cdd:PRK06060  155 GTTGPPKAAIHRHADPLTfVDAMCRKALRLTPEDTGLCSARMYF---------AYGLGNSVWFPlaTGGSAVINSAPVTP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4081 MNENGITATILP------PTYAAYL----NPDRMPSLKKLITGGSAASV---EFVQQWKDKVLYFNAYGPTEASIVTsiw 4147
Cdd:PRK06060  226 EAAAILSARFGPsvlygvPNFFARVidscSPDSFRSLRCVVSAGEALELglaERLMEFFGGIPILDGIGSTEVGQTF--- 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4148 deASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPE--LTAEKFVDnpfepgermyrT 4225
Cdd:PRK06060  303 --VSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------T 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4226 GDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQR-----ELTAAE 4300
Cdd:PRK06060  370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgatidGSVMRD 449
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 386647928 4301 LRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:PRK06060  450 LHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
PRK06164 PRK06164
acyl-CoA synthetase; Validated
7444-7928 2.30e-28

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 124.47  E-value: 2.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7444 REQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAY 7523
Cdd:PRK06164    8 RADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7524 VPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQEcVSFDGKVIAADDEQ--------AYGEDGSNL---------------- 7579
Cdd:PRK06164   88 IAVNTRYRSHEVAHILGRGRARWLVVWPGFKG-IDFAAILAAVPPDAlpplraiaVVDDAADATpapapgarvqlfalpd 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7580 --------EPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVqfASLSFDAScweifkalfF 7651
Cdd:PRK06164  167 pappaaagERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLL--AALPFCGV---------F 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7652 G-ATL--YIPAKDTILDYPLFES-----YMNENGITAAI-----LPPTYAIYLSPDRLPSLKKL-ITGGSAASVEFVQQW 7717
Cdd:PRK06164  236 GfSTLlgALAGGAPLVCEPVFDAartarALRRHRVTHTFgndemLRRILDTAGERADFPSARLFgFASFAPALGELAALA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7718 KDK-VRYFNAYGPTEASIVTSVWAASPDgLDLRSVPIGRPI-ANHQIFIVDSQN-HMLPVGVAGELCISGAGLARGYLNR 7794
Cdd:PRK06164  316 RARgVPLTGLYGSSEVQALVALQPATDP-VSVRIEGGGRPAsPEARVRARDPQDgALLPDGESGEIEIRAPSLMRGYLDN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7795 PELTAEKFVDNPFlagermYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIArGDANGQ 7874
Cdd:PRK06164  395 PDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG-ATRDGK 467
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 7875 QQLCAYFVAD--RELTVSELRGTLSQELPGYMIPSYFVQLEQMPLT--PNG-KIDRNAL 7928
Cdd:PRK06164  468 TVPVAFVIPTdgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
7446-7928 2.67e-28

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 124.55  E-value: 2.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7446 QTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYV 7524
Cdd:PRK12492   24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7525 PIDPEYPEDRIRYMLEDSGAQVL----LTQRHLQECV------------------SFDGKVI------------------ 7564
Cdd:PRK12492  104 NTNPLYTAREMRHQFKDSGARALvylnMFGKLVQEVLpdtgieylieakmgdllpAAKGWLVntvvdkvkkmvpayhlpq 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7565 AADDEQAYGED-GSNLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCS--------LKLMFAETLRITEEDRVVQFA 7634
Cdd:PRK12492  184 AVPFKQALRQGrGLSLKPVpVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnmlqvracLSQLGPDGQPLMKEGQEVMIA 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7635 SL------SFDASC----------------------------WEiFKALFFGATLYIpakdTILDYPLFESYmnengita 7680
Cdd:PRK12492  264 PLplyhiyAFTANCmcmmvsgnhnvlitnprdipgfikelgkWR-FSALLGLNTLFV----ALMDHPGFKDL-------- 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7681 ailpptyaiylspdRLPSLKKLITGGSAASVEFVQQWKDKV--RYFNAYGPTEASIVTSvwaASPDGLDLRSVPIGRPIA 7758
Cdd:PRK12492  331 --------------DFSALKLTNSGGTALVKATAERWEQLTgcTIVEGYGLTETSPVAS---TNPYGELARLGTVGIPVP 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7759 NHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKfvdnpfLAGERMYRTGDLARWLPDGNIEYLGRIDHQV 7838
Cdd:PRK12492  394 GTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEA------LDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7839 KIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA-DRELTVSELRGTLSQELPGYMIPSYFVQLEQMPL 7917
Cdd:PRK12492  468 IVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVArDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPM 547
                         570
                  ....*....|.
gi 386647928 7918 TPNGKIDRNAL 7928
Cdd:PRK12492  548 TPVGKILRREL 558
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
5950-6430 4.55e-28

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 123.85  E-value: 4.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5950 DHLAVTFEDKQ----LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIR 6025
Cdd:PRK04319   59 DKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6026 YMLEDSGAKLLLVQGHLLDR------------------ASFADKLVNLNDDGAYHEDGSNLEPVNgPEHLTYVIYTSGTT 6087
Cdd:PRK04319  139 DRLEDSEAKVLITTPALLERkpaddlpslkhvllvgedVEEGPGTLDFNALMEQASDEFDIEWTD-REDGAILHYTSGST 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6088 GRPKGVMVEHRNVVrlvkntnyvelneqTHiLQTGAVVFD-----------------ASTFEIWGALLNGGRLYVVRNEt 6150
Cdd:PRK04319  218 GKPKGVLHVHNAML--------------QH-YQTGKYVLDlheddvywctadpgwvtGTSYGIFAPWLNGATNVIDGGR- 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6151 iLDAVSLKNAIQQYGInTMWLTAPlynqlsqqdsgmfAGLKTLIVGGD-------------VLSV-----PHINRVLREH 6212
Cdd:PRK04319  282 -FSPERWYRILEDYKV-TVWYTAP-------------TAIRMLMGAGDdlvkkydlsslrhILSVgeplnPEVVRWGMKV 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6213 AGLSIVNGYGPTEnttfstTHTIVGEQKEAVPI-----GKPINNSTAYIVDSKLSLLPVGVWGELIV--GGDGVARGYLN 6285
Cdd:PRK04319  347 FGLPIHDNWWMTE------TGGIMIANYPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWN 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6286 RPeltaEKFvESSFLPGerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESG 6365
Cdd:PRK04319  421 NP----EKY-ESYFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVR 493
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 6366 QKQLCAyFVAER-------ELtIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPAPQGNAPVG 6430
Cdd:PRK04319  494 GEIIKA-FVALRpgyepseEL-KEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELGLPEG 563
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1301-1795 5.40e-28

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 122.87  E-value: 5.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1301 ALFEKQAERTpevaAVVYEN-----DRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYV 1375
Cdd:PRK08008   15 DLADVYGHKT----ALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1376 PLDPDYPSDRIQFMLEDSAASVLLTQTH---LQERAQQWGQTLQAVLCLDDEAAYAED---------ASNVANVNE---- 1439
Cdd:PRK08008   91 PINARLLREESAWILQNSQASLLVTSAQfypMYRQIQQEDATPLRHICLTRVALPADDgvssftqlkAQQPATLCYappl 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1440 -PHDLAYVIYTSGTTGRPKGVMIEHRSLVntAAGYRREY--RLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPK 1516
Cdd:PRK08008  171 sTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEK 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1517 DDridpARlHYW--ISEEKITIFESTPALI-----IPFMDYVAEHGL-DMssMELLitssdSCSVTDYRVLQERFGsqFR 1588
Cdd:PRK08008  249 YS----AR-AFWgqVCKYRATITECIPMMIrtlmvQPPSANDRQHCLrEV--MFYL-----NLSDQEKDAFEERFG--VR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1589 IINAYGVTEAaIDSSLYDEPlaklPEAGNVP-IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGI---GVARGYLNRPEL 1664
Cdd:PRK08008  315 LLTSYGMTET-IVGIIGDRP----GDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1665 TEEKFvdspfvEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVL 1744
Cdd:PRK08008  390 TAKVL------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAI 463
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 1745 CAY--FTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK08008  464 KAFvvLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
3851-4337 5.70e-28

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 126.19  E-value: 5.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3851 QQEQTIHGLFEEQALRNPDAVAVV-FEKSQLTYGELNERANRLARTLRDaGVRPDQLVGLMVERSLEMVVGIMAIMKAGg 3929
Cdd:PRK08633  612 EALPPLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALARLLKR-ELKDEENVGILLPPSVAGALANLALLLAG- 689
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3930 aYIPIDPEYP--EDRIRYMLEDSGAQALLTQRHLRERVSFAG---------TFVAVDD--------------EQAYHADG 3984
Cdd:PRK08633  690 -KVPVNLNYTasEAALKSAIEQAQIKTVITSRKFLEKLKNKGfdlelpenvKVIYLEDlkakiskvdkltalLAARLLPA 768
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3985 SNLEPVVGPNH----LAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVqfASLSFdascweiFKALFFG 4060
Cdd:PRK08633  769 RLLKRLYGPTFkpddTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVIL--SSLPF-------FHSFGLT 839
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4061 ATLYIPTSTTI--------LDYPLFESYMNENGITATILPPTY-AAYL-----NPDRMPSLKKLITGGSAASVEFVQQWK 4126
Cdd:PRK08633  840 VTLWLPLLEGIkvvyhpdpTDALGIAKLVAKHRATILLGTPTFlRLYLrnkklHPLMFASLRLVVAGAEKLKPEVADAFE 919
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4127 DK--VLYFNAYGPTEASIVTS-----IWDEASDSLGDRKSVPIGRPLANHRIYVVDSHN-RMLPVGVAGELCISGVGLAR 4198
Cdd:PRK08633  920 EKfgIRILEGYGATETSPVASvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDPETfEELPPGEDGLILIGGPQVMK 999
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4199 GYLNRPELTAEKFVDnpfEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKI--DAVQEAIVLA 4276
Cdd:PRK08633 1000 GYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVFAVTA 1076
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 4277 REDANGQQQLVAyFVAQRELTAAELRATMSQ-ELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK08633 1077 VPDEKKGEKLVV-LHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
3853-4337 5.91e-28

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 122.87  E-value: 5.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3853 EQTIHGLFEEQALRNPDAVAVVFEK-----SQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKA 3927
Cdd:PRK08008    6 GQHLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3928 GGAYIPIDPEYPEDRIRYMLEDSGAQALLTQ-------RHLRERVSFAGTFVAVDDEQAYHADGS--------------N 3986
Cdd:PRK08008   86 GAIMVPINARLLREESAWILQNSQASLLVTSaqfypmyRQIQQEDATPLRHICLTRVALPADDGVssftqlkaqqpatlC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3987 LEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQ-FASLSFDASCWEIFKALFFGATLYI 4065
Cdd:PRK08008  166 YAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTvMPAFHIDCQCTAAMAAFSAGATFVL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4066 PTSTT-------ILDY--------PLFesymnengITATILPPTYAAylnpDRMPSLKKLITGGSAASVE---FVQQWKd 4127
Cdd:PRK08008  246 LEKYSarafwgqVCKYratiteciPMM--------IRTLMVQPPSAN----DRQHCLREVMFYLNLSDQEkdaFEERFG- 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4128 kVLYFNAYGPTEaSIVTSIWDEASDSlgdRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGV---GLARGYLNRP 4204
Cdd:PRK08008  313 -VRLLTSYGMTE-TIVGIIGDRPGDK---RRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDP 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4205 ELTAEKfvdnpFEPGERMYrTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQ 4284
Cdd:PRK08008  388 KATAKV-----LEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 4285 QLVAY--FVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK08008  462 AIKAFvvLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
2345-2828 5.92e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 123.60  E-value: 5.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2345 KTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVP 2424
Cdd:PRK06710   24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2425 IDPEYPEDRISYMLEDSSAQVLLAQ---------------------RRLQERVSF-------------AGTVVTVDD-EQ 2469
Cdd:PRK06710  104 TNPLYTERELEYQLHDSGAKVILCLdlvfprvtnvqsatkiehvivTRIADFLPFpknllypfvqkkqSNLVVKVSEsET 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2470 AYAGDGSNLESAVG-------PNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFdascW 2542
Cdd:PRK06710  184 IHLWNSVEKEVNTGvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPF----F 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2543 EVF-QTLFFGATLYIPTKETIL---DYQWFERYMSDNGITTATLPPT-YAVYLNPDHMPDFK----RLIAAGSASSLELL 2613
Cdd:PRK06710  260 HVYgMTAVMNLSIMQGYKMVLIpkfDMKMVFEAIKKHKVTLFPGAPTiYIALLNSPLLKEYDissiRACISGSAPLPVEV 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2614 QQWKDKV---KYFNAYGPTEDSICTT---IWTpstedisqlKSVP--IGGPIVNHRIYIVDAHY-QPVPVGVAGELCIAG 2684
Cdd:PRK06710  340 QEKFETVtggKLVEGYGLTESSPVTHsnfLWE---------KRVPgsIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKG 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2685 VGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAI 2764
Cdd:PRK06710  411 PQIMKGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVV 483
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 2765 VIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK06710  484 TIGVPDPYRGETVKAFVVlkEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
7443-7923 7.11e-28

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 123.46  E-value: 7.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7443 AREQTIHGLFEEQAERMPEKAAVVFENTQ------LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAI 7516
Cdd:cd17634    50 ATLNLAANALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLAC 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7517 MKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLT-------------QRHLQECVSFDG----KVIAADDEQA-YGEDGS- 7577
Cdd:cd17634   130 ARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvragrsvplKKNVDDALNPNVtsveHVIVLKRTGSdIDWQEGr 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7578 -------------NLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMFAETLRITEEDRVVQFASLSF-DAS 7641
Cdd:cd17634   210 dlwwrdliakaspEHQPEaMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWvTGH 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7642 CWEIFKALFFGATLYI-------PAKDTILDYplfesyMNENGITAAILPPTYAIYLSPD--------RLPSLKKLITGG 7706
Cdd:cd17634   290 SYLLYGPLACGATTLLyegvpnwPTPARMWQV------VDKHGVNILYTAPTAIRALMAAgddaiegtDRSSLRILGSVG 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7707 SAASVEfVQQW------KDKVRYFNAYGPTEAS--IVTSVwaasPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAG 7778
Cdd:cd17634   364 EPINPE-AYEWywkkigKEKCPVVDTWWQTETGgfMITPL----PGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEG 438
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7779 ELCISGA--GLARGYLNRPEltaeKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLK 7856
Cdd:cd17634   439 NLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVA 514
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7857 IASVQETIVIARGDANGQQQLCAYFVADRELTVS-----ELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:cd17634   515 HPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpelyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK07529 PRK07529
AMP-binding domain protein; Validated
3854-4337 8.00e-28

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 123.91  E-value: 8.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3854 QTIHGLFEEQALRNPDAVAVVF--------EKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIM 3925
Cdd:PRK07529   25 ASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3926 KAGGAYiPIDPEYPEDRIRYMLEDSGAQALLT-------------------------------QRHLRERVSFAGTFVAV 3974
Cdd:PRK07529  105 AAGIAN-PINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvaevlaalpelrtvvevdlARYLPGPKRLAVPLIRR 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3975 DDEQAYH----------ADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDrvVQFASL 4044
Cdd:PRK07529  184 KAHARILdfdaelarqpGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGD--TVFCGL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4045 SF---DASCWEIFKALFFGATLYIPTS-----TTILD--YPLFESYmnenGITATILPPT-YAAYLnpdRMP-------S 4106
Cdd:PRK07529  262 PLfhvNALLVTGLAPLARGAHVVLATPqgyrgPGVIAnfWKIVERY----RINFLSGVPTvYAALL---QVPvdghdisS 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4107 LKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTSIwdeaSDSLGDRKSVPIGRPLANHRIYVV-----DSHNR 4179
Cdd:PRK07529  335 LRYALCGAAPLPVEVFRRFEAAtgVRIVEGYGLTEATCVSSV----NPPDGERRIGSVGLRLPYQRVRVVilddaGRYLR 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4180 MLPVGVAGELCISGVGLARGYLNrpeltAEKfvDNPFEPGERMYRTGDLVRWLPDGNLEYLGRidhqVK---IR-GYRIE 4255
Cdd:PRK07529  411 DCAVDEVGVLCIAGPNVFSGYLE-----AAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGR----AKdliIRgGHNID 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4256 LGEVETQLAKIDAVQEAIVLAREDANGQQQLVAY--FVAQRELTAAELRATMSQELPN-YMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK07529  480 PAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYvqLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKI 559

                  ....*
gi 386647928 4333 DRKAL 4337
Cdd:PRK07529  560 FKPAL 564
PRK07470 PRK07470
acyl-CoA synthetase; Validated
7456-7923 8.53e-28

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 122.46  E-value: 8.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLLTQR--------------HLQECVSFDGKVIAADDEQAYGED-GSNLEPV-VGPNHLAYVIYTSGTTG 7599
Cdd:PRK07470   97 AYLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHlGARVANAaVDHDDPCWFFFTSGTTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7600 KPKGVMVEHHglcslKLMFAETLRI-------TEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKDtiLDYPLFESY 7672
Cdd:PRK07470  177 RPKAAVLTHG-----QMAFVITNHLadlmpgtTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSER--FDPAEVWAL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 MNENGITAAILPPTYAIYL----SPDRL--PSLKKLITGGSAASVEFVQQWKDK-----VRYFNAYGPTEASIVTSVWAA 7741
Cdd:PRK07470  250 VERHRVTNLFTVPTILKMLvehpAVDRYdhSSLRYVIYAGAPMYRADQKRALAKlgkvlVQYFGLGEVTGNITVLPPALH 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7742 SP-DGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLA 7820
Cdd:PRK07470  330 DAeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RTGDLG 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7821 RWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVAdRE---LTVSELRGTLS 7897
Cdd:PRK07470  403 HLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA-RDgapVDEAELLAWLD 481
                         490       500
                  ....*....|....*....|....*.
gi 386647928 7898 QELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:PRK07470  482 GKVARYKLPKRFFFWDALPKSGYGKI 507
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
883-1153 8.71e-28

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 120.67  E-value: 8.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  883 LEGA-LDRNRLEEAFRALIARHETLRTgieMVGGEPMQRIYPEV---EFAVEHIR-ANEEEADAAVKQfIRA------FD 951
Cdd:cd19535    32 FDGEdLDPDRLERAWNKLIARHPMLRA---VFLDDGTQQILPEVpwyGITVHDLRgLSEEEAEAALEE-LRErlshrvLD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  952 LAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLY--GGEDLPALRIQYKDYaVWQQSEAQKEQLKRQE 1029
Cdd:cd19535   108 VERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYedPGEPLPPLELSFRDY-LLAEQALRETAYERAR 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1030 AYWLEvfR-------GELPVLEMPTDYARPAVQSyagnaLRFELDAQKREGLQRIASENGATLYMVLLAAYTILLQKYTG 1102
Cdd:cd19535   187 AYWQE--RlptlppaPQLPLAKDPEEIKEPRFTR-----REHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSG 259
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1103 QEDVVIGTPIAGRThgDLHP----LIGMFVNT--LAIRnyPAADKTFLSYLEDVKET 1153
Cdd:cd19535   260 QPRFLLNLTLFNRL--PLHPdvndVVGDFTSLllLEVD--GSEGQSFLERARRLQQQ 312
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
2336-2828 9.12e-28

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 122.69  E-value: 9.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2336 ATAADYEADKTIHQLFEEQAERIPDHPAVVFEGQQ--LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMF 2413
Cdd:PRK05852    7 AAPMASDFGPRIADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2414 AVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLL------AQRRLQERVSFAGTV-VTVDDEQAYAGDGSNLESAVGPN- 2485
Cdd:PRK05852   87 AASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidadgpHDRAEPTTRWWPLTVnVGGDSGPSGGTLSVHLDAATEPTp 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2486 ----------DLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVF-QTLFFGATL 2554
Cdd:PRK05852  167 atstpeglrpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALlATLASGGAV 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2555 YIPTKETILDYQWFERyMSDNGITTATLPPTYAVYL--NPDHMPDFK-----RLIAAGSAS-SLELLQQWKDK--VKYFN 2624
Cdd:PRK05852  247 LLPARGRFSAHTFWDD-IKAVGATWYTAVPTIHQILleRAATEPSGRkpaalRFIRSCSAPlTAETAQALQTEfaAPVVC 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2625 AYGPTEDS--ICTT--IWTPSTEDISQlkSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAE 2700
Cdd:PRK05852  326 AFGMTEAThqVTTTqiEGIGQTENPVV--STGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2701 KFVDNPFepgermyRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAY 2780
Cdd:PRK05852  404 NFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAV 476
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 2781 FV--ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK05852  477 IVprESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
5949-6415 9.45e-28

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 123.07  E-value: 9.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFED------KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPED 6022
Cdd:cd17634    67 GDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6023 RIRYMLEDSGAKLLLV------QGHLLDRASFADKLVNLN-------------------DDGA---YHEDGSNLEPVNGP 6074
Cdd:cd17634   147 AVAGRIIDSSSRLLITadggvrAGRSVPLKKNVDDALNPNvtsvehvivlkrtgsdidwQEGRdlwWRDLIAKASPEHQP 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6075 EHLT-----YVIYTSGTTGRPKGVMveHRNVVRLVKNTnyvelneqthilQTGAVVFDASTFEIWGALLNGGRL----YV 6145
Cdd:cd17634   227 EAMNaedplFILYTSGTTGKPKGVL--HTTGGYLVYAA------------TTMKYVFDYGPGDIYWCTADVGWVtghsYL 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6146 VRNETILDAVSLK--------------NAIQQYGINTMWLTAPLYNQLSQQDSGMFAG-----LKTLIVGGDVLSvPHIN 6206
Cdd:cd17634   293 LYGPLACGATTLLyegvpnwptparmwQVVDKHGVNILYTAPTAIRALMAAGDDAIEGtdrssLRILGSVGEPIN-PEAY 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6207 RVLREHAGLS---IVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGD--GVAR 6281
Cdd:cd17634   372 EWYWKKIGKEkcpVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTR 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6282 GYLNRPeltaEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VR 6360
Cdd:cd17634   452 TLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgIP 527
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6361 EDESGQKQLCaYFVAERELTIG-----ELRAALSQELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:cd17634   528 HAIKGQAPYA-YVVLNHGVEPSpelyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
7583-7928 9.47e-28

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 125.42  E-value: 9.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7583 VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVqfASLSFdascweiFKALFFGATLYIPAKDT 7662
Cdd:PRK08633  779 FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVIL--SSLPF-------FHSFGLTVTLWLPLLEG 849
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7663 I--------LDYPLFESYMNENGITAAILPPTY-AIYL-----SPDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNA 7726
Cdd:PRK08633  850 IkvvyhpdpTDALGIAKLVAKHRATILLGTPTFlRLYLrnkklHPLMFASLRLVVAGAEKLKPEVADAFEEKfgIRILEG 929
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7727 YGPTEASIVTSVwaASPDGLDLRSVP--------IGRPIANHQIFIVDSQN-HMLPVGVAGELCISGAGLARGYLNRPEL 7797
Cdd:PRK08633  930 YGATETSPVASV--NLPDVLAADFKRqtgskegsVGMPLPGVAVRIVDPETfEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7798 TAEKFVDnpfLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARG--DANGQQ 7875
Cdd:PRK08633 1008 TAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAvpDEKKGE 1084
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 7876 QLCAYFVADrELTVSELRGTLSQ-ELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK08633 1085 KLVVLHTCG-AEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK07788 PRK07788
acyl-CoA synthetase; Validated
2292-2830 1.06e-27

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 122.34  E-value: 1.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2292 ETIARMAKHLEQLLTAIAKAPEAPIAGLEMLTAAEQtqlhhvFNATAADYEAdktihqlfeeQAERIPDHPAVVFEGQQL 2371
Cdd:PRK07788   12 TRGSAEAHYLRVMIRSGAVDLERPDNGLRLAADIRR------YGPFAGLVAH----------AARRAPDRAALIDERGTL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2372 TYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRR 2451
Cdd:PRK07788   76 TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2452 LQERVSFA--------GTVVTVDDEQAYAGDGSNLESAVGPNDLA----------YIIYTSGTTGKPKGVMVEHhglcsl 2513
Cdd:PRK07788  156 FTDLLSALppdlgrlrAWGGNPDDDEPSGSTDETLDDLIAGSSTAplpkppkpggIVILTSGTTGTPKGAPRPE------ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2514 kqmfANTLQINAQ--DRV-------VQFASLSFDASCWEVFQ-TLFFGATLYIPTK---ETILdyqwfeRYMSDNGITTA 2580
Cdd:PRK07788  230 ----PSPLAPLAGllSRVpfragetTLLPAPMFHATGWAHLTlAMALGSTVVLRRRfdpEATL------EDIAKHKATAL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2581 TLPPTY---AVYLNPDHMPDF-----KRLIAAGSASSLELLQQWKD---KVKYfNAYGPTEDSICtTIWTPstEDISQLK 2649
Cdd:PRK07788  300 VVVPVMlsrILDLGPEVLAKYdtsslKIIFVSGSALSPELATRALEafgPVLY-NLYGSTEVAFA-TIATP--EDLAEAP 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2650 SVpIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDltaEKFVDNpfepgerMYRTGDLAKWLPDGTIE 2729
Cdd:PRK07788  376 GT-VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD---KQIIDG-------LLSSGDVGYFDEDGLLF 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2730 YLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGELSGELPGYMIPA 2807
Cdd:PRK07788  445 VDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVkaPGAALDEDAIKDYVRDNLARYKVPR 524
                         570       580
                  ....*....|....*....|...
gi 386647928 2808 HFVQLERMPLTPNGKIDRKALPA 2830
Cdd:PRK07788  525 DVVFLDELPRNPTGKVLKRELRE 547
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
4878-5394 1.08e-27

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 122.56  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4878 PAAPDAPENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAV 4957
Cdd:PRK06155   12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4958 WKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQER---AQQWGQTLQAALCLDDEAAYAEDAS------------ 5022
Cdd:PRK06155   92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAAleaADPGDLPLPAVWLLDAPASVSVPAGwstaplppldap 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5023 -NVANVnEPHDLAYVIYTSGTTGRPKGVMIEHRSL----VNTAAGY---RREYRLDQFPV-RLLQLASFSfdvfvgdiaR 5093
Cdd:PRK06155  172 aPAAAV-QPGDTAAILYTSGTTGPSKGVCCPHAQFywwgRNSAEDLeigADDVLYTTLPLfHTNALNAFF---------Q 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5094 TLYNGGTMVICPKddridparlhywiseekitiFESTpaliiPFMDYVAEHGL-------DMSSMVLLITSSDSCSVTDY 5166
Cdd:PRK06155  242 ALLAGATYVLEPR--------------------FSAS-----GFWPAVRRHGAtvtyllgAMVSILLSQPARESDRAHRV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5167 RV-------------LQERFGsqFRIINAYGVTEAaiDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLNPVPVGV 5233
Cdd:PRK06155  297 RValgpgvpaalhaaFRERFG--VDLLDGYGSTET--NFVIAVTHGSQRPGS----MGRLAPGFEARVVDEHDQELPDGE 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5234 LGELCIGG---IGVARGYLNRPELTEEKFVDSPFVEGERLYRTgdlarwmPDGNVDFIGRIDNQAKIRGYRIETGEIETQ 5310
Cdd:PRK06155  369 PGELLLRAdepFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQV 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5311 LLKAEGVREavvvvredakgqkvlCAHFTAESELKLSE------LRSSLSQE-----------LPGYMIPSYFVQLEQLP 5373
Cdd:PRK06155  442 LLSHPAVAA---------------AAVFPVPSELGEDEvmaavvLRDGTALEpvalvrhceprLAYFAVPRYVEFVAALP 506
                         570       580
                  ....*....|....*....|.
gi 386647928 5374 LTANGKIDRKALPAPDASMQT 5394
Cdd:PRK06155  507 KTENGKVQKFVLREQGVTADT 527
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
274-742 1.09e-27

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 121.64  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML 353
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  354 EDSGTQVLL-SQGHLQERVSFSG----TWIRLDDEeayhedgSNLESVNgpehltyviYTSGTTGKPKGNLTTHR----- 423
Cdd:cd12118    98 RHSEAKVLFvDREFEYEDLLAEGdpdfEWIPPADE-------WDPIALN---------YTSGTTGRPKGVVYHHRgayln 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  424 ---NII--RVVKNTNYidvtgqdkLLQLSSYSFDGSTFdIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVMFITT 498
Cdd:cd12118   162 alaNILewEMKQHPVY--------LWTLPMFHCNGWCF-PWTVAAVGGTNVCLRK---VDAKAIYDLIEKHKVTHFCGAP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  499 AFFNVLVDMNPDCLRHArailfgGERVSV--------SHVRKALGHLGpGKIKHVYGPTESTVFATS------YDVHEVE 564
Cdd:cd12118   230 TVLNMLANAPPSDARPL------PHRVHVmtagapppAAVLAKMEELG-FDVTHVYGLTETYGPATVcawkpeWDELPTE 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  565 EGAVSIPIGG--PISNTAIYIVNAQNkLQPI---GV-AGELCVAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDL 638
Cdd:cd12118   303 ERARLKARQGvrYVGLEEVDVLDPET-MKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAFRGG-------WFHSGDL 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  639 ARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVR-ESANGEKqLCAyYVA---DRSLPANEVRST 714
Cdd:cd12118   375 AVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpDEKWGEV-PCA-FVElkeGAKVTEEEIIAF 452
                         490       500
                  ....*....|....*....|....*...
gi 386647928  715 LSQELPAYMLPSYFVQLEqMPLTTNGKV 742
Cdd:cd12118   453 CREHLAGFMVPKTVVFGE-LPKTSTGKI 479
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1304-1790 1.10e-27

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 122.58  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1304 EKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 1383
Cdd:PRK07786   24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1384 DRIQFMLEDSAASVLLTQTHLQERA---QQWGQTLQAVL---------CLDDEAAYAEDASNVANVNEPHDL-AYVIYTS 1450
Cdd:PRK07786  104 PEIAFLVSDCGAHVVVTEAALAPVAtavRDIVPLLSTVVvaggssddsVLGYEDLLAEAGPAHAPVDIPNDSpALIMYTS 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1451 GTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ------FPVRLLQLASfsfdvfVGDIARTLYNGGTMVICPKdDRIDPAR 1524
Cdd:PRK07786  184 GTTGRPKGAVLTHANLTGQAMTCLRTNGADInsdvgfVGVPLFHIAG------IGSMLPGLLLGAPTVIYPL-GAFDPGQ 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1525 LHYWISEEKITIFESTPAliiPFMDYVAEHGLDMSSMELLITSSDSCSVTD--YRVLQERF-GSQfrIINAYGVTEAAID 1601
Cdd:PRK07786  257 LLDVLEAEKVTGIFLVPA---QWQAVCAEQQARPRDLALRVLSWGAAPASDtlLRQMAATFpEAQ--ILAAFGQTEMSPV 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1602 SSLYD--EPLAKLpeaGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFveger 1679
Cdd:PRK07786  332 TCMLLgeDAIRKL---GSV--GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF----- 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1680 lyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKV---LCAYFTAESELKL 1756
Cdd:PRK07786  402 --HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVpvaVAAVRNDDAALTL 479
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 1757 SELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:PRK07786  480 EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
3867-4332 1.18e-27

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 122.69  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3867 NPDAVAVVFEKSQ------LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPE 3940
Cdd:cd17634    66 NGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3941 DRIRYMLEDSGAQALLTQ---------------------------RHL----RERVSFAGTFVAVDDEQAYHADGS-NLE 3988
Cdd:cd17634   146 EAVAGRIIDSSSRLLITAdggvragrsvplkknvddalnpnvtsvEHVivlkRTGSDIDWQEGRDLWWRDLIAKASpEHQ 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3989 PV-VGPNHLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMFANTLQMTEQDRVVQFASLSF-DASCWEIFKALFFGATLYI 4065
Cdd:cd17634   226 PEaMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWvTGHSYLLYGPLACGATTLL 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4066 -------PTSTTILDYplfesyMNENGITATILPPTYAAYLNP---------DRmPSLKKLITGGSAASVEfVQQWKDKV 4129
Cdd:cd17634   306 yegvpnwPTPARMWQV------VDKHGVNILYTAPTAIRALMAagddaiegtDR-SSLRILGSVGEPINPE-AYEWYWKK 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4130 L------YFNAYGPTEAS--IVTSIwdeasDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGV--GLARG 4199
Cdd:cd17634   378 IgkekcpVVDTWWQTETGgfMITPL-----PGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRT 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4200 YLNRPEltaeKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLARED 4279
Cdd:cd17634   453 LFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPH 528
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 4280 ANGQQQLVAYFVAQRELT-----AAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:cd17634   529 AIKGQAPYAYVVLNHGVEpspelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7471-7928 1.33e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 120.64  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7471 QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEypedrirymledsgaqvlLTQ 7550
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG------------------MGR 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7551 RHLQECVS------FDGKVIAADDeqaygedgsnlepvvgpnhlAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRI 7624
Cdd:cd05910    64 KNLKQCLQeaepdaFIGIPKADEP--------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7625 TEEDRvvqfaslsfDASCWEIFkALF---FGATLYIPAKDTI----LDYPLFESYMNENGITAAILPPtyAIYLSPDR-- 7695
Cdd:cd05910   124 RPGEV---------DLATFPLF-ALFgpaLGLTSVIPDMDPTrparADPQKLVGAIRQYGVSIVFGSP--ALLERVARyc 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7696 ------LPSLKKLITGGSAASVEFVQQWK----DKVRYFNAYGPTEASIVTSV--------WAASPDGLdlRSVPIGRPI 7757
Cdd:cd05910   192 aqhgitLPSLRRVLSAGAPVPIALAARLRkmlsDEAEILTPYGATEALPVSSIgsrellatTTAATSGG--AGTCVGRPI 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7758 ANHQIFIVD---------SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPflAGERMYRTGDLARWLPDGNI 7828
Cdd:cd05910   270 PGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN--SEGFWHRMGDLGYLDDEGRL 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7829 EYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQ-LCAYFVADRELTVS----ELRGTLSQELPGY 7903
Cdd:cd05910   348 WFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPvLCVEPLPGTITPRArleqELRALAKDYPHTQ 427
                         490       500
                  ....*....|....*....|....*..
gi 386647928 7904 MIPSYFVQlEQMPLTP--NGKIDRNAL 7928
Cdd:cd05910   428 RIGRFLIH-PSFPVDIrhNAKIFREKL 453
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
4894-5380 1.36e-27

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 122.19  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4894 EKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 4973
Cdd:PRK07786   24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4974 DRIQFMLEDSAASVLLTQTHLQERA---QQWGQTLQAAL---------CLDDEAAYAEDASNVANVNEPHDL-AYVIYTS 5040
Cdd:PRK07786  104 PEIAFLVSDCGAHVVVTEAALAPVAtavRDIVPLLSTVVvaggssddsVLGYEDLLAEAGPAHAPVDIPNDSpALIMYTS 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5041 GTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ------FPVRLLQLASfsfdvfVGDIARTLYNGGTMVICPKdDRIDPAR 5114
Cdd:PRK07786  184 GTTGRPKGAVLTHANLTGQAMTCLRTNGADInsdvgfVGVPLFHIAG------IGSMLPGLLLGAPTVIYPL-GAFDPGQ 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5115 LHYWISEEKITIFESTPAliiPFMDYVAEHGLDMSSMVLLITSSDSCSVTD--YRVLQERF-GSQfrIINAYGVTEAAID 5191
Cdd:PRK07786  257 LLDVLEAEKVTGIFLVPA---QWQAVCAEQQARPRDLALRVLSWGAAPASDtlLRQMAATFpEAQ--ILAAFGQTEMSPV 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5192 SSLYD--EPLAKLpeaGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFveger 5269
Cdd:PRK07786  332 TCMLLgeDAIRKL---GSV--GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF----- 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5270 lyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKV---LCAHFTAESELKL 5346
Cdd:PRK07786  402 --HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVpvaVAAVRNDDAALTL 479
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 5347 SELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:PRK07786  480 EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
5945-6419 1.43e-27

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 121.96  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQ------LTYGELNERANRLARTLRNAGVQPDQmVGLMVERSLEMVVGMIAILKAGGAYVPIDPD 6018
Cdd:cd05931     3 AAARPDRPAYTFLDDEggreetLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6019 YPE---DRIRYMLEDSGAKLLLVQGHLLD-------RASFADKLVNLNDDgAYHEDGSNLEPVNGPEH--LTYVIYTSGT 6086
Cdd:cd05931    82 TPGrhaERLAAILADAGPRVVLTTAAALAavrafaaSRPAAGTPRLLVVD-LLPDTSAADWPPPSPDPddIAYLQYTSGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6087 TGRPKGVMVEHRNVVrlvknTNYVELNEQTHiLQTGAVVfdAStfeiW----------GALL----NGGRLY-------V 6145
Cdd:cd05931   161 TGTPKGVVVTHRNLL-----ANVRQIRRAYG-LDPGDVV--VS----WlplyhdmgliGGLLtplySGGPSVlmspaafL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6146 VRNETILDAVSlknaiqQYGINTMwlTAPlyN-------------QLSQQDSGmfaGLKTLIVGGDVLSVPHINRVLREH 6212
Cdd:cd05931   229 RRPLRWLRLIS------RYRATIS--AAP--NfaydlcvrrvrdeDLEGLDLS---SWRVALNGAEPVRPATLRRFAEAF 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6213 A--GL---SIVNGYGPTENTTFSTTH------TIVGEQKEA------------------VPIGKPINNSTAYIVDSK-LS 6262
Cdd:cd05931   296 ApfGFrpeAFRPSYGLAEATLFVSGGppgtgpVVLRVDRDAlagravavaaddpaarelVSCGRPLPDQEVRIVDPEtGR 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6263 LLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDLARwLPDGTLEYKGRIDEQVKIRG-----YRI 6337
Cdd:cd05931   376 ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGrnhypQDI 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6338 E--LGEIEEQLLK--VASVK------EATVIVREDESGQKQLcayfvAERELtIGELRAALSQElpnYMIPSH---FVPL 6404
Cdd:cd05931   455 EatAEEAHPALRPgcVAAFSvpddgeERLVVVAEVERGADPA-----DLAAI-AAAIRAAVARE---HGVAPAdvvLVRP 525
                         570
                  ....*....|....*
gi 386647928 6405 ERMPLTPNGKIDRRA 6419
Cdd:cd05931   526 GSIPRTSSGKIQRRA 540
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
5961-6567 1.64e-27

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 123.60  E-value: 1.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQG 6040
Cdd:PRK06060   31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 HLLDRasFADKLV----NLNDDGAYHEDgSNLEPVNGpEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNT--NYVELNE 6114
Cdd:PRK06060  111 ALRDR--FQPSRVaeaaELMSEAARVAP-GGYEPMGG-DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrKALRLTP 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6115 QTHILQTGAVVFDAST-FEIWGALLNGGRLYV----VRNETildAVSLKNAIQQ---YGINTMWltAPLYNQLSQqDSgm 6186
Cdd:PRK06060  187 EDTGLCSARMYFAYGLgNSVWFPLATGGSAVInsapVTPEA---AAILSARFGPsvlYGVPNFF--ARVIDSCSP-DS-- 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6187 FAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIvgEQKEAVPIGKPINNSTAYIVDSKLSLLPV 6266
Cdd:PRK06060  259 FRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRV--DEWRLGTLGRVLPPYEIRVVAPDGTTAGP 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6267 GVWGELIVGGDGVARGYLNRPEltaekfvesSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQL 6346
Cdd:PRK06060  337 GVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLI 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6347 LKVASVKEATVIVREDESGQKQLCAYFVAERELTIGE-----LRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL- 6420
Cdd:PRK06060  408 IEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALr 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6421 ---PA----------------------PQGNAPVGAEYVAPRTEQEKaLAAVWQ--------AVLG--AERVGVTD---- 6461
Cdd:PRK06060  488 kqsPTkpiwelsltepgsgvraqrddlSASNMTIAGGNDGGATLRER-LVALRQerqrlvvdAVCAeaAKMLGEPDpwsv 566
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6462 ----HFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTLAQLSQHIQPVARMID------QGEVTGEIGLTPIqrwf 6530
Cdd:PRK06060  567 dqdlAFSELGFDSQMTVTLCKRLAAVtGLRLPETVGWDYGSISGLAQYLEAELAGGHgrlksaGPVNSGATGLWAI---- 642
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 386647928 6531 fDQSLADLHHFNQAFMLHRKDRFDEaALRQVLQKLAE 6567
Cdd:PRK06060  643 -EEQLNKVEELVAVIADGEKQRVAD-RLRALLGTIAG 677
PRK07470 PRK07470
acyl-CoA synthetase; Validated
3864-4356 2.03e-27

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 121.30  E-value: 2.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRI 3943
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 RYMLEDSGAQALLTQR--------------HLRERVSFAGTFVA--VDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTG 4007
Cdd:PRK07470   97 AYLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGldYEALVARHLGARVANAAVDHDDPCWFFFTSGTTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4008 KPKGVMVEHHglcSLKLMFANTL-----QMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTtiLDYP----LFE 4078
Cdd:PRK07470  177 RPKAAVLTHG---QMAFVITNHLadlmpGTTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSER--FDPAevwaLVE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4079 SYMNENGITA-TILP-----PTYAAYlnpDRmPSLKKLITGGSA---ASVEFVQQWKDKVL--YFnayGPTEASIVTSIW 4147
Cdd:PRK07470  252 RHRVTNLFTVpTILKmlvehPAVDRY---DH-SSLRYVIYAGAPmyrADQKRALAKLGKVLvqYF---GLGEVTGNITVL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4148 DEASDSLGDRKSVPI---GRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermyR 4224
Cdd:PRK07470  325 PPALHDAEDGPDARIgtcGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------R 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4225 TGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAqRE---LTAAEL 4301
Cdd:PRK07470  398 TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA-RDgapVDEAEL 476
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 4302 RATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPApegSMHAGGEYVAPRTP 4356
Cdd:PRK07470  477 LAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE---ELEERGLLDLERAP 528
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
7451-7928 2.29e-27

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 121.70  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPE 7529
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7530 YPEDRIRYMLEDSGAQ-----------------------VLLT--------------------------QRHLQECVSFD 7560
Cdd:PRK08974  108 YTPRELEHQLNDSGAKaivivsnfahtlekvvfktpvkhVILTrmgdqlstakgtlvnfvvkyikrlvpKYHLPDAISFR 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7561 gKVIAADDEQAYgedgsnLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCS----LKLMFAETLRITEEdRVVQFASL 7636
Cdd:PRK08974  188 -SALHKGRRMQY------VKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqAKAAYGPLLHPGKE-LVVTALPL 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7637 sfdascWEIFkALFFGATLYIPAKDTIL------DYPLFESYMNENGITAAILPPTY--AIYLSPD----RLPSLKKLIT 7704
Cdd:PRK08974  260 ------YHIF-ALTVNCLLFIELGGQNLlitnprDIPGFVKELKKYPFTAITGVNTLfnALLNNEEfqelDFSSLKLSVG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7705 GGSAASVEFVQQWKD--KVRYFNAYGPTEASIVTsvwAASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCI 7782
Cdd:PRK08974  333 GGMAVQQAVAERWVKltGQYLLEGYGLTECSPLV---SVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWV 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7783 SGAGLARGYLNRPELTAEKFVDNpFLAgermyrTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQE 7862
Cdd:PRK08974  410 KGPQVMLGYWQRPEATDEVIKDG-WLA------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 7863 TIVIARGDANGQQQLCAYFVA-DRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK08974  483 VAAVGVPSEVSGEAVKIFVVKkDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK07788 PRK07788
acyl-CoA synthetase; Validated
3855-4339 2.29e-27

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 121.57  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3855 TIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPI 3934
Cdd:PRK07788   50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3935 DPEYPEDRIRYMLEDSGAQALLTQRHLRERVSFA--------GTFVAVDDEQAYHADGSNLEPVVG----------PNHL 3996
Cdd:PRK07788  130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALppdlgrlrAWGGNPDDDEPSGSTDETLDDLIAgsstaplpkpPKPG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3997 AYVIYTSGTTGKPKGVMVEH-HGLCSLKLMFANT-LQMTEqdrVVQFASLSFDA---SCWEIfkALFFGATLYIP----T 4067
Cdd:PRK07788  210 GIVILTSGTTGTPKGAPRPEpSPLAPLAGLLSRVpFRAGE---TTLLPAPMFHAtgwAHLTL--AMALGSTVVLRrrfdP 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4068 STTILDyplfesyMNENGITATILPPTY---------AAYLNPDrMPSLKKLITGGSAASVEFVQQWKD---KVLYfNAY 4135
Cdd:PRK07788  285 EATLED-------IAKHKATALVVVPVMlsrildlgpEVLAKYD-TSSLKIIFVSGSALSPELATRALEafgPVLY-NLY 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4136 GPTEASIVTsIWDEAsdslgDRKSVP--IGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPEltaEKFVD 4213
Cdd:PRK07788  356 GSTEVAFAT-IATPE-----DLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD---KQIID 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4214 NpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ 4293
Cdd:PRK07788  427 G-------LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA 499
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 4294 --RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:PRK07788  500 pgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
5961-6420 2.39e-27

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 119.55  E-value: 2.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQg 6040
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 hlldrasfADKLVNLNDDGAYHedgsnlepvngpehltyvIYTSGTTGRPKGVMVEHRNVVrlvkntNYVELNEQTHILQ 6120
Cdd:cd05973    80 --------AANRHKLDSDPFVM------------------MFTSGTTGLPKGVPVPLRALA------AFGAYLRDAVDLR 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6121 TGAVVFDAST--------FEIWGALLNGGRlyVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQL--SQQDSGMFAGL 6190
Cdd:cd05973   128 PEDSFWNAADpgwayglyYAITGPLALGHP--TILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLmaAGAEVPARPKG 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6191 KTLIV--GGDVLSvPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGV 6268
Cdd:cd05973   206 RLRRVssAGEPLT-PEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGE 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6269 WGELIVGGDGVA----RGYLNRPELTaekfvessflPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEE 6344
Cdd:cd05973   285 PGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6345 QLLKVASVKEATVIVREDESgQKQLCAYFVAERELTIG------ELRAALSQELPNYMIPS--HFVplERMPLTPNGKID 6416
Cdd:cd05973   355 ALIEHPAVAEAAVIGVPDPE-RTEVVKAFVVLRGGHEGtpaladELQLHVKKRLSAHAYPRtiHFV--DELPKTPSGKIQ 431

                  ....
gi 386647928 6417 RRAL 6420
Cdd:cd05973   432 RFLL 435
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
3878-4303 2.48e-27

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 120.16  E-value: 2.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3878 SQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLT 3957
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3958 QRHlrervsfagtfvavddeqayhadgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEH----HGLCSLKLMFantlQMT 4033
Cdd:cd17640    84 END--------------------------------SDDLATIIYTSGTTGNPKGVMLTHanllHQIRSLSDIV----PPQ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4034 EQDRVVQFASL--SFDASCwEIFKALFFGATLY--IPT-STTILDYP---------LFESYmnENGITATI--LPPT--- 4094
Cdd:cd17640   128 PGDRFLSILPIwhSYERSA-EYFIFACGCSQAYtsIRTlKDDLKRVKphyivsvprLWESL--YSGIQKQVskSSPIkqf 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4095 -YAAYLNPDRmpsLKKLITGGSAAS---VEFVQQWKDKVLyfNAYGPTEASIVTSIWDEASDSLGDrksvpIGRPLANHR 4170
Cdd:cd17640   205 lFLFFLSGGI---FKFGISGGGALPphvDTFFEAIGIEVL--NGYGLTETSPVVSARRLKCNVRGS-----VGRPLPGTE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4171 IYVVDSHNR-MLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRI-DHQVK 4248
Cdd:cd17640   275 IKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAkDTIVL 348
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 4249 IRGYRIELGEVETQLAKIDAVQEAIVLAREdangQQQLVAYFVAQRELTAAELRA 4303
Cdd:cd17640   349 SNGENVEPQPIEEALMRSPFIEQIMVVGQD----QKRLGALIVPNFEELEKWAKE 399
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
7451-7928 2.55e-27

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 121.15  E-value: 2.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVF--ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDP 7528
Cdd:PRK05852   21 LVEVAATRLPEAPALVVtaDRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7529 EYPEDRIRYMLEDSGAQVLL------------TQRHLQECVSfdgkvIAADDEQAYGEDGSNLEPVVGPNHL-------- 7588
Cdd:PRK05852  101 ALPIAEQRVRSQAAGARVVLidadgphdraepTTRWWPLTVN-----VGGDSGPSGGTLSVHLDAATEPTPAtstpeglr 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7589 ---AYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASL----SFDAScweIFKALFFGATLYIPAKD 7661
Cdd:PRK05852  176 pddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLyhghGLIAA---LLATLASGGAVLLPARG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7662 TILDYPLFESYMNENGITAAILPPTYAIYL-------SPDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEA 7732
Cdd:PRK05852  253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLeraatepSGRKPAALRFIRSCSAPLTAETAQALQTEfaAPVVCAFGMTEA 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7733 S-IVTSV---WAASPDGLDLRSVPIGRPIANhQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFl 7808
Cdd:PRK05852  333 ThQVTTTqieGIGQTENPVVSTGLVGRSTGA-QIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL- 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7809 agermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRE 7886
Cdd:PRK05852  411 ------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVprESAP 484
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928 7887 LTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK05852  485 PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
6527-6786 2.69e-27

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 119.38  E-value: 2.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6527 QR-WFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRkSENGyAAWNRaIGEGELYSLEVADFRD 6605
Cdd:cd19531     9 QRlWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFV-EVDG-EPVQV-ILPPLPLPLPVVDLSG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6606 VKSAEQAVEAKA---NEIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEEVRL 6681
Cdd:cd19531    86 LPEAEREAEAQRlarEEARRPFDLARGPLLRATLLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6682 PAktdsfrtWSEQLAAYA-------QSPAMENERAYW-EQIAQT-AVAPLPKDKQsdRSLQQDSE--SITIQWSRKETEQ 6750
Cdd:cd19531   166 PP-------LPIQYADYAvwqrewlQGEVLERQLAYWrEQLAGApPVLELPTDRP--RPAVQSFRgaRVRFTLPAELTAA 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 386647928 6751 lLKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLV 6786
Cdd:cd19531   237 -LRALARREGATLFMTLLAAFQVLLHRYSGQDDIVV 271
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
4886-5385 2.88e-27

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 120.94  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4886 NEAFHALFEKQAECTPEAAAVVYEN-----DRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKA 4960
Cdd:PRK08008    6 GQHLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4961 GGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTH---LQERAQQWGQTLQAALCLDDEAAYAED---------ASNVANVN 5028
Cdd:PRK08008   86 GAIMVPINARLLREESAWILQNSQASLLVTSAQfypMYRQIQQEDATPLRHICLTRVALPADDgvssftqlkAQQPATLC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5029 E-----PHDLAYVIYTSGTTGRPKGVMIEHRSLVntAAGYRREY--RLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTM 5101
Cdd:PRK08008  166 YapplsTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATF 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5102 VICPKDDridpARlHYW--ISEEKITIFESTPALI-----IPFMDYVAEHGL-DMssMVLLitssdSCSVTDYRVLQERF 5173
Cdd:PRK08008  244 VLLEKYS----AR-AFWgqVCKYRATITECIPMMIrtlmvQPPSANDRQHCLrEV--MFYL-----NLSDQEKDAFEERF 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5174 GsqFRIINAYGVTEAaIDSSLYDEPlaklPEAGNVP-IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGI---GVARGYL 5249
Cdd:PRK08008  312 G--VRLLTSYGMTET-IVGIIGDRP----GDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYY 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5250 NRPELTEEKFvdspfvEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK 5329
Cdd:PRK08008  385 LDPKATAKVL------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSI 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 5330 GQKVLCAH--FTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK08008  459 RDEAIKAFvvLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK07788 PRK07788
acyl-CoA synthetase; Validated
5945-6422 3.37e-27

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 120.80  E-value: 3.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK07788   59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHLLDRASFA-DKLVNLN-------------------DDGAYHEDGSNLEPVNGPEHLtyVIYTS 6084
Cdd:PRK07788  139 AEVAAREGVKALVYDDEFTDLLSALpPDLGRLRawggnpdddepsgstdetlDDLIAGSSTAPLPKPPKPGGI--VILTS 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6085 GTTGRPKGVMvehRNVVRlvkntnyvelneqthILQTGAVVFD-------------ASTFEIWGaLLNGGRLYVVRNETI 6151
Cdd:PRK07788  217 GTTGTPKGAP---RPEPS---------------PLAPLAGLLSrvpfragettllpAPMFHATG-WAHLTLAMALGSTVV 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6152 L----DAVSLKNAIQQYGINTMwLTAPLYNQ----LSQQDSGMF--AGLKTLIVGGDVLSVPHINRVLrEHAGLSIVNGY 6221
Cdd:PRK07788  278 LrrrfDPEATLEDIAKHKATAL-VVVPVMLSrildLGPEVLAKYdtSSLKIIFVSGSALSPELATRAL-EAFGPVLYNLY 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6222 GPTENtTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLN-RPELTAEKFVESsfl 6300
Cdd:PRK07788  356 GSTEV-AFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgRDKQIIDGLLSS--- 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6301 pgercyrtGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQKqLCAYFVAE--R 6377
Cdd:PRK07788  432 --------GDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgVDDEEFGQR-LRAFVVKApgA 502
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 6378 ELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPA 6422
Cdd:PRK07788  503 ALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
3999-4334 3.52e-27

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 116.98  E-value: 3.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3999 VIYTSGTTGKPKGVMVEHhglcslKLMFANT-------LQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTI 4071
Cdd:cd17635     6 VIFTSGTTGEPKAVLLAN------KTFFAVPdilqkegLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4072 LDyPLFESyMNENGITATILPPTYAAYLNPD------RMPSLKKLITGGS---AASVEFVQqWKDKVLYFNAYGPTEASI 4142
Cdd:cd17635    80 YK-SLFKI-LTTNAVTTTCLVPTLLSKLVSElksanaTVPSLRLIGYGGSraiAADVRFIE-ATGLTNTAQVYGLSETGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4143 VTSIwdEASDSLGDRKSVpiGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgerm 4222
Cdd:cd17635   157 ALCL--PTDDDSIEINAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV------ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4223 yRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELR 4302
Cdd:cd17635   227 -NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIR 305
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 386647928 4303 A---TMSQELPNYMIPSYFVQLAQMPLTPNGKIDR 4334
Cdd:cd17635   306 AlkhTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
8071-8315 4.14e-27

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 118.31  E-value: 4.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8071 DRFEAVFRQLIERHETLRTGFeMANG--EPVQRVYSDVEFAVEY-SKADREEAVEIAQRFVRP----FDLRKPPLLRVGL 8143
Cdd:cd19544    39 DAFLAALQQVIDRHDILRTAI-LWEGlsEPVQVVWRQAELPVEElTLDPGDDALAQLRARFDPrryrLDLRQAPLLRAHV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8144 IEVEP-ERHILMLDMHHIISDGASVGILQEEFSRLYAGE--ELPPLrIQYKDYAAWQRSEAyakRVKQQEGYWLQTLAGe 8220
Cdd:cd19544   118 AEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRaaALPPP-VPYRNFVAQARLGA---SQAEHEAFFREMLGD- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8221 lpvIELPT------DYERTSTRSfegAELEFEADEALTQRLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVA 8294
Cdd:cd19544   193 ---VDEPTapfgllDVQGDGSDI---TEARLALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLS 266
                         250       260
                  ....*....|....*....|...
gi 386647928 8295 GRTHA--DVEPIIGMFVNTLAIR 8315
Cdd:cd19544   267 GRMQGgaGADRALGMFINTLPLR 289
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
405-747 4.26e-27

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 123.50  E-value: 4.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 VIYTSGTTGKPKGNLTTHRNI------IRVVKNTNYIDVTgqdkllqLSS----YSFdGSTFDIFGALLNGAKLVLVPKE 474
Cdd:PRK08633  787 IIFSSGSEGEPKGVMLSHHNIlsnieqISDVFNLRNDDVI-------LSSlpffHSF-GLTVTLWLPLLEGIKVVYHPDP 858
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  475 TvlDVAKLAGLIEKQQISVMFITTAFFNVLV---DMNPDCLRHARAILFGGE----RVSVSHVRKaLGHlgpgKIKHVYG 547
Cdd:PRK08633  859 T--DALGIAKLVAKHRATILLGTPTFLRLYLrnkKLHPLMFASLRLVVAGAEklkpEVADAFEEK-FGI----RILEGYG 931
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  548 PTEST---------VFATSYDVHE-VEEGAVSIPIGGpisnTAIYIVNAQN-KLQPIGVAGELCVAGDGLARGYLNRPDL 616
Cdd:PRK08633  932 ATETSpvasvnlpdVLAADFKRQTgSKEGSVGMPLPG----VAVRIVDPETfEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  617 TAEKFADnpfAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKL---EAIEKATVVVRESANGE 693
Cdd:PRK08633 1008 TAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlggEEVVFAVTAVPDEKKGE 1084
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928  694 KqLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK08633 1085 K-LVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
7591-7923 4.62e-27

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 116.45  E-value: 4.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7591 VIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDR--VVQ--FASLSFDASCweiFKALFFGATLYIPAkdtILDY 7666
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRylIINpfFHTFGYKAGI---VACLLTGATVVPVA---VFDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7667 PLFESYMNENGITAAILPPTyaIYLS----PDR----LPSLKKLITGGSAASVEFVQQWKDKVRYFN---AYGPTEASIV 7735
Cdd:cd17638    79 DAILEAIERERITVLPGPPT--LFQSlldhPGRkkfdLSSLRAAVTGAATVPVELVRRMRSELGFETvltAYGLTEAGVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7736 TsvWAASPDGLDLRSVPIGRPIANHQIFIVDsqnhmlpvgvAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyR 7815
Cdd:cd17638   157 T--MCRPGDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWL------H 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7816 TGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSE--LR 7893
Cdd:cd17638   219 TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEedVI 298
                         330       340       350
                  ....*....|....*....|....*....|
gi 386647928 7894 GTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:cd17638   299 AWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK08315 PRK08315
AMP-binding domain protein; Validated
5933-6415 5.25e-27

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 120.69  E-value: 5.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5933 SDKTIHQLFEEQAERIPDHLAVTFEDKQL--TYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGG 6010
Cdd:PRK08315   14 LEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6011 AYVPIDPDYPEDRIRYMLEDSGAKLLLV------------------------QGHL-------------LDRASFA---- 6049
Cdd:PRK08315   94 ILVTINPAYRLSELEYALNQSGCKALIAadgfkdsdyvamlyelapelatcePGQLqsarlpelrrvifLGDEKHPgmln 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6050 -DKLVNL---NDDGAYHEDGSNL---EPVNgpehltyVIYTSGTTGRPKGVMVEHRNVV---RLV-KNTNYVE------- 6111
Cdd:PRK08315  174 fDELLALgraVDDAELAARQATLdpdDPIN-------IQYTSGTTGFPKGATLTHRNILnngYFIgEAMKLTEedrlcip 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6112 -------------LNEQTHilqtGA-VVFDASTFEiwgallnggrlyvvrNETILDAVSLKNAIQQYGINTMWLTaplyn 6177
Cdd:PRK08315  247 vplyhcfgmvlgnLACVTH----GAtMVYPGEGFD---------------PLATLAAVEEERCTALYGVPTMFIA----- 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6178 QLSQQDSGMF--AGLKTLIVGGDVLSVPHINRVLRE-H-AGLSIVngYGPTENTTFST-THTIVGEQKEAVPIGKPINNS 6252
Cdd:PRK08315  303 ELDHPDFARFdlSSLRTGIMAGSPCPIEVMKRVIDKmHmSEVTIA--YGMTETSPVSTqTRTDDPLEKRVTTVGRALPHL 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6253 TAYIVDSKLS-LLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVk 6331
Cdd:PRK08315  381 EVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWM------HTGDLAVMDEEGYVNIVGRIKDMI- 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6332 IRG----Y-RielgEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAALSQELPNYMIPSHFVPL 6404
Cdd:PRK08315  454 IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRpgATLTEEDVRDFCRGKIAHYKIPRYIRFV 529
                         570
                  ....*....|.
gi 386647928 6405 ERMPLTPNGKI 6415
Cdd:PRK08315  530 DEFPMTVTGKI 540
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
7473-7928 5.39e-27

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 120.26  E-value: 5.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7473 TYRELNERANRLARTLR-AEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQR 7551
Cdd:cd05928    43 SFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 HL--------QECVSFDGKVI-----------------AADDEQAYGEDGSNlEPVVgpnhlayVIYTSGTTGKPKgvMV 7606
Cdd:cd05928   123 ELapevdsvaSECPSLKTKLLvseksrdgwlnfkellnEASTEHHCVETGSQ-EPMA-------IYFTSGTTGSPK--MA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7607 EHhGLCSLKLMFAETLR----ITEEDRVVQFASLSF-DASCWEIFKALFFGATLYI---PAKDT--ILD----YPlfesy 7672
Cdd:cd05928   193 EH-SHSSLGLGLKVNGRywldLTASDIMWNTSDTGWiKSAWSSLFEPWIQGACVFVhhlPRFDPlvILKtlssYP----- 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 mnengITAAILPPT-YAIYLSPD----RLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEasivTSVWAASPDG 7745
Cdd:cd05928   267 -----ITTFCGAPTvYRMLVQQDlssyKFPSLQHCVTGGEPLNPEVLEKWKAQtgLDIYEGYGQTE----TGLICANFKG 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7746 LDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCIS-----GAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLA 7820
Cdd:cd05928   338 MKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAATIRGD-------FYLTGDRG 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7821 RWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV-------ADRELTVSELR 7893
Cdd:cd05928   411 IMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqflsHDPEQLTKELQ 490
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 7894 GTLSQELPGYMIPSY--FVQleQMPLTPNGKIDRNAL 7928
Cdd:cd05928   491 QHVKSVTAPYKYPRKveFVQ--ELPKTVTGKIQRNEL 525
PLN02574 PLN02574
4-coumarate--CoA ligase-like
5961-6420 5.39e-27

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 120.33  E-value: 5.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQ 6039
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6040 GHLLDRASFADKLVNLNDDGAYHEDGSN----------------LEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVRL 6103
Cdd:PLN02574  147 PENVEKLSPLGVPVIGVPENYDFDSKRIefpkfyelikedfdfvPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAM 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6104 VKntNYVELNEQTHILQTGAVVFDAS--TFEIWG------ALLNGGRLYVVRNEtiLDAVSLKNAIQQYGINTMWLTAPL 6175
Cdd:PLN02574  227 VE--LFVRFEASQYEYPGSDNVYLAAlpMFHIYGlslfvvGLLSLGSTIVVMRR--FDASDMVKVIDRFKVTHFPVVPPI 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6176 YNQLSQQDSGM----FAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINN 6251
Cdd:PLN02574  303 LMALTKKAKGVcgevLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPN 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6252 STAYIVD-SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQV 6330
Cdd:PLN02574  383 MQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYFDEDGYLYIVDRLKEII 456
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6331 KIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERE--LTIGELRAALSQELPNYMIPSHFVPLERMP 6408
Cdd:PLN02574  457 KYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGstLSQEAVINYVAKQVAPYKKVRKVVFVQSIP 536
                         490
                  ....*....|..
gi 386647928 6409 LTPNGKIDRRAL 6420
Cdd:PLN02574  537 KSPAGKILRREL 548
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
6254-6507 5.49e-27

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 115.23  E-value: 5.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6254 AYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLPGERcYRTGDLARWLPDGTLEYKGRIDEQVKIR 6333
Cdd:COG3433    31 LLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQ-ADDLRLLLRRGLGPGGGLERLVQQVVIR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6334 GYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNG 6413
Cdd:COG3433   110 AERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLAL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6414 KIDRRALPAPQGNA-PVGAEYVAPRTEQ---EKALAAVWQAVLG--AERVGVTDHFFELGGDSIKSIQVSSRLHQAGYKL 6487
Cdd:COG3433   190 KVVARAAPALAAAEaLLAAASPAPALETaltEEELRADVAELLGvdPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDV 269
                         250       260
                  ....*....|....*....|
gi 386647928 6488 EIRDLFKYPTLAQLSQHIQP 6507
Cdd:COG3433   270 SFADLAEHPTLAAWWALLAA 289
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3878-4337 5.80e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 118.72  E-value: 5.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3878 SQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQAllt 3957
Cdd:cd05910     1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDA--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3958 qrhlrervsFAGTFVAVDDeqayhadgsnlepvvgpnhlAYVIYTSGTTGKPKGVMVEHHglcslklMFANTLQMTEQDr 4037
Cdd:cd05910    78 ---------FIGIPKADEP--------------------AAILFTSGSTGTPKGVVYRHG-------TFAAQIDALRQL- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4038 vVQFASLSFDASCWEIFkALF---FGATLYIP----TSTTILDYPLFESYMNENGITATILPP----TYAAY--LNPDRM 4104
Cdd:cd05910   121 -YGIRPGEVDLATFPLF-ALFgpaLGLTSVIPdmdpTRPARADPQKLVGAIRQYGVSIVFGSPalleRVARYcaQHGITL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4105 PSLKKLITGGSAASVEFVQQWK----DKVLYFNAYGPTEASIVTSIwdEASDSLGDRKSVP-------IGRPLANHRIYV 4173
Cdd:cd05910   199 PSLRRVLSAGAPVPIALAARLRkmlsDEAEILTPYGATEALPVSSI--GSRELLATTTAATsggagtcVGRPIPGVRVRI 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4174 VD---------SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDnpfEPGERM-YRTGDLVRWLPDGNLEYLGRI 4243
Cdd:cd05910   277 IEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKID---DNSEGFwHRMGDLGYLDDEGRLWFCGRK 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4244 DHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAyfVAQRELTA-------AELRATMSQELPNYMIPS 4316
Cdd:cd05910   354 AHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLC--VEPLPGTItprarleQELRALAKDYPHTQRIGR 431
                         490       500
                  ....*....|....*....|...
gi 386647928 4317 YFVQlAQMPLTP--NGKIDRKAL 4337
Cdd:cd05910   432 FLIH-PSFPVDIrhNAKIFREKL 453
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
2340-2828 5.87e-27

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 120.31  E-value: 5.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2340 DYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQAlgvKTD-QP---VGLMLERSLEMVVGMFAV 2415
Cdd:PRK12492   19 DLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQ---HTDlVPgdrIAVQMPNVLQYPIAVFGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2416 LKAGGAYVPIDPEYPEDRISYMLEDSSAQVL----LAQRRLQERVSFAGT-------------------VVTVDDE---- 2468
Cdd:PRK12492   96 LRAGLIVVNTNPLYTAREMRHQFKDSGARALvylnMFGKLVQEVLPDTGIeylieakmgdllpaakgwlVNTVVDKvkkm 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2469 -------QAYA-------GDGSNLES-AVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCS-LKQMFANTLQINA------- 2525
Cdd:PRK12492  176 vpayhlpQAVPfkqalrqGRGLSLKPvPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAnMLQVRACLSQLGPdgqplmk 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2526 QDRVVQFASL------SFDASCWEVFQTlfFGATLYIPTKETILDY-----QW-FERYMSDNGITTATLpptyavylnpD 2593
Cdd:PRK12492  256 EGQEVMIAPLplyhiyAFTANCMCMMVS--GNHNVLITNPRDIPGFikelgKWrFSALLGLNTLFVALM----------D 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2594 HmPDFKRLI--------AAGSASSLELLQQWKDKV--KYFNAYGPTEDSICTTiwTPSTEDISQLKSVpiGGPIVNHRIY 2663
Cdd:PRK12492  324 H-PGFKDLDfsalkltnSGGTALVKATAERWEQLTgcTIVEGYGLTETSPVAS--TNPYGELARLGTV--GIPVPGTALK 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2664 IVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFvdnpfePGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGY 2743
Cdd:PRK12492  399 VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2744 RIELGEIEEQLL---KVASVqeAIVIAHDDASGQKqlCAYFVADR--TMTVGELRGELSGELPGYMIPAHFVQLERMPLT 2818
Cdd:PRK12492  473 NVYPNEIEDVVMahpKVANC--AAIGVPDERSGEA--VKLFVVARdpGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMT 548
                         570
                  ....*....|
gi 386647928 2819 PNGKIDRKAL 2828
Cdd:PRK12492  549 PVGKILRREL 558
PRK13382 PRK13382
bile acid CoA ligase;
3847-4340 5.90e-27

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 120.25  E-value: 5.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3847 AAEYQQEQTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMK 3926
Cdd:PRK13382   36 AAMRREGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3927 AGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLRERV--SFAGT-----FVAVDDEQAYH------ADGSNLEPVVGP 3993
Cdd:PRK13382  116 IGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVdrALADCpqatrIVAWTDEDHDLtvevliAAHAGQRPEPTG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3994 NHLAYVIYTSGTTGKPKGVM-VEHHGLCSLKLMFANTLQMTEQDRVVqfASLSFDAscWEiFKALFFGATLyiptSTTIL 4072
Cdd:PRK13382  196 RKGRVILLTSGTTGTPKGARrSGPGGIGTLKAILDRTPWRAEEPTVI--VAPMFHA--WG-FSQLVLAASL----ACTIV 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4073 DYPLFE-----SYMNENGITATILPPTY--------AAYLNPDRMPSLKKLITGGSAASVEFVQQWKDK---VLYfNAYG 4136
Cdd:PRK13382  267 TRRRFDpeatlDLIDRHRATGLAVVPVMfdrimdlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQfgdVIY-NNYN 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4137 PTEASIVTSIWDEasdslgDRKSVP--IGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYlnrpelTAEKfvDN 4214
Cdd:PRK13382  346 ATEAGMIATATPA------DLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------TSGS--TK 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4215 PFEPGerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQR 4294
Cdd:PRK13382  412 DFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 4295 ELTAA--ELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAP 4340
Cdd:PRK13382  490 GASATpeTLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
3859-4437 6.10e-27

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 122.12  E-value: 6.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY 3938
Cdd:COG3319     6 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 PEDRIRYMLEDSGAQALLTQ-----RHLRERVSFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVM 4013
Cdd:COG3319    86 LALAAAAAALLLAALALLLAllaalALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4014 VEHHGLCSLKLMFANTLQMTEQDRVVQFAS-LSFDASCWEIFKALFFGATLYIPTSTTILDYPLFESYMNENGITATILP 4092
Cdd:COG3319   166 LVLAALLALLLAALLALALALAALLLLALAaALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4093 PTYAAYLNPDRMPSLKKLITGGSAASVEFVQQWKDKVL-----YFNAYGPTEASIVTSIWDEASDSLGDRKSVPIGRPLA 4167
Cdd:COG3319   246 ALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLaaaaaLAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4168 NHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQV 4247
Cdd:COG3319   326 VLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQR 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4248 KIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLT 4327
Cdd:COG3319   406 LRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLL 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4328 PNGKIDRKALPAPEGSmHAGGEYVAPRTPTEAKLAHIWQDVLGLEKVGVKDNFFELGGHSLRATALASKVRKELNMELPL 4407
Cdd:COG3319   486 LLLAALLLAAAAPAAA-AAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLL 564
                         570       580       590
                  ....*....|....*....|....*....|
gi 386647928 4408 RHIFQFPTVEQLAEAIGQLEQQEFDAIPVV 4437
Cdd:COG3319   565 LALLLAPTLAALAAALAAAAAAAALSPLVP 594
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
5491-5902 7.20e-27

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 117.40  E-value: 7.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5491 YPVSSAQKRLYIL--HQlegaEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGF-ELVNGEPVQRVYKEVNFAV 5567
Cdd:cd19545     2 YPCTPLQEGLMALtaRQ----PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPISW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5568 EhYRTSEAEAGEVVRGfvRTFDLaKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGESLAPlRIQY 5647
Cdd:cd19545    78 T-ESTSLDEYLEEDRA--APMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5648 KDYATWqqseAQQEQMKRQEAYWLDMFRGELPVL--ELPT--DYPRP-AVRKFEGSLLQRqlepklgeglqriaAESGAT 5722
Cdd:cd19545   153 SRFVKY----LRQLDDEAAAEFWRSYLAGLDPAVfpPLPSsrYQPRPdATLEHSISLPSS--------------ASSGVT 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5723 LYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTH--SDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKE---TMLgaye 5797
Cdd:cd19545   215 LATVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKdllDMI---- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5798 hqsyPFE--------ELVEKAQPARDlsrnplFDTLFALQNK---ETGELQLDGLR--LTPYPAEHTVAkfdLSVDVTEG 5864
Cdd:cd19545   291 ----PFEhtglqnirRLGPDARAACN------FQTLLVVQPAlpsSTSESLELGIEeeSEDLEDFSSYG---LTLECQLS 357
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 386647928 5865 SEGLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19545   358 GSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
279-744 9.45e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 118.31  E-value: 9.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  279 VTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGT 358
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  359 QVLLsqghlqervsfsgtwirlddeeayhedgsnlesVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIirvVKNTNYIDVT 438
Cdd:cd05914    81 KAIF---------------------------------VSDEDDVALINYTSGTTGNSKGVMLTYRNI---VSNVDGVKEV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  439 G----QDKLLQLSSYSFD-GSTFDIFGALLNGAKLVLVPKETvldvAKLAGLIEKQQISVMFITTAFFNVL--------- 504
Cdd:cd05914   125 VllgkGDKILSILPLHHIyPLTFTLLLPLLNGAHVVFLDKIP----SAKIIALAFAQVTPTLGVPVPLVIEkifkmdiip 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  505 ------------VDMNPDCLRHA--RAIL--FGGE-RVSVS-------HVRKALGHLGpGKIKHVYGPTESTVFATSYDV 560
Cdd:cd05914   201 kltlkkfkfklaKKINNRKIRKLafKKVHeaFGGNiKEFVIggakinpDVEEFLRTIG-FPYTIGYGMTETAPIISYSPP 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  561 HEVEEGAVSIPIggPISNTAIYivnaqnKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLAR 640
Cdd:cd05914   280 NRIRLGSAGKVI--DGVEVRID------SPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGK 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  641 WLPDGTIEYVGRIDDQ-VKIRGFRIELGEIEAHLLKLEAIEKATVVVREsanGEKQLCAYYVADR------SLPAN---- 709
Cdd:cd05914   346 IDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQE---KKLVALAYIDPDFldvkalKQRNIidai 422
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 386647928  710 --EVRSTLSQELPAYMLPSYF-VQLEQMPLTTNGKVDR 744
Cdd:cd05914   423 kwEVRDKVNQKVPNYKKISKVkIVKEEFEKTPKGKIKR 460
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
253-744 1.65e-26

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 119.11  E-value: 1.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  253 GTDYP-RDTTIHRLFEEQAERRPDAVAVTF--EDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMG 329
Cdd:PRK12583   10 GGDKPlLTQTIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  330 ILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLL------------------------SQGHLQ-ERVSFSGTWIRLDDEE 384
Cdd:PRK12583   90 TARIGAILVNINPAYRASELEYALGQSGVRWVIcadafktsdyhamlqellpglaegQPGALAcERLPELRGVVSLAPAP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  385 -----AYHEDGSNLESVNG-----------PEHLTYVIYTSGTTGKPKGNLTTHRNIIrvvkNTNYI-----DVTGQDKL 443
Cdd:PRK12583  170 ppgflAWHELQARGETVSRealaerqasldRDDPINIQYTSGTTGFPKGATLSHHNIL----NNGYFvaeslGLTEHDRL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  444 -LQLSSYSFDGSTFDIFGALLNGAKLVLvPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVdmNPDC----LRHARAI 518
Cdd:PRK12583  246 cVPVPLYHCFGMVLANLGCMTVGACLVY-PNEAFDPLATLQAVEEERCTALYGVPTMFIAELD--HPQRgnfdLSSLRTG 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  519 LFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAVSiPIGGPISNTAIYIVNAQNKLQPIGVAGE 598
Cdd:PRK12583  323 IMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVE-TVGRTQPHLEVKVVDPDGATVPRGEIGE 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  599 LCVAGDGLARGYLNRPDLTAEKFADNPFapgerMYrTGDLARWLPDGTIEYVGRIDDQVkIRGFR-IELGEIEAHLLKLE 677
Cdd:PRK12583  402 LCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHP 474
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  678 AIEKATVV-VRESANGEkQLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDR 744
Cdd:PRK12583  475 AVADVQVFgVPDEKYGE-EIVAWVRlhPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
2350-2828 1.98e-26

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 118.62  E-value: 1.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2350 LFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQ-ALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPE 2428
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2429 YPEDRISYMLEDSSAQVLLAqrrlqerVS-FAGTVVTVDDE-------------QAYAGDGS----------------NL 2478
Cdd:PRK08974  108 YTPRELEHQLNDSGAKAIVI-------VSnFAHTLEKVVFKtpvkhviltrmgdQLSTAKGTlvnfvvkyikrlvpkyHL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2479 ESAVG-------------------PNDLAYIIYTSGTTGKPKGVMVEHhglcslKQMFANTLQINA---------QDRVV 2530
Cdd:PRK08974  181 PDAISfrsalhkgrrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTH------RNMLANLEQAKAaygpllhpgKELVV 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2531 QFASLsfdascWEVFqTLFFGATLYIPTKETIL------DYQWFERYMSDNGITTATLPPTY--AVYLNPD-HMPDFKRL 2601
Cdd:PRK08974  255 TALPL------YHIF-ALTVNCLLFIELGGQNLlitnprDIPGFVKELKKYPFTAITGVNTLfnALLNNEEfQELDFSSL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2602 ---IAAGSASSLELLQQWKD--KVKYFNAYGPTEdsiCTTIWTPSTEDISQlKSVPIGGPIVNHRIYIVDAHYQPVPVGV 2676
Cdd:PRK08974  328 klsVGGGMAVQQAVAERWVKltGQYLLEGYGLTE---CSPLVSVNPYDLDY-YSGSIGLPVPSTEIKLVDDDGNEVPPGE 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2677 AGELCIAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLK 2756
Cdd:PRK08974  404 PGELWVKGPQVMLGYWQRPEATDEVIKDG-------WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 2757 VASVQE--AIVIAHdDASGqkQLCAYFVA--DRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK08974  477 HPKVLEvaAVGVPS-EVSG--EAVKIFVVkkDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK07514 PRK07514
malonyl-CoA synthase; Validated
273-747 2.05e-26

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 118.05  E-value: 2.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  273 RPDAVAVTFED-RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRY 351
Cdd:PRK07514   15 DRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  352 MLEDSGTQVLLSQGHLQErvsfsgtWIR-------------LDD-------EEAYHEDGSNLESVNGPEHLTYVIYTSGT 411
Cdd:PRK07514   95 FIGDAEPALVVCDPANFA-------WLSkiaaaagaphvetLDAdgtgsllEAAAAAPDDFETVPRGADDLAAILYTSGT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  412 TGKPKGNLTTHRNII---RVVKntNYIDVTGQDKLLQ-LSSYSFDGSTFDIFGALLNGAKLVLVPKetvLDVAKLAGLIE 487
Cdd:PRK07514  168 TGRSKGAMLSHGNLLsnaLTLV--DYWRFTPDDVLIHaLPIFHTHGLFVATNVALLAGASMIFLPK---FDPDAVLALMP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  488 kqQISVMFITTAFFNVLVD---MNPDCLRHARaiLFggerVSVS-------HV--RKALGHlgpgKIKHVYGPTEsTVFA 555
Cdd:PRK07514  243 --RATVMMGVPTFYTRLLQeprLTREAAAHMR--LF----ISGSapllaetHRefQERTGH----AILERYGMTE-TNMN 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  556 TS--YDvHEVEEGAVSIPIGGpisnTAIYIVN-AQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgerm 632
Cdd:PRK07514  310 TSnpYD-GERRAGTVGFPLPG----VSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------ 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  633 YRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAiekatvvVRESAN--------GEkQLCAYYVADR 704
Cdd:PRK07514  379 FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPG-------VVESAVigvphpdfGE-GVTAVVVPKP 450
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 386647928  705 --SLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK07514  451 gaALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
5937-6420 3.02e-26

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 117.68  E-value: 3.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5937 IHQLFEEQAERIPDHLAVTFEDKQ--LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVP 6014
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6015 IDPDYPEDRIRYMLEDSGAKLLLVQG-----HLLDRASFADKLVNLNDDGAYHED------GSNLEP---VNGPEHL--- 6077
Cdd:PRK05852   98 LDPALPIAEQRVRSQAAGARVVLIDAdgphdRAEPTTRWWPLTVNVGGDSGPSGGtlsvhlDAATEPtpaTSTPEGLrpd 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6078 -TYVIYTSGTTGRPKGVMVEHRNVVRLVKN--TNYvELNEQTHILQT-------GAVVFDASTFEIWGALL--NGGRLYV 6145
Cdd:PRK05852  178 dAMIMFTGGTTGLPKMVPWTHANIASSVRAiiTGY-RLSPRDATVAVmplyhghGLIAALLATLASGGAVLlpARGRFSA 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6146 vrnETILDAVSLKNAiqqygintMWLTA-PLYNQL-----SQQDSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVN 6219
Cdd:PRK05852  257 ---HTFWDDIKAVGA--------TWYTAvPTIHQIlleraATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVC 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6220 GYGPTENTTFSTTHTIVGEQKEAVPIGK--PINNSTA---YIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKF 6294
Cdd:PRK05852  326 AFGMTEATHQVTTTQIEGIGQTENPVVStgLVGRSTGaqiRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6295 VESSFlpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFV 6374
Cdd:PRK05852  406 TDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 6375 --AERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK05852  479 prESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK06164 PRK06164
acyl-CoA synthetase; Validated
2346-2828 3.83e-26

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 117.54  E-value: 3.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI 2425
Cdd:PRK06164   11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2426 DPEYPEDRISYMLEDSSAQVLLAQRRLQeRVSFAGTVVTVDDE-----QAYA---GDGSNL------------------- 2478
Cdd:PRK06164   91 NTRYRSHEVAHILGRGRARWLVVWPGFK-GIDFAAILAAVPPDalpplRAIAvvdDAADATpapapgarvqlfalpdpap 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2479 -----ESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLS--FDAScwEVFQTLFFG 2551
Cdd:PRK06164  170 paaagERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCgvFGFS--TLLGALAGG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2552 ATLYIptkETILDYQWFERYMSDNGITTatlppTYA-------VYLNPDHMPDFKRL----IAAGSASSLELLQQWKDK- 2619
Cdd:PRK06164  248 APLVC---EPVFDAARTARALRRHRVTH-----TFGndemlrrILDTAGERADFPSArlfgFASFAPALGELAALARARg 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2620 VKYFNAYGPTEDSICTTIWtPSTEDISqLKSVPIGGPIVNH-RIYIVDAHYQPV-PVGVAGELCIAGVGLARGYLNRPDL 2697
Cdd:PRK06164  320 VPLTGLYGSSEVQALVALQ-PATDPVS-VRIEGGGRPASPEaRVRARDPQDGALlPDGESGEIEIRAPSLMRGYLDNPDA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2698 TAEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDdaSGQKQL 2777
Cdd:PRK06164  398 TARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT--RDGKTV 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 2778 CAYFV-------ADRTMTVGELRGELSgelpGYMIPAHFVQLERMPLT--PNG-KIDRKAL 2828
Cdd:PRK06164  470 PVAFViptdgasPDEAGLMAACREALA----GFKVPARVQVVEAFPVTesANGaKIQKHRL 526
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
3870-4332 5.31e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 116.54  E-value: 5.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3870 AVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLED 3949
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3950 SGAQAL---------------LTQRHLRERVSFAGtfvAVDDEQAYHADGSNLEPVVGPNHLA--YVIYTSGTTGKPKGV 4012
Cdd:PRK08276   82 SGAKVLivsaaladtaaelaaELPAGVPLLLVVAG---PVPGFRSYEEALAAQPDTPIADETAgaDMLYSSGTTGRPKGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4013 MVEHHGL----CSLKLMFANTLQMTEQDRVVQF--------ASLSFDAScweifkALFFGATLYI-----PTSTtiLDyp 4075
Cdd:PRK08276  159 KRPLPGLdpdeAPGMMLALLGFGMYGGPDSVYLspaplyhtAPLRFGMS------ALALGGTVVVmekfdAEEA--LA-- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4076 LFESYMnengITATILPPT-YAAYLN-PDR------MPSLKKLITGGSAASVEFVQQ---WKDKVLYfNAYGPTEASIVT 4144
Cdd:PRK08276  229 LIERYR----VTHSQLVPTmFVRMLKlPEEvrarydVSSLRVAIHAAAPCPVEVKRAmidWWGPIIH-EYYASSEGGGVT 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4145 SIwdEASDSLGDRKSVpiGRPLANhRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDnpfepgERMYR 4224
Cdd:PRK08276  304 VI--TSEDWLAHPGSV--GKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNP------HGWVT 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4225 TGDlVRWL-PDGNLeYL-GRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN-GQQ-----QLVAYFVAQREL 4296
Cdd:PRK08276  373 VGD-VGYLdEDGYL-YLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEmGERvkavvQPADGADAGDAL 450
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 4297 tAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK08276  451 -AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
7452-7906 5.46e-26

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 117.67  E-value: 5.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7452 FEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGA--------- 7522
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVvallntqqr 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7523 --------------YVPIDPEYPEdriryMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPV----VG 7584
Cdd:PRK08279  123 gavlahslnlvdakHLIVGEELVE-----AFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPAsrsgVT 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7585 PNHLAYVIYTSGTTGKPKGVMVEHH-GLCSLKlMFAETLRITEEDR-------------VVQFASL-----------SFD 7639
Cdd:PRK08279  198 AKDTAFYIYTSGTTGLPKAAVMSHMrWLKAMG-GFGGLLRLTPDDVlycclplyhntggTVAWSSVlaagatlalrrKFS 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7640 ASC-WEIFKAlfFGATL--YI----------PAKDTILDYPLfeSYMNENGITAAILPptyaiylspdrlpslkklitgg 7706
Cdd:PRK08279  277 ASRfWDDVRR--YRATAfqYIgelcryllnqPPKPTDRDHRL--RLMIGNGLRPDIWD---------------------- 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7707 saasvEFVQQWKDKvRYFNAYGPTEASIVTSvwaaSPDGLDlRSVPIGRPIANHQIFIV-----------DSQNHMLPVG 7775
Cdd:PRK08279  331 -----EFQQRFGIP-RILEFYAASEGNVGFI----NVFNFD-GTVGRVPLWLAHPYAIVkydvdtgepvrDADGRCIKVK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7776 V--AGELC--ISGAGLARGYlNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIE 7851
Cdd:PRK08279  400 PgeVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVE 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7852 EQLLKIASVQETIV--IARGDANGQQQLCAYFVAD-RELTVSELRGTLSQELPGYMIP 7906
Cdd:PRK08279  479 NALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADgAEFDLAALAAHLYERLPAYAVP 536
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
3995-4334 5.57e-26

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 112.88  E-value: 5.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3995 HLAYVIYTSGTTGKPKGVMVEHHG-----LCSLKLMfantlQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSt 4069
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSwiesfVCNEDLF-----NISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4070 tiLDYPLFESYMNENGITATILPPTY-AAYLNPDRMPSLKKLITGGSAASVE-----FVQQWKDKVLYfNAYGPTEASIV 4143
Cdd:cd17633    75 --FNPKSWIRKINQYNATVIYLVPTMlQALARTLEPESKIKSIFSSGQKLFEstkkkLKNIFPKANLI-EFYGTSELSFI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4144 TSIWDEASdslgdRKSVPIGRPLANHRIYVVDSHNrmlpvGVAGELCISGVGLARGYLNRPELTAEKFvdnpfepgermY 4223
Cdd:cd17633   152 TYNFNQES-----RPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------M 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4224 RTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQrELTAAELRA 4303
Cdd:cd17633   211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKR 289
                         330       340       350
                  ....*....|....*....|....*....|.
gi 386647928 4304 TMSQELPNYMIPSYFVQLAQMPLTPNGKIDR 4334
Cdd:cd17633   290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
262-749 6.73e-26

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 117.59  E-value: 6.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  262 IHRLFEEQAERRPDAVAVTFED-----RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGA 336
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  337 YVPIDPEYPEERIRYMLEDSGTQVLLSQG--------------------------------HLQERVSFS-GTWIRLDDE 383
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevnlkeeadkacaqcptvekvvvvrHLGNDFTPAkGRDLSYDEE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  384 EAYHEDGSnleSVNGPEHLTYVIYTSGTTGKPKGNLTTHRNI-IRVVKNTNY-IDVTGQDKLLQLSSYSFDGSTFDIFGA 461
Cdd:cd05968   223 KETAGDGA---ERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFqFDLKPGDLLTWFTDLGWMMGPWLIFGG 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  462 LLNGAKLVL---VPKETVLDvaKLAGLIEKQQISVMFITTAFFNVLV-----DMNPDCLRHARAILFGGERVSVSHVRKA 533
Cdd:cd05968   300 LILGATMVLydgAPDHPKAD--RLWRMVEDHEITHLGLSPTLIRALKprgdaPVNAHDLSSLRVLGSTGEPWNPEPWNWL 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  534 LGHLGPGK--IKHVYGPTE-STVFATSYDVHEVEEGAVSipigGPISNTAIYIVNAQNklQPI-GVAGELCVAGD--GLA 607
Cdd:cd05968   378 FETVGKGRnpIINYSGGTEiSGGILGNVLIKPIKPSSFN----GPVPGMKADVLDESG--KPArPEVGELVLLAPwpGMT 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  608 RGYLNRPDltaeKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEA-IEKATVVV 686
Cdd:cd05968   452 RGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAvLESAAIGV 527
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  687 RESANGEKQLCAYYVADRSLP----ANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPA 749
Cdd:cd05968   528 PHPVKGEAIVCFVVLKPGVTPtealAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1305-1795 7.00e-26

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 115.27  E-value: 7.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1305 KQAERTPEVaavvyendRLTYRELNERANRLARMLRAQGV-KPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPdyps 1383
Cdd:cd05958     1 RTCLRSPER--------EWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1384 driqfMLEDsaasvlltqthlQERAQQWGQTLQAVLCLDDEAAYAEDASNVAnvnephdlayviYTSGTTGRPKGVMIEH 1463
Cdd:cd05958    69 -----LLRP------------KELAYILDKARITVALCAHALTASDDICILA------------FTSGTTGAPKATMHFH 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1464 RSLVNTAAGYRREY---RLDQFPVRLLQLAsFSFDvFVGDIARTLYNGGTMVICPKDdriDPARLHYWISEEKITIFEST 1540
Cdd:cd05958   120 RDPLASADRYAVNVlrlREDDRFVGSPPLA-FTFG-LGGVLLFPFGVGASGVLLEEA---TPDLLLSAIARYKPTVLFTA 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1541 PALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAaidsslYDEPLAKLPEAGNV-P 1619
Cdd:cd05958   195 PTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP--IIDGIGSTEM------FHIFISARPGDARPgA 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1620 IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGylnrpeLTEEKFVDspFVEGERLYrTGDLARWMPDGNVDFIG 1699
Cdd:cd05958   267 TGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRY------LADKRQRT--YVQGGWNI-TGDTYSRDPDGYFRHQG 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1700 RIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYF-----TAESELKLSELRSSLSQELPGYMIPS 1774
Cdd:cd05958   338 RSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVvlrpgVIPGPVLARELQDHAKAHIAPYKYPR 417
                         490       500
                  ....*....|....*....|.
gi 386647928 1775 YFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05958   418 AIEFVTELPRTATGKLQRFAL 438
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
265-747 8.02e-26

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 116.69  E-value: 8.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  265 LFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPE 343
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  344 YPEERIRYMLEDSGTQ--VLLSQ-GHLQERVSFSgTWI------RLDDE------------------------------- 383
Cdd:PRK08974  108 YTPRELEHQLNDSGAKaiVIVSNfAHTLEKVVFK-TPVkhviltRMGDQlstakgtlvnfvvkyikrlvpkyhlpdaisf 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  384 -EAYHEdGSNLESVN---GPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVK--NTNYIDVTGQDKLLQLSSYSFdgstFD 457
Cdd:PRK08974  187 rSALHK-GRRMQYVKpelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqaKAAYGPLLHPGKELVVTALPL----YH 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  458 IFGALLN-------GAKLVLV--PKetvlDVAKLAGLIEKQQISVMFITTAFFNVLVDmNPDclrhARAILFGGERVSVS 528
Cdd:PRK08974  262 IFALTVNcllfielGGQNLLItnPR----DIPGFVKELKKYPFTAITGVNTLFNALLN-NEE----FQELDFSSLKLSVG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  529 ---HVRKALG---------HLGPGkikhvYGPTEST--VFATSYDVHEvEEGAvsipIGGPISNTAIYIVNAQNKLQPIG 594
Cdd:PRK08974  333 ggmAVQQAVAerwvkltgqYLLEG-----YGLTECSplVSVNPYDLDY-YSGS----IGLPVPSTEIKLVDDDGNEVPPG 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  595 VAGELCVAGDGLARGYLNRPDLTAEKFADNPFApgermyrTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIE-AHL 673
Cdd:PRK08974  403 EPGELWVKGPQVMLGYWQRPEATDEVIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEdVVM 475
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928  674 LKLEAIEKATVVVRESANGEKqLCAYYVA-DRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK08974  476 LHPKVLEVAAVGVPSEVSGEA-VKIFVVKkDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK07788 PRK07788
acyl-CoA synthetase; Validated
7438-7930 8.25e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 116.57  E-value: 8.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7438 TAAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIM 7517
Cdd:PRK07788   41 LAADIRRYGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7518 KAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLtqrHLQEcvsFDGKVIAADDE----QAYGEDGSNLEPVVG--------- 7584
Cdd:PRK07788  121 KVGARIILLNTGFSGPQLAEVAAREGVKALV---YDDE---FTDLLSALPPDlgrlRAWGGNPDDDEPSGStdetlddli 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7585 -----------PNHLAYVIYTSGTTGKPKGVMVEH-HGLCSLKLMFAET-LRITEedrVVQFASLSFDA---SCWEIfkA 7648
Cdd:PRK07788  195 agsstaplpkpPKPGGIVILTSGTTGTPKGAPRPEpSPLAPLAGLLSRVpFRAGE---TTLLPAPMFHAtgwAHLTL--A 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7649 LFFGATLYIP----AKDTILDyplfesyMNENGITAAILPPTY---AIYLSPDRLP-----SLKKLITGGSAASVEFVQQ 7716
Cdd:PRK07788  270 MALGSTVVLRrrfdPEATLED-------IAKHKATALVVVPVMlsrILDLGPEVLAkydtsSLKIIFVSGSALSPELATR 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7717 WKD---KVRYfNAYGPTEASIVTsvwAASPDglDLRSVP--IGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGY 7791
Cdd:PRK07788  343 ALEafgPVLY-NLYGSTEVAFAT---IATPE--DLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7792 LNRPEltaEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDA 7871
Cdd:PRK07788  417 TDGRD---KQIIDG-------LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDE 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 7872 NGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPA 7930
Cdd:PRK07788  487 EFGQRLRAFVVkaPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
255-747 8.89e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 116.79  E-value: 8.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  255 DYPrdtTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRN-AGVQADQLVGLMVERSLEMIVGIMGILKA 333
Cdd:PRK05677   22 EYP---NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  334 GGAYVPIDPEYPEERIRYMLEDSGTQVLL---SQGHLQERVsFSGTWIR------LDDE--------------------E 384
Cdd:PRK05677   99 GLIVVNTNPLYTAREMEHQFNDSGAKALVclaNMAHLAEKV-LPKTGVKhvivteVADMlpplkrllinavvkhvkkmvP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  385 AYH-------------EDGSNLESVN-GPEHLTYVIYTSGTTGKPKGNLTTHRNII------RVVKNTNYIDvtGQDKLL 444
Cdd:PRK05677  178 AYHlpqavkfndalakGAGQPVTEANpQADDVAVLQYTGGTTGVAKGAMLTHRNLVanmlqcRALMGSNLNE--GCEILI 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  445 Q-LSSYSFDGSTFDIFGALLNGAKLVLVPKETvlDVAKLAGLIEKQQISVMFITTAFFNVLvdmnpdCLRHA-RAILFGG 522
Cdd:PRK05677  256 ApLPLYHIYAFTFHCMAMMLIGNHNILISNPR--DLPAMVKELGKWKFSGFVGLNTLFVAL------CNNEAfRKLDFSA 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  523 ERVSVSHvRKALGHLGPGKIKHV--------YGPTESTVFATSYDVHEVEEGAvsipIGGPISNTAIYIVNAQNKLQPIG 594
Cdd:PRK05677  328 LKLTLSG-GMALQLATAERWKEVtgcaicegYGMTETSPVVSVNPSQAIQVGT----IGIPVPSTLCKVIDDDGNELPLG 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  595 VAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLL 674
Cdd:PRK05677  403 EVGELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLA 476
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  675 KLEAI-EKATVVVRESANGEKqlCAYYVADR---SLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK05677  477 ALPGVlQCAAIGVPDEKSGEA--IKVFVVVKpgeTLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
7443-7930 9.16e-26

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 117.21  E-value: 9.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7443 AREQTIHGLFEEQAERMPEKAAVVFENTQ-----LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIM 7517
Cdd:cd05968    58 GRMNIVEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7518 KAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQ-----------------RHLQECVSFDGKVI----AADDEQAYGEDG 7576
Cdd:cd05968   138 RIGGIVVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkeeadKACAQCPTVEKVVVvrhlGNDFTPAKGRDL 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7577 SNLEPVVGPN-HLA--------YVIYTSGTTGKPKGVmVEHHGLCSLKLMF--AETLRITEEDRVVQFASLSFDASCWEI 7645
Cdd:cd05968   218 SYDEEKETAGdGAErtesedplMIIYTSGTTGKPKGT-VHVHAGFPLKAAQdmYFQFDLKPGDLLTWFTDLGWMMGPWLI 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7646 FKALFFGATLYI-------PAKDTILDyplfesYMNENGITAAILPPTYAIYL-----SPDRLPSLKKLITGGSAASVEF 7713
Cdd:cd05968   297 FGGLILGATMVLydgapdhPKADRLWR------MVEDHEITHLGLSPTLIRALkprgdAPVNAHDLSSLRVLGSTGEPWN 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7714 VQQW--------KDKVRYFNAYGPTEASivtsvwaaspdGLDLRSVPIgRPIA---------NHQIFIVDSQNHMLPVGV 7776
Cdd:cd05968   371 PEPWnwlfetvgKGRNPIINYSGGTEIS-----------GGILGNVLI-KPIKpssfngpvpGMKADVLDESGKPARPEV 438
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7777 aGELCISGA--GLARGYLNRPeltaEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQL 7854
Cdd:cd05968   439 -GELVLLAPwpGMTRGFWRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVL 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7855 LKIASVQETIVIA-RGDANGQQQLCayFVADR------ELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNA 7927
Cdd:cd05968   514 NAHPAVLESAAIGvPHPVKGEAIVC--FVVLKpgvtptEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRV 591

                  ...
gi 386647928 7928 LPA 7930
Cdd:cd05968   592 IRA 594
PRK07514 PRK07514
malonyl-CoA synthase; Validated
5949-6420 9.26e-26

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 115.74  E-value: 9.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5949 PDHLAVTFEDKQ-LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYM 6027
Cdd:PRK07514   16 RDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6028 LEDSGAKLLLVQGHLLD------RASFADKLVNLNDDGayheDGSNLE----------PV-NGPEHLTYVIYTSGTTGRP 6090
Cdd:PRK07514   96 IGDAEPALVVCDPANFAwlskiaAAAGAPHVETLDADG----TGSLLEaaaaapddfeTVpRGADDLAAILYTSGTTGRS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6091 KGVMVEHRNVVrlvknTNYVELNE-----------------QTHILqtgavvFDASTfeiwGALLNGGRLYvvrnetILD 6153
Cdd:PRK07514  172 KGAMLSHGNLL-----SNALTLVDywrftpddvlihalpifHTHGL------FVATN----VALLAGASMI------FLP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6154 AVSLKNAIQQYGINTMWLTAP-LYNQLSQQD-------SGMfaglkTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTE 6225
Cdd:PRK07514  231 KFDPDAVLALMPRATVMMGVPtFYTRLLQEPrltreaaAHM-----RLFISGSAPLLAETHREFQERTGHAILERYGMTE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6226 nTTFSTTHTIVGEQKeAVPIGKPINNSTAYIVDSKL-SLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpger 6304
Cdd:PRK07514  306 -TNMNTSNPYDGERR-AGTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF----- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6305 cYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQkQLCAYFVAER--ELTI 6381
Cdd:PRK07514  379 -FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIgVPHPDFGE-GVTAVVVPKPgaALDE 456
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 386647928 6382 GELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK07514  457 AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
5935-6420 1.13e-25

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 116.51  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5935 KTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKAGGAYV 6013
Cdd:PRK08751   25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6014 PIDPDYPEDRIRYMLEDSGAKLLLV------------------------QGHLLDRA-----SFADKLVN-LNDDgaYHE 6063
Cdd:PRK08751  105 NVNPLYTPRELKHQLIDSGASVLVVidnfgttvqqviadtpvkqvittgLGDMLGFPkaalvNFVVKYVKkLVPE--YRI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6064 DGS-------------NLEPVN-GPEHLTYVIYTSGTTGRPKGVMVEHRNvvrLVKNTNYVE--LNEQTHILQTGAVVFD 6127
Cdd:PRK08751  183 NGAirfrealalgrkhSMPTLQiEPDDIAFLQYTGGTTGVAKGAMLTHRN---LVANMQQAHqwLAGTGKLEEGCEVVIT 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6128 A-STFEIWGALLNGgrLYVVR----NETILDAVSLKNAIQQY---------GINTMW---LTAPLYNQLSqqdsgmFAGL 6190
Cdd:PRK08751  260 AlPLYHIFALTANG--LVFMKiggcNHLISNPRDMPGFVKELkktrftaftGVNTLFnglLNTPGFDQID------FSSL 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6191 KTLIVGGDVlsvphINRVLREH----AGLSIVNGYGPTENTTFSTTHTIVGEQKEAvPIGKPINNSTAYIVDSKLSLLPV 6266
Cdd:PRK08751  332 KMTLGGGMA-----VQRSVAERwkqvTGLTLVEAYGLTETSPAACINPLTLKEYNG-SIGLPIPSTDACIKDDAGTVLAI 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6267 GVWGELIVGGDGVARGYLNRPELTAEkfvessFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQL 6346
Cdd:PRK08751  406 GEIGELCIKGPQVMKGYWKRPEETAK------VMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVI 479
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6347 LKVASVKE-ATVIVREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK08751  480 AMMPGVLEvAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
5961-6320 1.16e-25

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 116.16  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGV--QPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLV 6038
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6039 QGHLldrasfadKLVNLNDdgaYHEDGS-NLEPVN--GPEHLTYVIYTSGTTGRPKGVMVEHRNVVrlvknTNYVELNEQ 6115
Cdd:cd05927    86 DAGV--------KVYSLEE---FEKLGKkNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIV-----SNVAGVFKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6116 THILQTgAVVFD--------ASTFE---IWGALLNGGRLYVVRNE-------------TILDAV-----SLKNAIQQYGI 6166
Cdd:cd05927   150 LEILNK-INPTDvyisylplAHIFErvvEALFLYHGAKIGFYSGDirlllddikalkpTVFPGVprvlnRIYDKIFNKVQ 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6167 NTMWLTAPLYN-QLSQQDSGMFAG-----------------------LKTLIVGGDVLSvPHINRVLREHAGLSIVNGYG 6222
Cdd:cd05927   229 AKGPLKRKLFNfALNYKLAELRSGvvraspfwdklvfnkikqalggnVRLMLTGSAPLS-PEVLEFLRVALGCPVLEGYG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6223 PTENT--TFSTTH--TIVGEqkeavpIGKPINNSTAYIVD----SKLSLLPVGVwGELIVGGDGVARGYLNRPELTAEKF 6294
Cdd:cd05927   308 QTECTagATLTLPgdTSVGH------VGGPLPCAEVKLVDvpemNYDAKDPNPR-GEVCIRGPNVFSGYYKDPEKTAEAL 380
                         410       420
                  ....*....|....*....|....*.
gi 386647928 6295 VESSFLpgercyRTGDLARWLPDGTL 6320
Cdd:cd05927   381 DEDGWL------HTGDIGEWLPNGTL 400
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
7472-7928 1.17e-25

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 114.54  E-value: 1.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQr 7551
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 hlqecvsfdgkviaADDEQAYGEDgsnlePVVgpnhlayVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRvv 7631
Cdd:cd05973    80 --------------AANRHKLDSD-----PFV-------MMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS-- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7632 qFASLSFDASCWEIFKALFFGATLYIPakdTILDYPLFE-----SYMNENGITAAILPPT-YAIYLS-----PDRLP-SL 7699
Cdd:cd05973   132 -FWNAADPGWAYGLYYAITGPLALGHP---TILLEGGFSvestwRVIERLGVTNLAGSPTaYRLLMAagaevPARPKgRL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7700 KKLITGGSAASVEfVQQWKDK---VRYFNAYGPTEASIVtsVWAASPDGLDLRSVPIGRPIANHQIFIVDSQNHMLPVGV 7776
Cdd:cd05973   208 RRVSSAGEPLTPE-VIRWFDAalgVPIHDHYGQTELGMV--LANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGE 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7777 AGELCISGAGLA----RGYLNRpeltaekfvDNPFLAGeRMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEE 7852
Cdd:cd05973   285 PGRLAIDIANSPlmwfRGYQLP---------DTPAIDG-GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7853 QLLKIASVQETIVIARGDANGQQQLCAYFV------ADRELTvSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRN 7926
Cdd:cd05973   355 ALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrggheGTPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRF 433

                  ..
gi 386647928 7927 AL 7928
Cdd:cd05973   434 LL 435
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
6080-6420 1.20e-25

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 112.04  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6080 VIYTSGTTGRPKGVMVEHRNVVRLVKNTN-YVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNETildavSLK 6158
Cdd:cd17630     5 VILTSGSTGTPKAVVHTAANLLASAAGLHsRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQ-----ALA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6159 NAIQQYGINTMWLTAP-LYNQL-SQQDSGMFAGLKTLIVGGdvlsvPHINRVLREHA---GLSIVNGYGPTENTTFSTTH 6233
Cdd:cd17630    80 EDLAPPGVTHVSLVPTqLQRLLdSGQGPAALKSLRAVLLGG-----APIPPELLERAadrGIPLYTTYGMTETASQVATK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6234 TIVGEQKEAVpiGKPINNSTAYIVDSklsllpvgvwGELIVGGDGVARGYLNRPELTAekfvessfLPGERCYRTGDLAR 6313
Cdd:cd17630   155 RPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPE--------FNEDGWFTTKDLGE 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6314 WLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQKqLCAYFVAERELTIGELRAALSQEL 6392
Cdd:cd17630   215 LHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgVPDEELGQR-PVAVIVGRGPADPAELRAWLKDKL 293
                         330       340
                  ....*....|....*....|....*...
gi 386647928 6393 PNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd17630   294 ARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
1314-1798 1.30e-25

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 115.57  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1314 AAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDS 1393
Cdd:PRK12406    3 ATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1394 AASVLLTQTHLQEraQQWGQTLQAVLCLDDE------AAYA-EDASNVANVN-----------EPHDL------AYVIYT 1449
Cdd:PRK12406   83 GARVLIAHADLLH--GLASALPAGVTVLSVPtppeiaAAYRiSPALLTPPAGaidwegwlaqqEPYDGppvpqpQSMIYT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1450 SGTTGRPKGVMIEHRSLVNTAAGYR---REYRLDQfPVRLL------QLASFSFDVFVGDIartlynGGTMVICPkddRI 1520
Cdd:PRK12406  161 SGTTGHPKGVRRAAPTPEQAAAAEQmraLIYGLKP-GIRALltgplyHSAPNAYGLRAGRL------GGVLVLQP---RF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1521 DPARLHYWISEEKITIFESTPALIIPFMDYVAE--HGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEA 1598
Cdd:PRK12406  231 DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV--IYEYYGSTES 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1599 -AIDSSLYDEPLAKlpeAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVAR-GYLNRPELTEEkfvdspfVE 1676
Cdd:PRK12406  309 gAVTFATSEDALSH---PGTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-------ID 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1677 GERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFT--AESEL 1754
Cdd:PRK12406  377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEpqPGATL 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 386647928 1755 KLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 1798
Cdd:PRK12406  457 DEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
4912-5385 1.46e-25

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 114.11  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGV-KPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPdypsdriqfMLedsaasvllt 4990
Cdd:cd05958    10 EWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP---------LL---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4991 qthlqeRAQQWGQTLQ---AALCLDDEAAYAEDasnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREY 5067
Cdd:cd05958    71 ------RPKELAYILDkarITVALCAHALTASD-----------DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNV 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5068 ---RLDQFPVRLLQLAsFSFDvFVGDIARTLYNGGTMVICPKDdriDPARLHYWISEEKITIFESTPALIIPFMDYVAEH 5144
Cdd:cd05958   134 lrlREDDRFVGSPPLA-FTFG-LGGVLLFPFGVGASGVLLEEA---TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5145 GLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAaidsslYDEPLAKLPEAGNV-PIGKAALNAKFYIVD 5223
Cdd:cd05958   209 GPDLSSLRKCVSAGEALPAALHRAWKEATGIP--IIDGIGSTEM------FHIFISARPGDARPgATGKPVPGYEAKVVD 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5224 AHLNPVPVGVLGELCIGGIGVARGylnrpeLTEEKFVDspFVEGERLYrTGDLARWMPDGNVDFIGRIDNQAKIRGYRIE 5303
Cdd:cd05958   281 DEGNPVPDGTIGRLAVRGPTGCRY------LADKRQRT--YVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5304 TGEIETQLLKAEGVREAVVVVRED-AKGQK----VLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANG 5378
Cdd:cd05958   352 PPEVEDVLLQHPAVAECAVVGHPDeSRGVVvkafVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATG 431

                  ....*..
gi 386647928 5379 KIDRKAL 5385
Cdd:cd05958   432 KLQRFAL 438
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
3859-4337 1.52e-25

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 115.89  E-value: 1.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY 3938
Cdd:PRK07059   28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 PEDRIRYMLEDSGAQAL---------LTQ-------RH-----LRERVSFAGTFV------------------AVDDEQA 3979
Cdd:PRK07059  108 TPRELEHQLKDSGAEAIvvlenfattVQQvlaktavKHvvvasMGDLLGFKGHIVnfvvrrvkkmvpawslpgHVRFNDA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3980 YHAD-GSNLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHGLcslklmFANTLQM--------TEQDRVVQFASLsfdas 4049
Cdd:PRK07059  188 LAEGaRQTFKPVkLGPDDVAFLQYTGGTTGVSKGATLLHRNI------VANVLQMeawlqpafEKKPRPDQLNFV----- 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4050 C----WEIFkALFFGATLYIPT-STTIL-----DYPLFESYMNENGITatILPPT---YAAYLN-PD-RMPSLKKLIT-- 4112
Cdd:PRK07059  257 CalplYHIF-ALTVCGLLGMRTgGRNILipnprDIPGFIKELKKYQVH--IFPAVntlYNALLNnPDfDKLDFSKLIVan 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4113 -GGSAASVEFVQQWKDKV--LYFNAYGPTEASIVTSiwdeASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGEL 4189
Cdd:PRK07059  334 gGGMAVQRPVAERWLEMTgcPITEGYGLSETSPVAT----CNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEI 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4190 CISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAV 4269
Cdd:PRK07059  410 CIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGV 483
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4270 QEAIVLAREDANgQQQLVAYFVAQR--ELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK07059  484 LEVAAVGVPDEH-SGEAVKLFVVKKdpALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
401-744 1.71e-25

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 111.34  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  401 HLTYVIYTSGTTGKPKGNLTTHRN-IIRVVKNTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLvpkETVLDV 479
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSwIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  480 AKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLrHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTvFATsYD 559
Cdd:cd17633    78 KSWIRKINQYNATVIYLVPTMLQALARTLEPES-KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELS-FIT-YN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  560 VHEVEEGAVSIpiGGPISNTAIYIVNAQNklqpiGVAGELCVAGDGLARGYLNRPDLTAEKFadnpfapgermYRTGDLA 639
Cdd:cd17633   155 FNQESRPPNSV--GRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  640 RWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADrSLPANEVRSTLSQEL 719
Cdd:cd17633   217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKRFLKQKL 295
                         330       340
                  ....*....|....*....|....*
gi 386647928  720 PAYMLPSYFVQLEQMPLTTNGKVDR 744
Cdd:cd17633   296 SRYEIPKKIIFVDSLPYTSSGKIAR 320
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
4160-4430 1.87e-25

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 110.61  E-value: 1.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4160 VPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPF---EPGERMYRTGDLVRWLPDGN 4236
Cdd:COG3433    16 PPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVpypAQPGRQADDLRLLLRRGLGP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4237 LEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPS 4316
Cdd:COG3433    96 GGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4317 YFVQLAQMPLTPNGKIDRKALPAPEG-SMHAGGEYVAPRTP---TEAKLAHIWQDVLGL--EKVGVKDNFFELGGHSLRA 4390
Cdd:COG3433   176 SAVVALDALLLLALKVVARAAPALAAaEALLAAASPAPALEtalTEEELRADVAELLGVdpEEIDPDDNLFDLGLDSIRL 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 386647928 4391 TALASKVRKElNMELPLRHIFQFPTVEQLAEAIGQLEQQE 4430
Cdd:COG3433   256 MQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAA 294
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1299-1795 1.98e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 115.52  E-value: 1.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1299 FHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 1378
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1379 PDYPSDRIQFMLEDSAASVLLTQTHLQERAQ--QWGQTLQAVLC--LDDEAAYAED----------ASNVANVNEPH--- 1441
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILCLDLVFPRVTnvQSATKIEHVIVtrIADFLPFPKNllypfvqkkqSNLVVKVSESEtih 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 ---------------------DLAYVIYTSGTTGRPKGVMIEHRSLV-NTAAGYRREYRLDQFPVRLLQLASFsFDVF-- 1497
Cdd:PRK06710  186 lwnsvekevntgvevpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVVLGVLPF-FHVYgm 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1498 VGDIARTLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTdyr 1577
Cdd:PRK06710  265 TAVMNLSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVE--- 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1578 vLQERFG--SQFRIINAYGVTEAA--IDSSLYDEplAKLPEAGNVPIGkaalNAKFYIVDAHLNPV-PVGVLGELCIGGI 1652
Cdd:PRK06710  339 -VQEKFEtvTGGKLVEGYGLTESSpvTHSNFLWE--KRVPGSIGVPWP----DTEAMIMSLETGEAlPPGEIGEIVVKGP 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1653 GVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVV 1732
Cdd:PRK06710  412 QIMKGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVT 484
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 1733 VVREDAKGQKVLCAYFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK06710  485 IGVPDPYRGETVKAFVVLKEGTECSeeELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
256-747 2.02e-25

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 115.47  E-value: 2.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  256 YPRDTTIHRLFEEQAErrPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQ--LVGLmvERSLEMIVGIMGILKA 333
Cdd:PRK10946   21 YWQDLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtaLVQL--GNVAEFYITFFALLKL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  334 G---------------GAYV-PIDP-----------------------EYPEERIRYMLEDSGTQVLLsqghlqervsfs 374
Cdd:PRK10946   97 GvapvnalfshqrselNAYAsQIEPalliadrqhalfsdddflntlvaEHSSLRVVLLLNDDGEHSLD------------ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  375 gTWIRLDDEEayhedgsnleSVNGPEHLTYVIY---TSGTTGKPKGNLTTHRNIIRVVKNTNYI-DVTGQDKLL------ 444
Cdd:PRK10946  165 -DAINHPAED----------FTATPSPADEVAFfqlSGGSTGTPKLIPRTHNDYYYSVRRSVEIcGFTPQTRYLcalpaa 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  445 ---QLSSysfDGStfdiFGALLNGAKLVLVPKETVLDVAKLaglIEKQQISVmfitTAFFNVLVDM---------NPDCL 512
Cdd:PRK10946  234 hnyPMSS---PGA----LGVFLAGGTVVLAPDPSATLCFPL---IEKHQVNV----TALVPPAVSLwlqaiaeggSRAQL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  513 RHARAILFGGERVSVSHVRKALGHLGpGKIKHVYGPTESTVFATSYDVHEVEegaVSIPIGGPIS-NTAIYIVNAQNKLQ 591
Cdd:PRK10946  300 ASLKLLQVGGARLSETLARRIPAELG-CQLQQVFGMAEGLVNYTRLDDSDER---IFTTQGRPMSpDDEVWVADADGNPL 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  592 PIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEA 671
Cdd:PRK10946  376 PQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIEN 449
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  672 HLLKLEA-IEKATVVVRESANGEKQlCAYYVADRSLPANEVRSTL-SQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK10946  450 LLLRHPAvIHAALVSMEDELMGEKS-CAFLVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK13382 PRK13382
bile acid CoA ligase;
7439-7931 2.17e-25

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 115.24  E-value: 2.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7439 AAEYAREQTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMK 7518
Cdd:PRK13382   36 AAMRREGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7519 AGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQECV--SFDG-----KVIAADDEQAYG------EDGSNLEPVVGP 7585
Cdd:PRK13382  116 IGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVdrALADcpqatRIVAWTDEDHDLtvevliAAHAGQRPEPTG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7586 NHLAYVIYTSGTTGKPKGVM-VEHHGLCSLKLMFAETLRITEEDRVVqfASLSFDAscWEiFKALFFGATLyipaKDTIL 7664
Cdd:PRK13382  196 RKGRVILLTSGTTGTPKGARrSGPGGIGTLKAILDRTPWRAEEPTVI--VAPMFHA--WG-FSQLVLAASL----ACTIV 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7665 DYPLFE-----SYMNENGITAAILPPTY--------AIYLSPDRLPSLKKLITGGSAASVEFVQQWKDK---VRYfNAYG 7728
Cdd:PRK13382  267 TRRRFDpeatlDLIDRHRATGLAVVPVMfdrimdlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQfgdVIY-NNYN 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7729 PTEASIVTSvwaASPDglDLRSVP--IGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYlnrpelTAEKfvDNP 7806
Cdd:PRK13382  346 ATEAGMIAT---ATPA--DLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------TSGS--TKD 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7807 FLAGerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--AD 7884
Cdd:PRK13382  413 FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVlkPG 490
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 7885 RELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAP 7931
Cdd:PRK13382  491 ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
4443-4854 2.25e-25

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 112.78  E-value: 2.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4443 YPVSSAQKRLYIL--QQlegaAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGF-ELIDGEPVQRIYPEVDFAV 4519
Cdd:cd19545     2 YPCTPLQEGLMALtaRQ----PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPISW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4520 ETVQaSEQEAKAivRDFIRPFDLaKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGEELPGlRIQY 4599
Cdd:cd19545    78 TEST-SLDEYLE--EDRAAPMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4600 KDY--AVWQQSEAQKEQlkrqeaYWLEAFRGELPVL--EMPtdyaRPAVQSYAGDTLDFRMNSEISeglkriaAESGATL 4675
Cdd:cd19545   153 SRFvkYLRQLDDEAAAE------FWRSYLAGLDPAVfpPLP----SSRYQPRPDATLEHSISLPSS-------ASSGVTL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4676 YMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTH--ADLQSLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTlgafeHQTY 4753
Cdd:cd19545   216 ATVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDL-----LDMI 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4754 PFEE--LVDKLQMARDLSRNPLFDTMFSLQ-NTENKEMHLPGLHLTPYPTEYGM-SKFDLSLDMMEDSEGLECSLEFATA 4829
Cdd:cd19545   291 PFEHtgLQNIRRLGPDARAACNFQTLLVVQpALPSSTSESLELGIEEESEDLEDfSSYGLTLECQLSGSGLRVRARYDSS 370
                         410       420
                  ....*....|....*....|....*
gi 386647928 4830 LYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19545   371 VISEEQVERLLDQFEHVLQQLASAP 395
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
5491-5902 2.36e-25

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 113.56  E-value: 2.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5491 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN-GEPVQRVYKEVN--FAV 5567
Cdd:cd19547     2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAppWAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5568 EHYRTSE----AEAGEVVRGFVRT--FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNG---- 5637
Cdd:cd19547    82 LDWSGEDpdrrAELLERLLADDRAagLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEElahg 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5638 --ESLAPLRiQYKDYATWQQSEAQQEQmkRQEAYWLDMFRgELPvlelPTDYPR-PAVRKFEGSLLQRQLEPKLGEGLQR 5714
Cdd:cd19547   162 rePQLSPCR-PYRDYVRWIRARTAQSE--ESERFWREYLR-DLT----PSPFSTaPADREGEFDTVVHEFPEQLTRLVNE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5715 IAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGTPIAGRTH--SDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETM 5792
Cdd:cd19547   234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5793 LGAYEHQSYPFEELVEKAQPARdLSRNPLFDTLFALQNKETGELQLDGLRL----------TPYPAEHTVAKFdlsvdvt 5862
Cdd:cd19547   314 ATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIqiidlhaqekTEYPIGLIVLPL------- 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 386647928 5863 egsEGLELSMEYSTALYTRETIERMAKHFEQLLTAIVQAP 5902
Cdd:cd19547   386 ---QKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1292-1795 2.59e-25

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 114.90  E-value: 2.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1292 DAPENEVF-HALFEKQAERTPEVAAVVYEND-----RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGAL 1365
Cdd:cd05970    11 NVPENFNFaYDVVDAMAKEYPDKLALVWCDDageerIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1366 AVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLT------QTHLQERAQQWGQTLQAVLCLDDE----AAYAEDASNVA 1435
Cdd:cd05970    91 ALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaedniPEEIEKAAPECPSKPKLVWVGDPVpegwIDFRKLIKNAS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1436 NVNEP---------HDLAYVIYTSGTTGRPKgvMIEHrslVNTaagyrreyrldqFPVRLLQLASFSFDVFVGD----IA 1502
Cdd:cd05970   171 PDFERptansypcgEDILLVYFSSGTTGMPK--MVEH---DFT------------YPLGHIVTAKYWQNVREGGlhltVA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1503 RT---------LYN---GGTMVICPKDDRIDPARLHYWISEEKITIFeSTPALIIPFMDYVAEHGLDMSSMELLITSSDS 1570
Cdd:cd05970   234 DTgwgkavwgkIYGqwiAGAAVFVYDYDKFDPKALLEKLSKYGVTTF-CAPPTIYRFLIREDLSRYDLSSLRYCTTAGEA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1571 CSVTDYRVLQERFGSQFRiiNAYGVTEAAIDsslydepLAKLP--EAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELC 1648
Cdd:cd05970   313 LNPEVFNTFKEKTGIKLM--EGFGQTETTLT-------IATFPwmEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIV 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1649 IG-----GIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLArWM-PDGNVDFIGRIDNQAKIRGYRIETGEIETQLL 1722
Cdd:cd05970   384 IRtskgkPVGLFGGYYKDAEKTAEVWHDG-------YYHTGDAA-WMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALI 455
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 1723 KAEGVREAVVVVREDAK-GQK-----VLCAYFTAESELKlSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05970   456 QHPAVLECAVTGVPDPIrGQVvkatiVLAKGYEPSEELK-KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
PRK06145 PRK06145
acyl-CoA synthetase; Validated
270-747 2.98e-25

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 114.21  E-value: 2.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERI 349
Cdd:PRK06145   12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  350 RYMLEDSGTQVLLSQGHLQERVSFSGTWIRLDdeEAYHEDGSNL---------ESVNGPEHLTYVIYTSGTTGKPKGNLT 420
Cdd:PRK06145   92 AYILGDAGAKLLLVDEEFDAIVALETPKIVID--AAAQADSRRLaqggleippQAAVAPTDLVRLMYTSGTTDRPKGVMH 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  421 THRNII-RVVKNTNYIDVTGQDKLLQLSSYSFDGStFDIFG-ALLNGAKLVLVPKEtvLDVAKLAGLIEKQQISVMFITT 498
Cdd:PRK06145  170 SYGNLHwKSIDHVIALGLTASERLLVVGPLYHVGA-FDLPGiAVLWVGGTLRIHRE--FDPEAVLAAIERHRLTCAWMAP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  499 AFFNVLVDMnPDCLRH----ARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATSYDV-HEVEEGAVSipiG 573
Cdd:PRK06145  247 VMLSRVLTV-PDRDRFdldsLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAgREIEKIGST---G 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  574 GPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRI 653
Cdd:PRK06145  323 RALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLTDRK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  654 DDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEkQLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVQ 730
Cdd:PRK06145  396 KDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGE-RITAVVVlnPGATLTLEALDRHCRQRLASFKVPRQLKV 474
                         490
                  ....*....|....*..
gi 386647928  731 LEQMPLTTNGKVDRRAL 747
Cdd:PRK06145  475 RDELPRNPSGKVLKRVL 491
PRK07514 PRK07514
malonyl-CoA synthase; Validated
2359-2828 3.05e-25

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 114.20  E-value: 3.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAV-VFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYM 2437
Cdd:PRK07514   16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2438 LEDSSAQVLL-------AQRRLQERVSfAGTVVTVDDeqayAGDGSNLESA-----------VGPNDLAYIIYTSGTTGK 2499
Cdd:PRK07514   96 IGDAEPALVVcdpanfaWLSKIAAAAG-APHVETLDA----DGTGSLLEAAaaapddfetvpRGADDLAAILYTSGTTGR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2500 PKGVMVEHHGLCSLKQMFANTLQINAQDRVVQfaslsfdasCWEVFQT----------LFFGATLYiptketildyqWFE 2569
Cdd:PRK07514  171 SKGAMLSHGNLLSNALTLVDYWRFTPDDVLIH---------ALPIFHThglfvatnvaLLAGASMI-----------FLP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2570 RYmsDNGITTATLP--------PTYAVYL--NPD-------HMpdfkRLIAAGSASSL-ELLQQWKDKVKY--FNAYGPT 2629
Cdd:PRK07514  231 KF--DPDAVLALMPratvmmgvPTFYTRLlqEPRltreaaaHM----RLFISGSAPLLaETHREFQERTGHaiLERYGMT 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2630 EDSICTtiwtpstedisqlkSVP-----IGG------PIVNHRIYIVDAHyQPVPVGVAGELCIAGVGLARGYLNRPDLT 2698
Cdd:PRK07514  305 ETNMNT--------------SNPydgerRAGtvgfplPGVSLRVTDPETG-AELPPGEIGMIEVKGPNVFKGYWRMPEKT 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2699 AEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVI--AHDDASgqKQ 2776
Cdd:PRK07514  370 AEEFRADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIgvPHPDFG--EG 441
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2777 LCAYFVADRTMTVGE--LRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK07514  442 VTAVVVPKPGAALDEaaILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
2312-2830 3.15e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 114.32  E-value: 3.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2312 PEAPIAGLEMLTAAeqtqlhhvfnataadYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALG 2391
Cdd:PRK13383   17 PPSPRAVLRLLREA---------------SRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2392 VKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAY 2471
Cdd:PRK13383   82 VAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2472 AGDGSNLESAVGPNDlAYIIYTSGTTGKPKGVMVEHHglcsLKQMFANTLQINAQDRVVQFASLSFDAScweVFQTLFFG 2551
Cdd:PRK13383  162 GAEESGGRPAVAAPG-RIVLLTSGTTGKPKGVPRAPQ----LRSAVGVWVTILDRTRLRTGSRISVAMP---MFHGLGLG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2552 A-TLYIPTKETILDYQWF--ERYMSDNGITTA----TLPPTYAVYLN-PDH------MPDFKRLIAAGSASSLELLQQWK 2617
Cdd:PRK13383  234 MlMLTIALGGTVLTHRHFdaEAALAQASLHRAdaftAVPVVLARILElPPRvrarnpLPQLRVVMSSGDRLDPTLGQRFM 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2618 DKVK--YFNAYGPTEDSIcTTIWTPstediSQLKSVP--IGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYln 2693
Cdd:PRK13383  314 DTYGdiLYNGYGSTEVGI-GALATP-----ADLRDAPetVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY-- 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2694 rPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASG 2773
Cdd:PRK13383  386 -TDGGGKAVVDG-------MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERF 457
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2774 QKQLCAYFVADRTMTV--GELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALPA 2830
Cdd:PRK13383  458 GHRLAAFVVLHPGSGVdaAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
265-747 3.16e-25

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 115.12  E-value: 3.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  265 LFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEY 344
Cdd:PRK07059   28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  345 PEERIRYMLEDSGTQ---VLLSQGHLQERV------------------SFSGT---------------W-----IRLDDE 383
Cdd:PRK07059  108 TPRELEHQLKDSGAEaivVLENFATTVQQVlaktavkhvvvasmgdllGFKGHivnfvvrrvkkmvpaWslpghVRFNDA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  384 EAYHEdGSNLESVN-GPEHLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDK--------LLQLSSYSFDG 453
Cdd:PRK07059  188 LAEGA-RQTFKPVKlGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQMEAWLQPAFEKKprpdqlnfVCALPLYHIFA 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  454 STFDIFGALLNGAKLVLVPKEtvLDVAKLAGLIEKQQISVMFITTAFFNVLVDmNPDC----LRHARAILFGGERVSVSH 529
Cdd:PRK07059  267 LTVCGLLGMRTGGRNILIPNP--RDIPGFIKELKKYQVHIFPAVNTLYNALLN-NPDFdkldFSKLIVANGGGMAVQRPV 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  530 VRKALGHLGPGkIKHVYGPTESTVFATsydVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARG 609
Cdd:PRK07059  344 AERWLEMTGCP-ITEGYGLSETSPVAT---CNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAG 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  610 YLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAI-EKATVVVRE 688
Cdd:PRK07059  420 YWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVlEVAAVGVPD 493
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  689 SANGEKqLCAYYV-ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK07059  494 EHSGEA-VKLFVVkKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
7451-8047 3.37e-25

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 116.73  E-value: 3.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:COG3319     6 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVLLTQ-----RHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVM 7605
Cdd:COG3319    86 LALAAAAAALLLAALALLLAllaalALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7606 VEHHGLCSLKLMFAETLRITEEDRVVQFAS-LSFDASCWEIFKALFFGATLYIPAKDTILDYPLFESYMNENGITAAILP 7684
Cdd:COG3319   166 LVLAALLALLLAALLALALALAALLLLALAaALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7685 PTYAIYLSPDRLPSLKKLITGGSAASVEFVQQWKDKVRYF------NAYGPTEASIVTSVWAASPDGLDLRSVPIGRPIA 7758
Cdd:COG3319   246 ALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAaaalaaGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7759 NHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQV 7838
Cdd:COG3319   326 VLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQR 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7839 KIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLT 7918
Cdd:COG3319   406 LRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLL 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7919 PNGKIDRNALPAPEGSmQTGADFVEPRTPVEAELARIWQEVLGIGPISVKDNFFELGGHSLRATVLSSKVNKELNVNLPL 7998
Cdd:COG3319   486 LLLAALLLAAAAPAAA-AAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLL 564
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 7999 RDIFRFPTVEALAQVIDGLEQEEHSAIPVIGEReyypvSSAQKRLFILH 8047
Cdd:COG3319   565 LALLLAPTLAALAAALAAAAAAAALSPLVPLRA-----GGSGPPLFCVH 608
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
2342-2812 3.40e-25

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 115.36  E-value: 3.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2342 EADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGA 2421
Cdd:PRK08279   34 DSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2422 YVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYAGDG--------SNLESA------------ 2481
Cdd:PRK08279  114 VALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDtlddpegyEDLAAAaagapttnpasr 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2482 --VGPNDLAYIIYTSGTTGKPKGVMVEHH-GLCSLkQMFANTLQINAQDR-------------VVQFASL---------- 2535
Cdd:PRK08279  194 sgVTAKDTAFYIYTSGTTGLPKAAVMSHMrWLKAM-GGFGGLLRLTPDDVlycclplyhntggTVAWSSVlaagatlalr 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2536 -SFDASC-WEVFQTlfFGATL--YI----------PTKETILDYQWfeRYMSDNGittatlpptyavyLNPDHMPDFK-R 2600
Cdd:PRK08279  273 rKFSASRfWDDVRR--YRATAfqYIgelcryllnqPPKPTDRDHRL--RLMIGNG-------------LRPDIWDEFQqR 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2601 L----IAAGSASSlellqqwKDKVKYFNAYG--------PTEDSICTTI--WTPSTEDisqlksvPIGGPivnhriyivD 2666
Cdd:PRK08279  336 FgiprILEFYAAS-------EGNVGFINVFNfdgtvgrvPLWLAHPYAIvkYDVDTGE-------PVRDA---------D 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2667 AHYQPVPVGVAGELcIAGVGLAR---GYlNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGY 2743
Cdd:PRK08279  393 GRCIKVKPGEVGLL-IGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGE 470
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 2744 RIELGEIEEQLLKVASVQEAIV--IAHDDASGQKQLCAYFVAD-RTMTVGELRGELSGELPGYMIPAhFVQL 2812
Cdd:PRK08279  471 NVATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADgAEFDLAALAAHLYERLPAYAVPL-FVRL 541
PRK09274 PRK09274
peptide synthase; Provisional
3862-4248 3.45e-25

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 114.61  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3862 EQALRNPDAVAVVFEKS----------QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAY 3931
Cdd:PRK09274   14 RAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3932 IPIDPEYPEDRIRYMLEDSGAQALLTQ--RHLRERV---SFAG--TFVAVD----------DEQAYHADGSNLEPV-VGP 3993
Cdd:PRK09274   94 VLVDPGMGIKNLKQCLAEAQPDAFIGIpkAHLARRLfgwGKPSvrRLVTVGgrllwggttlATLLRDGAAAPFPMAdLAP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3994 NHLAYVIYTSGTTGKPKGVMVEHHglcslklMFANTLQMTEQDRvvQFASLSFDASCWEIFkALF---FGATLYIP---T 4067
Cdd:PRK09274  174 DDMAAILFTSGSTGTPKGVVYTHG-------MFEAQIEALREDY--GIEPGEIDLPTFPLF-ALFgpaLGMTSVIPdmdP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4068 STTILDYP--LFESyMNENGITATILPPTY------AAYLNPDRMPSLKKLITGG---SAASVEFVQQW-KDKVLYFNAY 4135
Cdd:PRK09274  244 TRPATVDPakLFAA-IERYGVTNLFGSPALlerlgrYGEANGIKLPSLRRVISAGapvPIAVIERFRAMlPPDAEILTPY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4136 GPTEASIVTSIwdEASDSLGDRKSVP-------IGRPLANHRIYVVD---------SHNRMLPVGVAGELCISGVGLARG 4199
Cdd:PRK09274  323 GATEALPISSI--ESREILFATRAATdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRS 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 4200 YLNRPELTAE-KFVDnpfEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVK 4248
Cdd:PRK09274  401 YYNRPEATRLaKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3998-4333 4.34e-25

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 111.32  E-value: 4.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3998 YVIYTSGTTGKPKGVMVEHHGLCSLKLMFAN------TLQMTEQDRVVQFASLSFDASC--------WEIFKALFFGATL 4063
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADfgtgefTPSEDAHKAAAAAAGTVMFPAPplmhgtgsWTAFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4064 YIPTSTTILDyPLFESYMNENGITATILPPTYAAYL-------NPDRMPSLKKLITGGSAASVEFVQQWKDKV---LYFN 4133
Cdd:cd05924    87 VLPDDRFDPE-EVWRTIEKHKVTSMTIVGDAMARPLidalrdaGPYDLSSLFAISSGGALLSPEVKQGLLELVpniTLVD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4134 AYGPTEASIV-TSIWDEASDSLGDRKsvpigrpLANHRIYVVDSHNRMLPVGVAGELCISGVGL-ARGYLNRPELTAEKF 4211
Cdd:cd05924   166 AFGSSETGFTgSGHSAGSGPETGPFT-------RANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4212 --VDnpfepGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAy 4289
Cdd:cd05924   239 peVD-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVA- 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 4290 FVAQRE---LTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:cd05924   313 VVQLREgagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
4903-5388 4.40e-25

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 114.03  E-value: 4.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4903 AAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLED 4982
Cdd:PRK12406    2 YATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4983 SAASVLLTQT----HLQERAQQWGQTLQAALCLDDEAAYA-EDASNVANVN-----------EPHDL------AYVIYTS 5040
Cdd:PRK12406   82 SGARVLIAHAdllhGLASALPAGVTVLSVPTPPEIAAAYRiSPALLTPPAGaidwegwlaqqEPYDGppvpqpQSMIYTS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5041 GTTGRPKGVMIEHRSLVNTAAGYR---REYRLDQfPVRLL------QLASFSFDVFVGDIartlynGGTMVICPkddRID 5111
Cdd:PRK12406  162 GTTGHPKGVRRAAPTPEQAAAAEQmraLIYGLKP-GIRALltgplyHSAPNAYGLRAGRL------GGVLVLQP---RFD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5112 PARLHYWISEEKITIFESTPALIIPFMDYVAE--HGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEA- 5188
Cdd:PRK12406  232 PEELLQLIERHRITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV--IYEYYGSTESg 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5189 AIDSSLYDEPLAKlpeAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVAR-GYLNRPELTEEkfvdspfVEG 5267
Cdd:PRK12406  310 AVTFATSEDALSH---PGTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-------IDR 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5268 ERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFT--AESELK 5345
Cdd:PRK12406  378 GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEpqPGATLD 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 386647928 5346 LSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 5388
Cdd:PRK12406  458 EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
267-742 4.58e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 114.49  E-value: 4.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  267 EEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQA-DQLVGLMVERSlEMIVGIMGILKAGGAYVPIDPEYP 345
Cdd:PRK07786   24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFRLT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  346 EERIRYMLEDSGTQVLLSQGHLQ-------ERVSFSGTWI---------RLDDEEAYHEDGSNLESVNGPEHLTYVI-YT 408
Cdd:PRK07786  103 PPEIAFLVSDCGAHVVVTEAALApvatavrDIVPLLSTVVvaggssddsVLGYEDLLAEAGPAHAPVDIPNDSPALImYT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  409 SGTTGKPKGNLTTHRNI-------IRvvknTNYIDVTgqdkllqlSSYSFDGSTFDIFGALLNGAKLVLVPKETVL---- 477
Cdd:PRK07786  183 SGTTGRPKGAVLTHANLtgqamtcLR----TNGADIN--------SDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIyplg 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  478 --DVAKLAGLIEKQQISVMFITTAFFNVLVD---MNPDCLRhARAILFGGERVSVSHVRkALGHLGPG-KIKHVYGPTES 551
Cdd:PRK07786  251 afDPGQLLDVLEAEKVTGIFLVPAQWQAVCAeqqARPRDLA-LRVLSWGAAPASDTLLR-QMAATFPEaQILAAFGQTEM 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  552 TvfatsyDVHEVEEGAVSI----PIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFa 627
Cdd:PRK07786  329 S------PVTCMLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF- 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  628 pgermyRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESAN-GEKQLCAYYVA--DR 704
Cdd:PRK07786  402 ------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRndDA 475
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 386647928  705 SLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKV 742
Cdd:PRK07786  476 ALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
PRK07638 PRK07638
acyl-CoA synthetase; Validated
261-755 4.86e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 113.34  E-value: 4.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLrNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPI 340
Cdd:PRK07638    2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  341 DPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWIRLDDE-----EAYHEDGSNLESV-NGPehlTYVIYTSGTTGK 414
Cdd:PRK07638   81 DIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEwkrmiEKYLPTYAPIENVqNAP---FYMGFTSGSTGK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  415 PKGNLTTHRNIIRVVK-NTNYIDVTGQDKLL---QLSSYSFdgstfdIFGA---LLNGAKLVLVPKETVLDVAKLaglIE 487
Cdd:PRK07638  158 PKAFLRAQQSWLHSFDcNVHDFHMKREDSVLiagTLVHSLF------LYGAistLYVGQTVHLMRKFIPNQVLDK---LE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  488 KQQISVMFITTAFFNVLVDMNpDCLRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTE-STVFATSYDVHEVEEG 566
Cdd:PRK07638  229 TENISVMYTVPTMLESLYKEN-RVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASElSFVTALVDEESERRPN 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  567 AVsipiGGPISNTAIYIVN-AQNKLQPiGVAGELCVAGDGLARGYLNRPDLTAEKFADnpfapgERMyRTGDLARWLPDG 645
Cdd:PRK07638  308 SV----GRPFHNVQVRICNeAGEEVQK-GEIGTVYVKSPQFFMGYIIGGVLARELNAD------GWM-TVRDVGYEDEEG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  646 TIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKqlcAYYVADRSLPANEVRSTLSQELPAYML 724
Cdd:PRK07638  376 FIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIgVPDSYWGEK---PVAIIKGSATKQQLKSFCLQRLSSFKI 452
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928  725 PSYFVQLEQMPLTTNGKVDRRALPAPEESME 755
Cdd:PRK07638  453 PKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
5960-6420 7.62e-25

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 113.33  E-value: 7.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5960 QLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVq 6039
Cdd:cd05932     6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6040 GHLLDRASFA--------DKLVNLNDDGAYHEDGSNL---------EPVNGPEHLTYVIYTSGTTGRPKGVMVEHRN--- 6099
Cdd:cd05932    85 GKLDDWKAMApgvpegliSISLPPPSAANCQYQWDDLiaqhppleeRPTRFPEQLATLIYTSGTTGQPKGVMLTFGSfaw 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6100 ----VVRLVKNT------NYVEL---NEQTHI----LQTGAVVFDASTFEIWGA---------LLNGGRLYVVRNETILD 6153
Cdd:cd05932   165 aaqaGIEHIGTEendrmlSYLPLahvTERVFVeggsLYGGVLVAFAESLDTFVEdvqrarptlFFSVPRLWTKFQQGVQD 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6154 AVSLKNaiqqygINTMwLTAPLYNQLSQQDsgMFAGL---KTLIVGGDVLSVPhiNRVLR--EHAGLSIVNGYGPTENTT 6228
Cdd:cd05932   245 KIPQQK------LNLL-LKIPVVNSLVKRK--VLKGLgldQCRLAGCGSAPVP--PALLEwyRSLGLNILEAYGMTENFA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6229 FSTThTIVGEQKEAVpIGKPINNSTAYIVDSklsllpvgvwGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRT 6308
Cdd:cd05932   314 YSHL-NYPGRDKIGT-VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFL------RT 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6309 GDLARWLPDGTLEYKGRIDEQVKI-RGYRIELGEIEEQLLKVASVkEATVIVREDES---GQKQLCAYFVAER-ELTIGE 6383
Cdd:cd05932   376 GDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPaplALVVLSEEARLRAdAFARAE 454
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 6384 LRAALSQELPNymIPSHFVPLERMP---------------LTPNGKIDRRAL 6420
Cdd:cd05932   455 LEASLRAHLAR--VNSTLDSHEQLAgivvvkdpwsidngiLTPTLKIKRNVL 504
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
7456-7928 8.75e-25

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 112.27  E-value: 8.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 rymledsgaQVLLTQRHLQECVSFDGkviaadDEQAYGEDGSNLEPVVGPNHLAY-------VIYTSGTTGKPKGVM--V 7606
Cdd:PRK09029   93 ---------EELLPSLTLDFALVLEG------ENTFSALTSLHLQLVEGAHAVAWqpqrlatMTLTSGSTGLPKAAVhtA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7607 EHH-----GLCSLklmfaetlriteedrvvqfasLSFDAS-CWE-------------IFKALFFGATLYIPAKDtildyP 7667
Cdd:PRK09029  158 QAHlasaeGVLSL---------------------MPFTAQdSWLlslplfhvsgqgiVWRWLYAGATLVVRDKQ-----P 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7668 LFESYmneNGITAAILPPTYAI-YLSPDRLP-SLKKLITGGSAASVEFVQQWKDK-VRYFNAYGPTE-ASIVTSVWAasp 7743
Cdd:PRK09029  212 LEQAL---AGCTHASLVPTQLWrLLDNRSEPlSLKAVLLGGAAIPVELTEQAEQQgIRCWCGYGLTEmASTVCAKRA--- 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7744 DGLDlrsvPIGRPIANHQIFIVDsqnhmlpvgvaGELCISGAGLARGYLNRPELTaekfvdnPFLAGERMYRTGDLARWL 7823
Cdd:PRK09029  286 DGLA----GVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7824 pDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGY 7903
Cdd:PRK09029  344 -NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVNLAEWLQDKLARF 422
                         490       500
                  ....*....|....*....|....*...
gi 386647928 7904 MIPsyfVQLEQMPLT-PNG--KIDRNAL 7928
Cdd:PRK09029  423 QQP---VAYYLLPPElKNGgiKISRQAL 447
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
2336-2828 9.26e-25

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 113.43  E-value: 9.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2336 ATAADYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLAR-TLQALGVKTDQPVGLMLERSLEMVVGMFA 2414
Cdd:PRK08751   16 AAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2415 VLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQERVS--FAGT----VVT------------------------ 2464
Cdd:PRK08751   96 VLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQqvIADTpvkqVITtglgdmlgfpkaalvnfvvkyvkk 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2465 -VDD---------EQAYA-GDGSNLESA-VGPNDLAYIIYTSGTTGKPKGVMVEHhglcslKQMFANTLQinaqdrvvqf 2532
Cdd:PRK08751  176 lVPEyringairfREALAlGRKHSMPTLqIEPDDIAFLQYTGGTTGVAKGAMLTH------RNLVANMQQ---------- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2533 aslsfdASCWevfqtlFFGATLYIPTKETILD----YQWFEryMSDNGITTATLPPTYAVYLNPDHMPDF---------- 2598
Cdd:PRK08751  240 ------AHQW------LAGTGKLEEGCEVVITalplYHIFA--LTANGLVFMKIGGCNHLISNPRDMPGFvkelkktrft 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2599 --------------------------KRLIAAGSASSLELLQQWKD--KVKYFNAYGPTEDSICTTIWTPSTEDISQlks 2650
Cdd:PRK08751  306 aftgvntlfngllntpgfdqidfsslKMTLGGGMAVQRSVAERWKQvtGLTLVEAYGLTETSPAACINPLTLKEYNG--- 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2651 vPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAeKFVDnpfepGERMYRTGDLAKWLPDGTIEY 2730
Cdd:PRK08751  383 -SIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETA-KVMD-----ADGWLHTGDIARMDEQGFVYI 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2731 LGRIDHQVKIRGYRIELGEIEEQLLKVASVQE-AIVIAHDDASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHF 2809
Cdd:PRK08751  456 VDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEvAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRII 535
                         570
                  ....*....|....*....
gi 386647928 2810 VQLERMPLTPNGKIDRKAL 2828
Cdd:PRK08751  536 EFRKELPKTNVGKILRREL 554
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
3864-4337 9.49e-25

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 112.27  E-value: 9.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRI 3943
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 rymledsgaQALLTQRHLRERVSFAGtFVAVDDEQAYHADGSNLEPVVGPNH--LAYVIYTSGTTGKPKGVM--VEHH-- 4017
Cdd:PRK09029   93 ---------EELLPSLTLDFALVLEG-ENTFSALTSLHLQLVEGAHAVAWQPqrLATMTLTSGSTGLPKAAVhtAQAHla 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4018 ---GLCSLklmfantLQMTEQDRVVqfasLS---FDASCWEIF-KALFFGATLYIPTSTtildyPLFESYmneNGITATI 4090
Cdd:PRK09029  163 saeGVLSL-------MPFTAQDSWL----LSlplFHVSGQGIVwRWLYAGATLVVRDKQ-----PLEQAL---AGCTHAS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4091 LPPTYA-AYLNPDRMP-SLKKLITGGSAASVEFVQQWKDK-VLYFNAYGPTE-ASIVTSiwdEASDSLGDrksvpIGRPL 4166
Cdd:PRK09029  224 LVPTQLwRLLDNRSEPlSLKAVLLGGAAIPVELTEQAEQQgIRCWCGYGLTEmASTVCA---KRADGLAG-----VGSPL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4167 ANHRIYVVDshnrmlpvgvaGELCISGVGLARGYLNRPELTaekfvdnPFEPGERMYRTGDLVRWLpDGNLEYLGRIDHQ 4246
Cdd:PRK09029  296 PGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTILGRLDNL 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4247 VKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIP-SYFVqlaqMP 4325
Cdd:PRK09029  357 FFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVNLAEWLQDKLARFQQPvAYYL----LP 432
                         490
                  ....*....|....*
gi 386647928 4326 LT-PNG--KIDRKAL 4337
Cdd:PRK09029  433 PElKNGgiKISRQAL 447
PRK08162 PRK08162
acyl-CoA synthetase; Validated
1304-1795 1.02e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 113.12  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1304 EKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 1383
Cdd:PRK08162   25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1384 DRIQFMLEDSAASVLLTQTHLQERAQQWGQTL--QAVLCLDDEAAYAEDASNVANVN---------------EPHDLAYV 1446
Cdd:PRK08162  105 ASIAFMLRHGEAKVLIVDTEFAEVAREALALLpgPKPLVIDVDDPEYPGGRFIGALDyeaflasgdpdfawtLPADEWDA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1447 I---YTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFD--VFVGDIARtlyNGGTMViCPKddRID 1521
Cdd:PRK08162  185 IalnYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNgwCFPWTVAA---RAGTNV-CLR--KVD 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1522 PARLHYWISEEKITIFESTPalIIpfmdyvaehgldmssMELLITSSDSC-SVTDYR-------------VLQ--ERFGs 1585
Cdd:PRK08162  259 PKLIFDLIREHGVTHYCGAP--IV---------------LSALINAPAEWrAGIDHPvhamvagaappaaVIAkmEEIG- 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1586 qFRIINAYGVTEAAIDSSLydepLAKLPEAGNVPIG-KAALNAK----FYIVDA-------HLNPVPVG--VLGELCIGG 1651
Cdd:PRK08162  321 -FDLTHVYGLTETYGPATV----CAWQPEWDALPLDeRAQLKARqgvrYPLQEGvtvldpdTMQPVPADgeTIGEIMFRG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1652 IGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVdfigRIDNQAK---IRG-YRIETGEIETQLLKAEGV 1727
Cdd:PRK08162  396 NIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYI----KIKDRSKdiiISGgENISSIEVEDVLYRHPAV 464
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 1728 REAVVVVREDAKGQKVLCAYFtaesELK------LSELRSSLSQELPGYMIPSYFVqLEQLPLTANGKIDRKAL 1795
Cdd:PRK08162  465 LVAAVVAKPDPKWGEVPCAFV----ELKdgasatEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
7463-7923 1.18e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 112.69  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7463 AAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDS 7542
Cdd:PRK08276    3 VIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7543 GAQVL---------------LTQRHLQECVSFDGkviAADDEQAYGEDGSNLEPVVGPNHLA--YVIYTSGTTGKPKGVM 7605
Cdd:PRK08276   83 GAKVLivsaaladtaaelaaELPAGVPLLLVVAG---PVPGFRSYEEALAAQPDTPIADETAgaDMLYSSGTTGRPKGIK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7606 VEHHGL-----CSLKLMFAETLRITEEDRVV-------QFASLSFDAScweifkALFFGATLYIPAK---DTILDypLFE 7670
Cdd:PRK08276  160 RPLPGLdpdeaPGMMLALLGFGMYGGPDSVYlspaplyHTAPLRFGMS------ALALGGTVVVMEKfdaEEALA--LIE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7671 SYMnengITAAILPPTYAIYLSpdRLP----------SLKKLITGGSAASVEFVQQ----WKDKVRYFnaYGPTEASIVT 7736
Cdd:PRK08276  232 RYR----VTHSQLVPTMFVRML--KLPeevrarydvsSLRVAIHAAAPCPVEVKRAmidwWGPIIHEY--YASSEGGGVT 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7737 svWAASPDGLDLR-SVpiGRPIANhQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDnpflagERMYR 7815
Cdd:PRK08276  304 --VITSEDWLAHPgSV--GKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNP------HGWVT 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7816 TGDLArWLPDGNIEYL-GRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDAN-GQQ-----QLCAYFVADRELT 7888
Cdd:PRK08276  373 VGDVG-YLDEDGYLYLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEmGERvkavvQPADGADAGDALA 451
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 386647928 7889 vSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:PRK08276  452 -AELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1935-2211 1.30e-24

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 111.04  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1935 LDRGKLEEAFRQLIARHETLRTGFeLVNGEpvQRVYKEVN---FAVEHYRTSEAEAGEV----VRGFV--RTFDLAKPPL 2005
Cdd:cd19535    37 LDPDRLERAWNKLIARHPMLRAVF-LDDGT--QQILPEVPwygITVHDLRGLSEEEAEAaleeLRERLshRVLDVERGPL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2006 LRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLY--NGESLATLRIQYKDYAVWQQSEEQLERvKRQEAYW--- 2080
Cdd:cd19535   114 FDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYedPGEPLPPLELSFRDYLLAEQALRETAY-ERARAYWqer 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2081 LDMFRG--ELPVLEMPTDYPRPAVRRfegstLSFRLDAGLNEALKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGT 2158
Cdd:cd19535   193 LPTLPPapQLPLAKDPEEIKEPRFTR-----REHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNL 267
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 2159 PIAGR--THGDLQPLIGMFVNT--LAIRnyPAGGKTFRSFLEEVKETTLGAYEHQTY 2211
Cdd:cd19535   268 TLFNRlpLHPDVNDVVGDFTSLllLEVD--GSEGQSFLERARRLQQQLWEDLDHSSY 322
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
273-757 1.33e-24

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 113.07  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  273 RPDAVAVTFEDRQ----LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEER 348
Cdd:PRK04319   57 RKDKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  349 IRYMLEDSGTQVLLSQGHLQER------------------VSFSGTWIRLDDEEAYHEDGSNLESVNgPEHLTYVIYTSG 410
Cdd:PRK04319  137 VRDRLEDSEAKVLITTPALLERkpaddlpslkhvllvgedVEEGPGTLDFNALMEQASDEFDIEWTD-REDGAILHYTSG 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  411 TTGKPKGNLTTHRNIIrvvknTNYIdvTGQdkllqlssYSFD-----------------GSTFDIFGALLNGAKLVLVPK 473
Cdd:PRK04319  216 STGKPKGVLHVHNAML-----QHYQ--TGK--------YVLDlheddvywctadpgwvtGTSYGIFAPWLNGATNVIDGG 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  474 EtvLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPD-----CLRHARAILFGGERVSVSHVR---KALGHlgpgkikhv 545
Cdd:PRK04319  281 R--FSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDlvkkyDLSSLRHILSVGEPLNPEVVRwgmKVFGL--------- 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  546 ygPTESTVFATsydvhevEEGAVSI------PI-----GGPISNTAIYIV-NAQNKLQPiGVAGELCV-AG-DGLARGYL 611
Cdd:PRK04319  350 --PIHDNWWMT-------ETGGIMIanypamDIkpgsmGKPLPGIEAAIVdDQGNELPP-NRMGNLAIkKGwPSMMRGIW 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  612 NRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-----V 686
Cdd:PRK04319  420 NNPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIgkpdpV 492
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  687 ResanGEkqLCAYYVADRS--LPANEVRSTLSQ----ELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETG 757
Cdd:PRK04319  493 R----GE--IIKAFVALRPgyEPSEELKEEIRGfvkkGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELGLPEG 563
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
260-738 1.35e-24

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 113.43  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  260 TTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGA--- 336
Cdd:PRK08279   37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  337 --------------------YVPIDPEYPE--ERIRYMLEDSGTQVLLSQGHLQERvsfsGTWIRLDDEEAYHEDGsNLE 394
Cdd:PRK08279  117 lntqqrgavlahslnlvdakHLIVGEELVEafEEARADLARPPRLWVAGGDTLDDP----EGYEDLAAAAAGAPTT-NPA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  395 SVNG--PEHLTYVIYTSGTTGKPKGNLTTHRniiRVVKNTNY----IDVTGQDKL-LQLSSYSFDGSTFDIFGALLNGAK 467
Cdd:PRK08279  192 SRSGvtAKDTAFYIYTSGTTGLPKAAVMSHM---RWLKAMGGfgglLRLTPDDVLyCCLPLYHNTGGTVAWSSVLAAGAT 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  468 LVLVPKetvldvaklagliekqqisvmFITTAFFnvlvdmnPDCLRHaRAILFG--GE--RVSVS----------HVRKA 533
Cdd:PRK08279  269 LALRRK---------------------FSASRFW-------DDVRRY-RATAFQyiGElcRYLLNqppkptdrdhRLRLM 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  534 LGH-LGPG---------KIKHV---YGPTESTVfaTSYDVHEVeEGAVSIPIGGPISNTAI---------YIVNAQNKLQ 591
Cdd:PRK08279  320 IGNgLRPDiwdefqqrfGIPRIlefYAASEGNV--GFINVFNF-DGTVGRVPLWLAHPYAIvkydvdtgePVRDADGRCI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  592 PIGvAGElcvAGDGLAR--------GYlNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFR 663
Cdd:PRK08279  397 KVK-PGE---VGLLIGRitdrgpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGEN 471
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  664 IELGEIEAHLLKLEAIEKATV--VVRESANGEKQLCAYYVAD-RSLPANEVRSTLSQELPAYMLPsYFVQLEQMPLTT 738
Cdd:PRK08279  472 VATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADgAEFDLAALAAHLYERLPAYAVP-LFVRLVPELETT 548
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
7446-7928 1.40e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 112.93  E-value: 1.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7446 QTIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYV 7524
Cdd:PRK05677   24 PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7525 PIDPEYPEDRIRYMLEDSGAQVLL---TQRHLQECV-------------------SFDGKVIAA---------------- 7566
Cdd:PRK05677  104 NTNPLYTAREMEHQFNDSGAKALVclaNMAHLAEKVlpktgvkhvivtevadmlpPLKRLLINAvvkhvkkmvpayhlpq 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7567 ----DDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCS----LKLMFAETLritEEDRVVQFASLSF 7638
Cdd:PRK05677  184 avkfNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqCRALMGSNL---NEGCEILIAPLPL 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7639 dascWEIFKALFFGATLYIPAKDTIL-----DYPLFESYMNENGITAAILPPTYAIYLSPDR------LPSLKKLITGGS 7707
Cdd:PRK05677  261 ----YHIYAFTFHCMAMMLIGNHNILisnprDLPAMVKELGKWKFSGFVGLNTLFVALCNNEafrkldFSALKLTLSGGM 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7708 AASVEFVQQWKD--KVRYFNAYGPTEASIVTSVwaASPDGLDLRSvpIGRPIANHQIFIVDSQNHMLPVGVAGELCISGA 7785
Cdd:PRK05677  337 ALQLATAERWKEvtGCAICEGYGMTETSPVVSV--NPSQAIQVGT--IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7786 GLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIV 7865
Cdd:PRK05677  413 QVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAA 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 7866 IARGDANGQQQLCAYFVA--DRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK05677  487 IGVPDEKSGEAIKVFVVVkpGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
PRK07514 PRK07514
malonyl-CoA synthase; Validated
3857-4337 1.49e-24

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 112.28  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3857 HGLFE--EQALRNPDAVAV-VFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIP 3933
Cdd:PRK07514    3 NNLFDalRAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3934 IDPEYPEDRIRYMLEDSGAQALLTQ-------RHLRERVSFAGTFVAVDD------EQAYHAdGSNLEPVV-GPNHLAYV 3999
Cdd:PRK07514   83 LNTAYTLAELDYFIGDAEPALVVCDpanfawlSKIAAAAGAPHVETLDADgtgsllEAAAAA-PDDFETVPrGADDLAAI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4000 IYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDR------------------VVQFASLS------FDAScwEIFK 4055
Cdd:PRK07514  162 LYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVlihalpifhthglfvatnVALLAGASmiflpkFDPD--AVLA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4056 ALffgatlyiPTSTTILDYPLFESYMNENgitatilpptyaAYLNPD---RMpslkKLITGGSAA-SVEFVQQWKDK--- 4128
Cdd:PRK07514  240 LM--------PRATVMMGVPTFYTRLLQE------------PRLTREaaaHM----RLFISGSAPlLAETHREFQERtgh 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4129 -VLyfNAYGPTEASIVTSiwdeaSDSLGDRKSVPIGRPLANHRIYVVDSHN-RMLPVGVAGELCISGVGLARGYLNRPEL 4206
Cdd:PRK07514  296 aIL--ERYGMTETNMNTS-----NPYDGERRAGTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEK 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4207 TAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQL 4286
Cdd:PRK07514  369 TAEEFRADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGV 442
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 4287 VAYFVAQR--ELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK07514  443 TAVVVPKPgaALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
3884-4337 1.51e-24

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 112.56  E-value: 1.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3884 ELNERANRLARTLRDA-GVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHLR 3962
Cdd:cd05928    46 ELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3963 ERV-------------------------SFAGTFVAVDDEQAYHADGSNlEPVVgpnhlayVIYTSGTTGKPKgvMVEH- 4016
Cdd:cd05928   126 PEVdsvasecpslktkllvseksrdgwlNFKELLNEASTEHHCVETGSQ-EPMA-------IYFTSGTTGSPK--MAEHs 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4017 HGLCSLKLmFANT---LQMTEQDRVVQFASLSF-DASCWEIFKALFFGATLYIPT-----STTILD----YPlfesymne 4083
Cdd:cd05928   196 HSSLGLGL-KVNGrywLDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGACVFVHHlprfdPLVILKtlssYP-------- 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4084 ngITATILPPT-YAAYLNPD----RMPSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTsiwdeasdslGD 4156
Cdd:cd05928   267 --ITTFCGAPTvYRMLVQQDlssyKFPSLQHCVTGGEPLNPEVLEKWKAQtgLDIYEGYGQTETGLIC----------AN 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4157 RKSVPI-----GRPLANHRIYVVDSHNRMLPVGVAGELCIS-----GVGLARGYLNRPELTAEKFVDNpfepgerMYRTG 4226
Cdd:cd05928   335 FKGMKIkpgsmGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAATIRGD-------FYLTG 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4227 DLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV--------AQRELTa 4298
Cdd:cd05928   408 DRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqflshDPEQLT- 486
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928 4299 AELRATMSQELPNYMIPSY--FVQlaQMPLTPNGKIDRKAL 4337
Cdd:cd05928   487 KELQQHVKSVTAPYKYPRKveFVQ--ELPKTVTGKIQRNEL 525
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
2362-2823 1.65e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 111.92  E-value: 1.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2362 PAVV--FEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLE 2439
Cdd:PRK08276    1 PAVImaPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2440 DSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYAGDG--------SNLESAVGPNDLA------YIIYTSGTTGKPKGV-- 2503
Cdd:PRK08276   81 DSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGpvpgfrsyEEALAAQPDTPIAdetagaDMLYSSGTTGRPKGIkr 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2504 -MVEHHGLCSLKQM---FANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTK---ETILDYqwFERYMsdng 2576
Cdd:PRK08276  161 pLPGLDPDEAPGMMlalLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKfdaEEALAL--IERYR---- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2577 ITTATLPPTYAVYL--NPDH------MPDFKRLIAAGSASSLELLQQ----WKDKV-KYfnaYGPTEDSICTTIwtpSTE 2643
Cdd:PRK08276  235 VTHSQLVPTMFVRMlkLPEEvrarydVSSLRVAIHAAAPCPVEVKRAmidwWGPIIhEY---YASSEGGGVTVI---TSE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2644 D-ISQLKSVpiGGPIVNhRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfepgERMYRTGDLAkW 2722
Cdd:PRK08276  309 DwLAHPGSV--GKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNP------HGWVTVGDVG-Y 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2723 L-PDGtieYL---GRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVI-AHDDASGQK-----QLCAYFVADRTMTvGEL 2792
Cdd:PRK08276  379 LdEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgVPDEEMGERvkavvQPADGADAGDALA-AEL 454
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 2793 RGELSGELPGYMIPAHFVQLERMPLTPNGKI 2823
Cdd:PRK08276  455 IAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1307-1795 1.73e-24

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 112.44  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 1386
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QFMLEDSAASVLLTQTHLQERA---QQWGQTLQAVLCLDD-------EAAYAEDA-SNVANVNEPHD-LAYVIYTSGTTG 1454
Cdd:PRK07470   97 AYLAEASGARAMICHADFPEHAaavRAASPDLTHVVAIGGaragldyEALVARHLgARVANAAVDHDdPCWFFFTSGTTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1455 RPKGVMIEHRSLvntaaGYRREYRL-DQFPV-----RLLQLASFSFDVFVG---DIARtlynGGTMVICPKDdRIDPARL 1525
Cdd:PRK07470  177 RPKAAVLTHGQM-----AFVITNHLaDLMPGtteqdASLVVAPLSHGAGIHqlcQVAR----GAATVLLPSE-RFDPAEV 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1526 HYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCsvtdYRVLQER----FGSqfRIINAYGVTEA--- 1598
Cdd:PRK07470  247 WALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPM----YRADQKRalakLGK--VLVQYFGLGEVtgn 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1599 -----AIDSSLYDEPLAKLPEAGNVPIGkaalnAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSP 1673
Cdd:PRK07470  321 itvlpPALHDAEDGPDARIGTCGFERTG-----MEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGW 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1674 FvegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESE 1753
Cdd:PRK07470  396 F-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDG 468
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 386647928 1754 LKLS--ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK07470  469 APVDeaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
855-1264 1.97e-24

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 110.08  E-value: 1.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  855 LSSAQKRLYILHQlegaeqSYNLPGvtllegALDRNRLEEAFRALIARHETLRTGI-EMVGGEPMQRIYPEVEFAVEHIR 933
Cdd:cd19545    14 LTARQPGAYVGQR------VFELPP------DIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPISWTEST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  934 ANEEEADAAVKQFIRAfdlaKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGEDLPAlRIQYKDY- 1012
Cdd:cd19545    82 SLDEYLEEDRAAPMGL----GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPFSRFv 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1013 -AVWQQSEAQKEQlkrqeaYWLEVFRGELPVL--EMPtdyaRPAVQSYAGNALRFELDAQKReglqriaSENGATLYMVL 1089
Cdd:cd19545   157 kYLRQLDDEAAAE------FWRSYLAGLDPAVfpPLP----SSRYQPRPDATLEHSISLPSS-------ASSGVTLATVL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1090 LAAYTILLQKYTGQEDVVIGTPIAGRTH---GDLHpLIGMFVNTLAIRNYPAADKTFLSYLEDVKETTLgaferQDYPFE 1166
Cdd:cd19545   220 RAAWALVLSRYTGSDDVVFGVTLSGRNApvpGIEQ-IVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLL-----DMIPFE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1167 E--LVDKLKLARDLSRNPLFDTMFTLQN---TENKEFRLPGLQLTPYPVEEHTSkFDLSLDIMESGDGFLCGIEYATALY 1241
Cdd:cd19545   294 HtgLQNIRRLGPDARAACNFQTLLVVQPalpSSTSESLELGIEEESEDLEDFSS-YGLTLECQLSGSGLRVRARYDSSVI 372
                         410       420
                  ....*....|....*....|...
gi 386647928 1242 KRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19545   373 SEEQVERLLDQFEHVLQQLASAP 395
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
2341-2828 2.12e-24

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 112.01  E-value: 2.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2341 YEADKTIHQLFEEQAEriPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGg 2420
Cdd:PRK10946   21 YWQDLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2421 aYVPIDPEYPEDR---ISYMLE-----------------DSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYAGDGSNLES 2480
Cdd:PRK10946   98 -VAPVNALFSHQRselNAYASQiepalliadrqhalfsdDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPAEDFTA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2481 AVGPND-LAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQF--ASLSFDASCWEVFQTLFFGATLYI- 2556
Cdd:PRK10946  177 TPSPADeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTVVLa 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2557 PTKETILDYQWFERYMSDngiTTATLPPTYAVYLNPDHMPDFK------RLIAAGSAS---SL------EL---LQQwkd 2618
Cdd:PRK10946  257 PDPSATLCFPLIEKHQVN---VTALVPPAVSLWLQAIAEGGSRaqlaslKLLQVGGARlseTLarripaELgcqLQQ--- 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2619 kvkyfnAYGPTEDSICTTIWTPSTEDISQLKSVPIGGpivNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLT 2698
Cdd:PRK10946  331 ------VFGMAEGLVNYTRLDDSDERIFTTQGRPMSP---DDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHN 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2699 AEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASV-QEAIVIAHDDASGQKQl 2777
Cdd:PRK10946  402 ASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAViHAALVSMEDELMGEKS- 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 2778 CAYFVADRTMTVGELRGELSGE-LPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK10946  475 CAFLVVKEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK07514 PRK07514
malonyl-CoA synthase; Validated
7449-7928 2.19e-24

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 111.89  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7449 HGLFEEQAERMPEKAAVVFENTQ---LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVP 7525
Cdd:PRK07514    3 NNLFDALRAAFADRDAPFIETPDglrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7526 IDPEYPEDRIRYMLEDSGAQVLLTQRHLQECVSfdgkVIAADDEQAY----GEDGS------------NLEPVV-GPNHL 7588
Cdd:PRK07514   83 LNTAYTLAELDYFIGDAEPALVVCDPANFAWLS----KIAAAAGAPHvetlDADGTgslleaaaaapdDFETVPrGADDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7589 AYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQfaslsfdasCWEIFK----------ALFFGATLYIP 7658
Cdd:PRK07514  159 AAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIH---------ALPIFHthglfvatnvALLAGASMIFL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7659 AK---DTILDY-PLFESYMnenGItaailpPTYAIYLSPDrlPSLKK-------LITGGSAA-SVEFVQQWKDKV--RYF 7724
Cdd:PRK07514  230 PKfdpDAVLALmPRATVMM---GV------PTFYTRLLQE--PRLTReaaahmrLFISGSAPlLAETHREFQERTghAIL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7725 NAYGPTEASIVTSvwaaSP-DGlDLRSVPIGRPIANHQIFIVDSQN-HMLPVGVAGELCISGAGLARGYLNRPELTAEKF 7802
Cdd:PRK07514  299 ERYGMTETNMNTS----NPyDG-ERRAGTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7803 VDNPFlagermYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV 7882
Cdd:PRK07514  374 RADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVV 447
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 7883 ADR--ELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK07514  448 PKPgaALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
3999-4332 2.21e-24

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 108.36  E-value: 2.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3999 VIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDR--VVQ--FASLSFDASCweiFKALFFGATLYiptSTTILDY 4074
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRylIINpfFHTFGYKAGI---VACLLTGATVV---PVAVFDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4075 PLFESYMNENGITATILPPT-YAAYLN-PDR----MPSLKKLITGGSAASVEFVQQWKDKVLYFN---AYGPTEASIVTS 4145
Cdd:cd17638    79 DAILEAIERERITVLPGPPTlFQSLLDhPGRkkfdLSSLRAAVTGAATVPVELVRRMRSELGFETvltAYGLTEAGVATM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4146 IwdEASDSLGDRKSVpIGRPLANHRIYVVDshnrmlpvgvAGELCISGVGLARGYLNRPELTAEKfVDnpfepGERMYRT 4225
Cdd:cd17638   159 C--RPGDDAETVATT-CGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEA-ID-----ADGWLHT 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4226 GDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRE--LTAAELRA 4303
Cdd:cd17638   220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvtLTEEDVIA 299
                         330       340
                  ....*....|....*....|....*....
gi 386647928 4304 TMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:cd17638   300 WCRERLANYKVPRFVRFLDELPRNASGKV 328
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
853-1134 2.38e-24

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 110.22  E-value: 2.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  853 YPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEgalDRNRLE---EAFRALIARHETLRTGI--EMVGgEPMQRIYPEVEF 927
Cdd:cd19544     2 YPLAPLQEGILFHHLLAEEGDPYLLRSLLAFD---SRARLDaflAALQQVIDRHDILRTAIlwEGLS-EPVQVVWRQAEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  928 AVEHIRAneEEADAAVKQFIRAF-------DLAKPPLLRVGLIELAP-ERHLLMFDMHHIVSDGISMDVLVEEFARLYGG 999
Cdd:cd19544    78 PVEELTL--DPGDDALAQLRARFdprryrlDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQAILAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1000 E--DLPALrIQYKDYaVWQQSEAQKEQlkRQEAYwlevFRGELPVLEMPT-DYARPAVQSYAGNA--LRFELDAQKREGL 1074
Cdd:cd19544   156 RaaALPPP-VPYRNF-VAQARLGASQA--EHEAF----FREMLGDVDEPTaPFGLLDVQGDGSDIteARLALDAELAQRL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 1075 QRIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRTHG--DLHPLIGMFVNTLAIR 1134
Cdd:cd19544   228 RAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGgaGADRALGMFINTLPLR 289
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
7751-8022 2.72e-24

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 107.14  E-value: 2.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7751 VPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEY 7830
Cdd:COG3433    16 PPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7831 LGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIA----RGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIP 7906
Cdd:COG3433    96 GGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVlaalRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7907 SYFVQLEQMPLTPNGKIDRNALPAPEGSMQTGADFVEPRTP---VEAELARIWQEVLGIGP--ISVKDNFFELGGHSLRA 7981
Cdd:COG3433   176 SAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALEtalTEEELRADVAELLGVDPeeIDPDDNLFDLGLDSIRL 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 386647928 7982 TVLSSKVNKElNVNLPLRDIFRFPTVEALAQVIDGLEQEEH 8022
Cdd:COG3433   256 MQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK07529 PRK07529
AMP-binding domain protein; Validated
1289-1795 3.64e-24

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 112.36  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1289 AAPDAPENevFHALFEKQAERTPEVAAVVY--------ENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADL 1360
Cdd:PRK07529   19 AARDLPAS--TYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPET 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1361 LVgalAVW--KAGGAYVPLDPDYPSDRIQFMLEDSAASVLLT-----QTHLQERAQQW---GQTLQAVLCLD-------- 1422
Cdd:PRK07529   97 HF---ALWggEAAGIANPINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVlaaLPELRTVVEVDlarylpgp 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1423 --------------------DE-AAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 1481
Cdd:PRK07529  174 krlavplirrkaharildfdAElARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGP 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 FPVRLLQLASFS-FDVFVGDIArTLYNGGTMVI-CPKDDRIDPARLHYW--ISEEKITIFESTPALIIPFMDyVAEHGLD 1557
Cdd:PRK07529  254 GDTVFCGLPLFHvNALLVTGLA-PLARGAHVVLaTPQGYRGPGVIANFWkiVERYRINFLSGVPTVYAALLQ-VPVDGHD 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1558 MSSMELLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAIDSSLYdeplaklPEAGNVPIGKAAL-----NAKFYIV 1632
Cdd:PRK07529  332 ISSLRYALCGAAPLPVEVFRRFEAATG--VRIVEGYGLTEATCVSSVN-------PPDGERRIGSVGLrlpyqRVRVVIL 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1633 D---AHLNPVPVGVLGELCIGGIGVARGYLNrpeltEEKfvDSPFVEGERLYRTGDLARWMPDGNVDFIGRidnqAK--- 1706
Cdd:PRK07529  403 DdagRYLRDCAVDEVGVLCIAGPNVFSGYLE-----AAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGR----AKdli 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1707 IR-GYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFT--AESELKLSELRSSLSQELPG-YMIPSYFVQLEQL 1782
Cdd:PRK07529  472 IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQlkPGASATEAELLAFARDHIAErAAVPKHVRILDAL 551
                         570
                  ....*....|...
gi 386647928 1783 PLTANGKIDRKAL 1795
Cdd:PRK07529  552 PKTAVGKIFKPAL 564
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1322-1795 3.90e-24

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 113.48  E-value: 3.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRaQGVKPNQLVGILADRSAdllVGAL---AVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVL 1398
Cdd:PRK08633  641 ELSYGKALTGALALARLLK-RELKDEENVGILLPPSV---AGALanlALLLAGKVPVNLNYTASEAALKSAIEQAQIKTV 716
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1399 LTQTHLQERAQQWGQTLQavLCLDDEAAYAED--------------------------ASNVANVNePHDLAYVIYTSGT 1452
Cdd:PRK08633  717 ITSRKFLEKLKNKGFDLE--LPENVKVIYLEDlkakiskvdkltallaarllparllkRLYGPTFK-PDDTATIIFSSGS 793
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1453 TGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASF-SFDvFVGDIARTLYNGGTMVICPkdDRIDPARLHYWISE 1531
Cdd:PRK08633  794 EGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFhSFG-LTVTLWLPLLEGIKVVYHP--DPTDALGIAKLVAK 870
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1532 EKITIFESTPALiipFMDYVAE---HGLDMSSMELLITSSDSC--SVTDyrVLQERFGsqFRIINAYGVTEAAidsslyd 1606
Cdd:PRK08633  871 HRATILLGTPTF---LRLYLRNkklHPLMFASLRLVVAGAEKLkpEVAD--AFEEKFG--IRILEGYGATETS------- 936
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1607 ePLAKLpeagNVPIGKAALNAK-----------------FYIVDAH-LNPVPVGVLGELCIGGIGVARGYLNRPELTEEK 1668
Cdd:PRK08633  937 -PVASV----NLPDVLAADFKRqtgskegsvgmplpgvaVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEV 1011
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1669 FVDspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRE---DAKGQKVLC 1745
Cdd:PRK08633 1012 IKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAvpdEKKGEKLVV 1088
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928 1746 AYftAESELKLSELRSSLSQ-ELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK08633 1089 LH--TCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK06164 PRK06164
acyl-CoA synthetase; Validated
5932-6420 4.07e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 111.37  E-value: 4.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5932 PSDKTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGA 6011
Cdd:PRK06164    7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6012 YVPIDPDYPEDRIRYMLEDSGAKLLLVQGH-------------------------LLDRAS-------FADKLVNLndDG 6059
Cdd:PRK06164   87 VIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidfaailaavppdalpplraiaVVDDAAdatpapaPGARVQLF--AL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6060 AYHEDGSNLEPVNGPEHLTYVIYT-SGTTGRPKGVMVEHRNVVRlvkntnYVELNEQTHILQTGAVVFDASTF------- 6131
Cdd:PRK06164  165 PDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLR------HARAIARAYGYDPGAVLLAALPFcgvfgfs 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6132 EIWGALLNGGRLYVvrnETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQ--DSGMFAGLKtlIVG-GDVLSVPHINRV 6208
Cdd:PRK06164  239 TLLGALAGGAPLVC---EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTagERADFPSAR--LFGfASFAPALGELAA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6209 LREHAGLSIVNGYGPTENTTFSTTHTI-VGEQKEAVPIGKPIN-NSTAYIVDSKL-SLLPVGVWGELIVGGDGVARGYLN 6285
Cdd:PRK06164  314 LARARGVPLTGLYGSSEVQALVALQPAtDPVSVRIEGGGRPASpEARVRARDPQDgALLPDGESGEIEIRAPSLMRGYLD 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6286 RPELTAEKFVESSFlpgercYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATViVREDESG 6365
Cdd:PRK06164  394 NPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQV-VGATRDG 466
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6366 QKQLCAYFVAE--RELTIGELRAALSQELPNYMIPSHFVPLERMPLT--PNG-KIDRRAL 6420
Cdd:PRK06164  467 KTVPVAFVIPTdgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
6992-7413 4.09e-24

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 109.88  E-value: 4.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAGAYFEQMRFTVQGSLDAEQFARSWNDLVARHAILRTNFfSGPRGEPLQIVYrDKRIGFVyeD 7071
Cdd:cd19546     7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF-PGDGGDVHQRIL-DADAARP--E 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7072 LSHLPADERQasVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFETYEAYVQGDR 7151
Cdd:cd19546    83 LPVVPATEEE--LPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7152 PEQKAAP-AYSQYIEW-------LENQDSAAAS--AYWSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERM 7221
Cdd:cd19546   161 PERAPLPlQFADYALWerellagEDDRDSLIGDqiAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7222 NRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSgRPAEIPGIEEMIGLFINTIPVRVACQPEESFADVMGRMQE 7301
Cdd:cd19546   241 MEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLP-RDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVRE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7302 AALESGRYDFYPLYEIQTQSAQKQELINHLLVfeNYPMDEQVEQAGGDDSGT---LSITDVDV---AEHTNYNFTVTVFP 7375
Cdd:cd19546   320 AVREARRHQDVPFERLAELLALPPSADRHPVF--QVALDVRDDDNDPWDAPElpgLRTSPVPLgteAMELDLSLALTERR 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 386647928 7376 GDE-----IVVRFDYNSFVFERADMERLKGHLLHMLEQIVADP 7413
Cdd:cd19546   398 NDDgdpdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
PRK07638 PRK07638
acyl-CoA synthetase; Validated
4893-5385 4.53e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 110.64  E-value: 4.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4893 FEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQlVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 4972
Cdd:PRK07638    7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLEDSAASVLLTQTHLQER-AQQWGQTLQAALCLDDEAAYAEDASNVANVNepHDLAYVIYTSGTTGRPKGVMI 5051
Cdd:PRK07638   86 QDELKERLAISNADMIVTERYKLNDlPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQ--NAPFYMGFTSGSTGKPKAFLR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5052 EHRSLVNTAAGYRREYRLdQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTP 5131
Cdd:PRK07638  164 AQQSWLHSFDCNVHDFHM-KREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRK---FIPNQVLDKLETENISVMYTVP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 ALIIPFmdYVAEHGLDmsSMVLLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAgnvpIG 5211
Cdd:PRK07638  240 TMLESL--YKENRVIE--NKMKIISSGAKWEAEAKEKIKNIF-PYAKLYEFYGASELSFVTALVDEESERRPNS----VG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5212 KAALNAKFYIVDAHlnpvpvgvlGELCIGG-IGVArgylnrpelteekFVDSP-----FVEGERLYRTGDLARWMPDGNV 5285
Cdd:PRK07638  311 RPFHNVQVRICNEA---------GEEVQKGeIGTV-------------YVKSPqffmgYIIGGVLARELNADGWMTVRDV 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5286 DFI---------GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQK-VLCAHFTAESElklsELRSSLS 5354
Cdd:PRK07638  369 GYEdeegfiyivGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwGEKpVAIIKGSATKQ----QLKSFCL 444
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 5355 QELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK07638  445 QRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
PRK09274 PRK09274
peptide synthase; Provisional
7454-7839 4.85e-24

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 111.14  E-value: 4.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7454 EQAERMPEKAAVVF----------ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAY 7523
Cdd:PRK09274   14 RAAQERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7524 VPIDPEYPEDRIRYMLEDSGAQVLLTQ-----------------RHLqecVSFDGKVI---AADDEQAYGEDGSNLEPV- 7582
Cdd:PRK09274   94 VLVDPGMGIKNLKQCLAEAQPDAFIGIpkahlarrlfgwgkpsvRRL---VTVGGRLLwggTTLATLLRDGAAAPFPMAd 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7583 VGPNHLAYVIYTSGTTGKPKGVMVEHHglcslklMFAETLRITEEDRvvQFASLSFDASCWEIFkALF---FGATLYIPA 7659
Cdd:PRK09274  171 LAPDDMAAILFTSGSTGTPKGVVYTHG-------MFEAQIEALREDY--GIEPGEIDLPTFPLF-ALFgpaLGMTSVIPD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7660 KDtiLDYP-------LFESyMNENGITAAILPPTY----AIYL--SPDRLPSLKKLITGG---SAASVEFVQQW-KDKVR 7722
Cdd:PRK09274  241 MD--PTRPatvdpakLFAA-IERYGVTNLFGSPALlerlGRYGeaNGIKLPSLRRVISAGapvPIAVIERFRAMlPPDAE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7723 YFNAYGPTEASIVTSVwaASPDGLD-LRSVP-------IGRPIANHQIFIVD---------SQNHMLPVGVAGELCISGA 7785
Cdd:PRK09274  318 ILTPYGATEALPISSI--ESREILFaTRAATdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGP 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 7786 GLARGYLNRPELTAEKFVDNPflAGERMYRTGDLARWLPDGNIEYLGRIDHQVK 7839
Cdd:PRK09274  396 MVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
4882-5385 5.02e-24

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 111.05  E-value: 5.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4882 DAPENEAF-HALFEKQAECTPEAAAVVYEND-----RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGAL 4955
Cdd:cd05970    11 NVPENFNFaYDVVDAMAKEYPDKLALVWCDDageerIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4956 AVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLT------QTHLQERAQQWGQTLQAALCLDDE----AAYAEDASNVA 5025
Cdd:cd05970    91 ALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaedniPEEIEKAAPECPSKPKLVWVGDPVpegwIDFRKLIKNAS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5026 NVNEP---------HDLAYVIYTSGTTGRPKgvMIEHrslVNTaagyrreyrldqFPVRLLQLASFSFDVFVGD----IA 5092
Cdd:cd05970   171 PDFERptansypcgEDILLVYFSSGTTGMPK--MVEH---DFT------------YPLGHIVTAKYWQNVREGGlhltVA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5093 RT---------LYN---GGTMVICPKDDRIDPARLHYWISEEKITIFeSTPALIIPFMDYVAEHGLDMSSMVLLITSSDS 5160
Cdd:cd05970   234 DTgwgkavwgkIYGqwiAGAAVFVYDYDKFDPKALLEKLSKYGVTTF-CAPPTIYRFLIREDLSRYDLSSLRYCTTAGEA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5161 CSVTDYRVLQERFGSQFRiiNAYGVTEAAIDsslydepLAKLP--EAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELC 5238
Cdd:cd05970   313 LNPEVFNTFKEKTGIKLM--EGFGQTETTLT-------IATFPwmEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIV 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5239 IG-----GIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLArWM-PDGNVDFIGRIDNQAKIRGYRIETGEIETQLL 5312
Cdd:cd05970   384 IRtskgkPVGLFGGYYKDAEKTAEVWHDG-------YYHTGDAA-WMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALI 455
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5313 KAEGVREAVVVVREDAK-GQK-----VLCAHFTAESELKlSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05970   456 QHPAVLECAVTGVPDPIrGQVvkatiVLAKGYEPSEELK-KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
2338-2828 5.16e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 111.39  E-value: 5.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2338 AADYEADK--TIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQAlgvKTD-QP---VGLMLERSLEMVVG 2411
Cdd:PRK05677   15 AAEINPDEypNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQ---HTDlKPgdrIAVQLPNVLQYPVA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2412 MFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVL--------LAQRRLqERVSFAGTVVT-VDDEQ------------- 2469
Cdd:PRK05677   92 VFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALvclanmahLAEKVL-PKTGVKHVIVTeVADMLpplkrllinavvk 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2470 -------AY-------------AGDGSNL-ESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLcslkqmFANTLQINA--- 2525
Cdd:PRK05677  171 hvkkmvpAYhlpqavkfndalaKGAGQPVtEANPQADDVAVLQYTGGTTGVAKGAMLTHRNL------VANMLQCRAlmg 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2526 ----QDRVVQFASL------SFDASCweVFQTLFFGATLYIPTKETILDY-----QWfeRYMSDNGITTATLpptyAVYL 2590
Cdd:PRK05677  245 snlnEGCEILIAPLplyhiyAFTFHC--MAMMLIGNHNILISNPRDLPAMvkelgKW--KFSGFVGLNTLFV----ALCN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2591 NPDHMP-DFKRL---IAAGSASSLELLQQWKD--KVKYFNAYGPTEDSICTTIWTPSTEDISQlksvpIGGPIVNHRIYI 2664
Cdd:PRK05677  317 NEAFRKlDFSALkltLSGGMALQLATAERWKEvtGCAICEGYGMTETSPVVSVNPSQAIQVGT-----IGIPVPSTLCKV 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2665 VDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYR 2744
Cdd:PRK05677  392 IDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFN 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2745 IELGEIEEQLLKVASVQEAIVIA-HDDASGQKqlCAYFVADR---TMTVGELRGELSGELPGYMIPAHFVQLERMPLTPN 2820
Cdd:PRK05677  466 VYPNELEDVLAALPGVLQCAAIGvPDEKSGEA--IKVFVVVKpgeTLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNV 543

                  ....*...
gi 386647928 2821 GKIDRKAL 2828
Cdd:PRK05677  544 GKILRREL 551
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1303-1795 5.33e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 110.25  E-value: 5.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1303 FEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQlVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 1382
Cdd:PRK07638    7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLEDSAASVLLTQTHLQER-AQQWGQTLQAVLCLDDEAAYAEDASNVANVNepHDLAYVIYTSGTTGRPKGVMI 1461
Cdd:PRK07638   86 QDELKERLAISNADMIVTERYKLNDlPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQ--NAPFYMGFTSGSTGKPKAFLR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1462 EHRSLVNTAAGYRREYRLdQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTP 1541
Cdd:PRK07638  164 AQQSWLHSFDCNVHDFHM-KREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRK---FIPNQVLDKLETENISVMYTVP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 ALIIPFM--DYVAEHgldmssmELLITSSDScsvtDYRVLQ-ERFGSQF---RIINAYGVTEAAIDSSLYDEPLAKLPEA 1615
Cdd:PRK07638  240 TMLESLYkeNRVIEN-------KMKIISSGA----KWEAEAkEKIKNIFpyaKLYEFYGASELSFVTALVDEESERRPNS 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1616 gnvpIGKAALNAKFYIVDAHlnpvpvgvlGELCIGG-IGVArgylnrpelteekFVDSP-----FVEGERLYRTGDLARW 1689
Cdd:PRK07638  309 ----VGRPFHNVQVRICNEA---------GEEVQKGeIGTV-------------YVKSPqffmgYIIGGVLARELNADGW 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1690 MPDGNVDFI---------GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKlsELR 1760
Cdd:PRK07638  363 MTVRDVGYEdeegfiyivGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQ--QLK 440
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 386647928 1761 SSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK07638  441 SFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
PRK08162 PRK08162
acyl-CoA synthetase; Validated
4894-5385 6.45e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 110.81  E-value: 6.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4894 EKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 4973
Cdd:PRK08162   25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4974 DRIQFMLEDSAASVLLTQThlqeraqQWGQTLQAALCL----------DDEAAYAEDA--------SNVANVNE------ 5029
Cdd:PRK08162  105 ASIAFMLRHGEAKVLIVDT-------EFAEVAREALALlpgpkplvidVDDPEYPGGRfigaldyeAFLASGDPdfawtl 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 PHDLAYVI---YTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFD--VFVGDIARtlyNGGTMViC 5104
Cdd:PRK08162  178 PADEWDAIalnYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNgwCFPWTVAA---RAGTNV-C 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5105 PKddRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTdyrVLQ--ERFGsqFRIINA 5182
Cdd:PRK08162  254 LR--KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAA---VIAkmEEIG--FDLTHV 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5183 YGVTEAAIDSSLydepLAKLPEAGNVPIG-KAALNAK----FYIVDA-------HLNPVPVG--VLGELCIGGIGVARGY 5248
Cdd:PRK08162  327 YGLTETYGPATV----CAWQPEWDALPLDeRAQLKARqgvrYPLQEGvtvldpdTMQPVPADgeTIGEIMFRGNIVMKGY 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5249 LNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVdfigRIDNQAK---IRG-YRIETGEIETQLLKAEGVREAVVVV 5324
Cdd:PRK08162  403 LKNPKATEEAFAGGWF-------HTGDLAVLHPDGYI----KIKDRSKdiiISGgENISSIEVEDVLYRHPAVLVAAVVA 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 5325 REDAKGQKVLCAhFTaesELK------LSELRSSLSQELPGYMIPSYFVqLEQLPLTANGKIDRKAL 5385
Cdd:PRK08162  472 KPDPKWGEVPCA-FV---ELKdgasatEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
4912-5385 6.47e-24

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 112.71  E-value: 6.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRaQGVKPNQLVGILADRSAdllVGAL---AVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVL 4988
Cdd:PRK08633  641 ELSYGKALTGALALARLLK-RELKDEENVGILLPPSV---AGALanlALLLAGKVPVNLNYTASEAALKSAIEQAQIKTV 716
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4989 LTQTHLQERAQQWGQTLQAALclDDEAAYAED--------------------------ASNVANVNePHDLAYVIYTSGT 5042
Cdd:PRK08633  717 ITSRKFLEKLKNKGFDLELPE--NVKVIYLEDlkakiskvdkltallaarllparllkRLYGPTFK-PDDTATIIFSSGS 793
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5043 TGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASF-SFDvFVGDIARTLYNGGTMVICPkdDRIDPARLHYWISE 5121
Cdd:PRK08633  794 EGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFhSFG-LTVTLWLPLLEGIKVVYHP--DPTDALGIAKLVAK 870
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5122 EKITIFESTPALiipFMDYVAE---HGLDMSSMVLLITSSDSC--SVTDyrVLQERFGsqFRIINAYGVTEAAidsslyd 5196
Cdd:PRK08633  871 HRATILLGTPTF---LRLYLRNkklHPLMFASLRLVVAGAEKLkpEVAD--AFEEKFG--IRILEGYGATETS------- 936
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5197 ePLAKLpeagNVPIGKAALNAK-----------------FYIVDAH-LNPVPVGVLGELCIGGIGVARGYLNRPELTEEK 5258
Cdd:PRK08633  937 -PVASV----NLPDVLAADFKRqtgskegsvgmplpgvaVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEV 1011
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5259 FVDspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRE---DAKGQKVLC 5335
Cdd:PRK08633 1012 IKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAvpdEKKGEKLVV 1088
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928 5336 AHftAESELKLSELRSSLSQ-ELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK08633 1089 LH--TCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
5909-6420 6.53e-24

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 110.84  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5909 LEMITAEEKEHIQRVFNATeAKYPSDKTIHQLFEEQAERIPDHLAVT--FEDKQLTYGELNERANRLARTLRNAGVQPDQ 5986
Cdd:PLN02330    3 MEIQKQEDNEHIFRSRYPS-VPVPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5987 MVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLL--------VQGHLL-------DRASFADK 6051
Cdd:PLN02330   82 VVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVtndtnygkVKGLGLpvivlgeEKIEGAVN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6052 LVNLNDDGAYHEDGSNLEPVNGPEhLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVELNEQT-HILQTGAVVFdast 6130
Cdd:PLN02330  162 WKELLEAADRAGDTSDNEEILQTD-LCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIgQVVTLGLIPF---- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6131 FEIWG-------ALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTMWLTAPLY-----NQLSQQDSGMFAGLKTLIVGGD 6198
Cdd:PLN02330  237 FHIYGitgiccaTLRNKGKVVVMSR---FELRTFLNALITQEVSFAPIVPPIIlnlvkNPIVEEFDLSKLKLQAIMTAAA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6199 VLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTHtivGEQKEAVPIGKpiNNSTAYIV----------DSKLSLlPVGV 6268
Cdd:PLN02330  314 PLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTH---GDPEKGHGIAK--KNSVGFILpnlevkfidpDTGRSL-PKNT 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6269 WGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLK 6348
Cdd:PLN02330  388 PGELCVRSQCVMQGYYNNKEETDRTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLT 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6349 VASVKEATVIVREDESGQKQLCAYFVAERELTIGElraalsQELPNYMIPS----------HFVplERMPLTPNGKIDRR 6418
Cdd:PLN02330  462 HPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE------EDILNFVAANvahykkvrvvQFV--DSIPKSLSGKIMRR 533

                  ..
gi 386647928 6419 AL 6420
Cdd:PLN02330  534 LL 535
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3880-4341 7.28e-24

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 109.19  E-value: 7.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPidpeypedrirymledsgAQALLTQR 3959
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 HLRERVSFAGTFVAVDDEqAYHADgsnlEPVvgpnhLAYviYTSGTTGKPKgvMVEH----HGLCSLKLMFANTLQmtEQ 4035
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDE-NTHAD----DPM-----LLY--FTSGTTSKPK--LVEHthrsYPVGHLSTMYWIGLK--PG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4036 DRVVQFASLSFDASCWEIFKA-LFFGATLYIptsttiLDYPLFES-----YMNENGITATILPPTYAAYLNPDRMPS--- 4106
Cdd:cd05974   127 DVHWNISSPGWAKHAWSCFFApWNAGATVFL------FNYARFDAkrvlaALVRYGVTTLCAPPTVWRMLIQQDLASfdv 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4107 -LKKLITGGSAASVEFVQQ----WKDKVLyfNAYGPTEASIvtsiwdEASDSLGDR-KSVPIGRPLANHRIYVVDshnrm 4180
Cdd:cd05974   201 kLREVVGAGEPLNPEVIEQvrraWGLTIR--DGYGQTETTA------LVGNSPGQPvKAGSMGRPLPGYRVALLD----- 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4181 lPVGVA---GELCIS-----GVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGY 4252
Cdd:cd05974   268 -PDGAPateGEVALDlgdtrPVGLMKGYAGDPDKTAHAMRGG-------YYRTGDIAMRDEDGYLTYVGRADDVFKSSDY 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4253 RIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV------AQRELTAAELRATMSQELPNYMIPSyfVQLAQMPL 4326
Cdd:cd05974   340 RISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyePSPETALEIFRFSRERLAPYKRIRR--LEFAELPK 417
                         490
                  ....*....|....*
gi 386647928 4327 TPNGKIDRKALPAPE 4341
Cdd:cd05974   418 TISGKIRRVELRRRE 432
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
7587-7925 7.39e-24

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 106.72  E-value: 7.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7587 HLAYVIYTSGTTGKPKGVMVEHHglcSLKLMFAET---LRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIpakDTI 7663
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSER---SWIESFVCNedlFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7664 LDYPLFESYMNENGITAAILPPT--YAIYLSPDRLPSLKKLITGGSAASVE----FVQQWKDKVRYfNAYGPTEASIVTs 7737
Cdd:cd17633    75 FNPKSWIRKINQYNATVIYLVPTmlQALARTLEPESKIKSIFSSGQKLFEStkkkLKNIFPKANLI-EFYGTSELSFIT- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7738 vWAASPDGLDLRSVpiGRPIANHQIFIVDSQNhmlpvGVAGELCISGAGLARGYLNRPELTAEKFvdnpflagermYRTG 7817
Cdd:cd17633   153 -YNFNQESRPPNSV--GRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7818 DLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADrELTVSELRGTLS 7897
Cdd:cd17633   214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKRFLK 292
                         330       340
                  ....*....|....*....|....*...
gi 386647928 7898 QELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd17633   293 QKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
5525-5900 8.21e-24

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 108.88  E-value: 8.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5525 LDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEV--NFAVEHYRTSEAEAGEVVRGFV----RTFDLAKPPLLRV 5598
Cdd:cd19534    34 LDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVeeLFRLEVVDLSSLAQAAAIEALAaeaqSSLDLEEGPLLAA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5599 GLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMY----NGESLA-PLRIQYKDYATWQQSEAQQEQMKRQEAYWLDM 5673
Cdd:cd19534   114 ALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYeqalAGEPIPlPSKTSFQTWAELLAEYAQSPALLEELAYWREL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5674 FRGELPvlELPTDYPRpavrkFEGSLLQRQLEpkLGEG-----LQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGT 5748
Cdd:cd19534   194 PAADYW--GLPKDPEQ-----TYGDARTVSFT--LDEEetealLQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFL 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5749 PIAGR----THSDLQPIIGMFVNTLAIRSYPDDKKTFRSFLDEVKETM---------------LGAYEHQSYPFEELVE- 5808
Cdd:cd19534   265 EGHGReeidPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLrripnkgigygilryLTPEGTKRLAFHPQPEi 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5809 -------KAQPARDlsrnplfDTLFALQNKETGELQLDGLRLTpypaehtvAKFDLSVDVTEGSegLELSMEYSTALYTR 5881
Cdd:cd19534   345 sfnylgqFDQGERD-------DALFVSAVGGGGSDIGPDTPRF--------ALLDINAVVEGGQ--LVITVSYSRNMYHE 407
                         410
                  ....*....|....*....
gi 386647928 5882 ETIERMAKHFEQLLTAIVQ 5900
Cdd:cd19534   408 ETIQQLADSYKEALEALIE 426
PRK07470 PRK07470
acyl-CoA synthetase; Validated
5945-6420 8.27e-24

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 110.13  E-value: 8.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHLLD-----RASFADKLVNLNDDGAYHED----------GSNLEPVNgPEHLT--YVIYTSGTT 6087
Cdd:PRK07470   97 AYLAEASGARAMICHADFPEhaaavRAASPDLTHVVAIGGARAGLdyealvarhlGARVANAA-VDHDDpcWFFFTSGTT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6088 GRPKGVMVEHRNVVRLVKNtnyvelneqtHI--LQTGAVVFDAStfeIWGALLNGGR-----LYVVRN-ETIL------D 6153
Cdd:PRK07470  176 GRPKAAVLTHGQMAFVITN----------HLadLMPGTTEQDAS---LVVAPLSHGAgihqlCQVARGaATVLlpserfD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6154 AVSLKNAIQQYGINTMWlTAPLYNQLSQQDSGM----FAGLKTLIVGG-------DVLSVPHINRVLREHAGLSIVNGyg 6222
Cdd:PRK07470  243 PAEVWALVERHRVTNLF-TVPTILKMLVEHPAVdrydHSSLRYVIYAGapmyradQKRALAKLGKVLVQYFGLGEVTG-- 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6223 pteNTTFSTTHTIVGEQKEAVPIGK---PINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSF 6299
Cdd:PRK07470  320 ---NITVLPPALHDAEDGPDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6300 lpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVRED----ESGqkqlCAYFVA 6375
Cdd:PRK07470  397 -------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDpvwgEVG----VAVCVA 465
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 6376 eRE---LTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK07470  466 -RDgapVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
PRK05691 PRK05691
peptide synthase; Validated
8004-8373 8.47e-24

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 113.34  E-value: 8.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8004 FPtveaLAQvidgLEQEEHSAIPVIGER--EYYPVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLI 8081
Cdd:PRK05691 3234 FP----LAQ----LTQAQLDALPVPAAEieDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVV 3305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8082 ERHETLRTGFEMANGEP-VQRVYSDVEFAVEY------SKADREEAVEIAQRFVRP--FDLRKPPLLRVGLIEVEPERHI 8152
Cdd:PRK05691 3306 ARHEALRASFSWNAGETmLQVIHKPGRTPIDYldwrglPEDGQEQRLQALHKQEREagFDLLNQPPFHLRLIRVDEARYW 3385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8153 LMLDMHHIISDGASVGILQEEFSRLYA--GE----ELPPLRiQYKDYAAWQRSEAYAkrvkQQEGYWLQTLAGELPVIEL 8226
Cdd:PRK05691 3386 FMMSNHHILIDAWCRSLLMNDFFEIYTalGEgreaQLPVPP-RYRDYIGWLQRQDLA----QARQWWQDNLRGFERPTPI 3460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8227 PTDyeRTSTRSFEGAELEFEADEALTQ-------RLNELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGR--T 8297
Cdd:PRK05691 3461 PSD--RPFLREHAGDSGGMVVGDCYTRldaadgaRLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvS 3538
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 8298 HADVEPIIGMFVNTLAIR-NYPAGDK--TFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDasrNPVFDTMFVLQN 8373
Cdd:PRK05691 3539 MPQMQRTVGLFINSIALRvQLPAAGQrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKG---QPLFDSLFVFEN 3614
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2371-2828 9.30e-24

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 108.76  E-value: 9.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVllaqr 2450
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARL----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2451 rlqervsfagtVVTVDDEQAYAGDGSNLEsavgpndlayiIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRvv 2530
Cdd:cd05973    76 -----------VVTDAANRHKLDSDPFVM-----------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS-- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2531 qFASLSFDASCWEVFQTLFFGATLYIPtkeTILDYQWFE-----RYMSDNGITTATLPPTYavylnpdhmpdFKRLIAAG 2605
Cdd:cd05973   132 -FWNAADPGWAYGLYYAITGPLALGHP---TILLEGGFSvestwRVIERLGVTNLAGSPTA-----------YRLLMAAG 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2606 SASSLELLQQWK-----------DKVKYFNA---------YGPTE-DSICTTIWTPSTEdisqLKSVPIGGPIVNHRIYI 2664
Cdd:cd05973   197 AEVPARPKGRLRrvssagepltpEVIRWFDAalgvpihdhYGQTElGMVLANHHALEHP----VHAGSAGRAMPGWRVAV 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2665 VDAHYQPVPVGVAGELCI--AGVGLA--RGYLNRPDLTaekfvdnpfePGERMYRTGDLAKWLPDGTIEYLGRIDHQVKI 2740
Cdd:cd05973   273 LDDDGDELGPGEPGRLAIdiANSPLMwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITM 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2741 RGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV-ADRTMTVGELRGELS----GELPGYMIP--AHFVqlE 2813
Cdd:cd05973   343 SGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlRGGHEGTPALADELQlhvkKRLSAHAYPrtIHFV--D 420
                         490
                  ....*....|....*
gi 386647928 2814 RMPLTPNGKIDRKAL 2828
Cdd:cd05973   421 ELPKTPSGKIQRFLL 435
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1288-1793 9.37e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 110.47  E-value: 9.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1288 PAAPDAPENEVFHaLFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAV 1367
Cdd:PRK05605   24 PHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1368 WKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL-------TQTHLQE-----------------RAQQWG----------- 1412
Cdd:PRK05605  103 LRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdkvapTVERLRRttpletivsvnmiaampLLQRLAlrlpipalrka 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1413 ---------QTLQAVLCLDDEAAYAEDASNVANVnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA---------GYR 1474
Cdd:PRK05605  183 raaltgpapGTVPWETLVDAAIGGDGSDVSHPRP-TPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkawvpglGDG 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1475 REYRLDQFPVrllqlasfsFDVFVGDIARTL--YNGGTMVICPkddRIDPARLHYWISEEKITIFESTPALIIPFMDYVA 1552
Cdd:PRK05605  262 PERVLAALPM---------FHAYGLTLCLTLavSIGGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAE 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1553 EHGLDMSSMELLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAidsslydePLAklpeAGNvPIGKAAL------- 1625
Cdd:PRK05605  330 ERGVDLSGVRNAFSGAMALPVSTVELWEKLTGG--LLVEGYGLTETS--------PII----VGN-PMSDDRRpgyvgvp 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1626 --NAKFYIVDAHlNP---VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGR 1700
Cdd:PRK05605  395 fpDTEVRIVDPE-DPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDR 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1701 IDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSE--LRSSLSQELPGYMIPSYFVQ 1778
Cdd:PRK05605  467 IKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYH 546
                         570
                  ....*....|....*
gi 386647928 1779 LEQLPLTANGKIDRK 1793
Cdd:PRK05605  547 VDELPRDQLGKVRRR 561
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
7437-7930 1.07e-23

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 111.28  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7437 NTAAEYAREQTIHGLFEEQAERMPEkaaVVfentqlTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAI 7516
Cdd:PRK06060    5 NLAGLLAEQASEAGWYDRPAFYAAD---VV------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLAC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7517 MKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIAAD-DEQAYGEDGSNLEPVVGpNHLAYVIYTS 7595
Cdd:PRK06060   76 LARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAElMSEAARVAPGGYEPMGG-DALAYATYTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7596 GTTGKPKGVMVEHHGLCS-LKLMFAETLRITEEDRVVQFASLSFdascweifkALFFGATLYIP--AKDTILDYPLFESY 7672
Cdd:PRK06060  155 GTTGPPKAAIHRHADPLTfVDAMCRKALRLTPEDTGLCSARMYF---------AYGLGNSVWFPlaTGGSAVINSAPVTP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 MNENGITAAILP------PTYAIYL----SPDRLPSLKKLITGGSAASV---EFVQQWKDKVRYFNAYGPTEASivTSVW 7739
Cdd:PRK06060  226 EAAAILSARFGPsvlygvPNFFARVidscSPDSFRSLRCVVSAGEALELglaERLMEFFGGIPILDGIGSTEVG--QTFV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7740 AASPDglDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPEltaekfvdnPFLAGERMYRTGDL 7819
Cdd:PRK06060  304 SNRVD--EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDR 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7820 ARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADR-----ELTVSELRG 7894
Cdd:PRK06060  373 VCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgatidGSVMRDLHR 452
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 7895 TLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPA 7930
Cdd:PRK06060  453 GLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
5930-6420 1.12e-23

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 110.14  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5930 KYPSdktIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKA 6008
Cdd:PRK08974   21 RYQS---LVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6009 GGAYVPIDPDYPEDRIRYMLEDSGAKLLLV------------------------QGHLLDRAS---------FADKLV-- 6053
Cdd:PRK08974   98 GMIVVNVNPLYTPRELEHQLNDSGAKAIVIvsnfahtlekvvfktpvkhviltrMGDQLSTAKgtlvnfvvkYIKRLVpk 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6054 -NLNDDGAYHEDGSN------LEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVVrlvkntnyvelneqTHILQTGAvvf 6126
Cdd:PRK08974  178 yHLPDAISFRSALHKgrrmqyVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNML--------------ANLEQAKA--- 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6127 dastfeIWGALLNGGRLYVV-----------------------RNETIL---DAVSLKNAIQQY------GINTM---WL 6171
Cdd:PRK08974  241 ------AYGPLLHPGKELVVtalplyhifaltvncllfielggQNLLITnprDIPGFVKELKKYpftaitGVNTLfnaLL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6172 TAPLYNQLSqqdsgmFAGLKtLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTENTTFST--THTIVGEQKEavpIGKPI 6249
Cdd:PRK08974  315 NNEEFQELD------FSSLK-LSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSvnPYDLDYYSGS---IGLPV 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6250 NNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEkFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQ 6329
Cdd:PRK08974  385 PSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWL------ATGDIAVMDEEGFLRIVDRKKDM 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6330 VKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGqkQLCAYFVAERE--LTIGELRAALSQELPNYMIPSHFVPLER 6406
Cdd:PRK08974  458 ILVSGFNVYPNEIEDVVMLHPKVLEVAAVgVPSEVSG--EAVKIFVVKKDpsLTEEELITHCRRHLTGYKVPKLVEFRDE 535
                         570
                  ....*....|....
gi 386647928 6407 MPLTPNGKIDRRAL 6420
Cdd:PRK08974  536 LPKSNVGKILRREL 549
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7590-7924 1.30e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 107.08  E-value: 1.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7590 YVIYTSGTTGKPKGVMVEHHGLCSLK-----LMFAETLRITEEDRV-VQFASLSFDASC--------WEIFKALFFGATL 7655
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIFRMLmggadFGTGEFTPSEDAHKAaAAAAGTVMFPAPplmhgtgsWTAFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7656 YIPakDTILD-YPLFESYMNENGITAAILPPTYAIYL-------SPDRLPSLKKLITGGSAASVEFVQQWKDKVRY---F 7724
Cdd:cd05924    87 VLP--DDRFDpEEVWRTIEKHKVTSMTIVGDAMARPLidalrdaGPYDLSSLFAISSGGALLSPEVKQGLLELVPNitlV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7725 NAYGPTEASIVTSVWAASpdgldlrSVPIGRP--IANHQIFIVDSQNHMLPVGVAGELCISGAGL-ARGYLNRPELTAEK 7801
Cdd:cd05924   165 DAFGSSETGFTGSGHSAG-------SGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAET 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7802 FvdnPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYF 7881
Cdd:cd05924   238 F---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVV 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 7882 VADR--ELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKID 7924
Cdd:cd05924   315 QLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
7451-7928 1.38e-23

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 109.72  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY 7530
Cdd:PRK07059   28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRIRYMLEDSGAQVL---------LTQ-------RH--------------------------------LQECVSFdGK 7562
Cdd:PRK07059  108 TPRELEHQLKDSGAEAIvvlenfattVQQvlaktavKHvvvasmgdllgfkghivnfvvrrvkkmvpawsLPGHVRF-ND 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7563 VIAAddeqayGEdGSNLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLR--ITEEDRVVQFASLsfd 7639
Cdd:PRK07059  187 ALAE------GA-RQTFKPVkLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpaFEKKPRPDQLNFV--- 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7640 asC----WEIFkALFF---------GATLYIP------------AKDTILDYP----LFESYMNengitaailpptyaiy 7690
Cdd:PRK07059  257 --CalplYHIF-ALTVcgllgmrtgGRNILIPnprdipgfikelKKYQVHIFPavntLYNALLN---------------- 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7691 lSPD-RLPSLKKLIT---GGSAASVEFVQQWKDKVRYF--NAYGPTEASIVTSvwaASPDGLDLRSVPIGRPIANHQIFI 7764
Cdd:PRK07059  318 -NPDfDKLDFSKLIVangGGMAVQRPVAERWLEMTGCPitEGYGLSETSPVAT---CNPVDATEFSGTIGLPLPSTEVSI 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7765 VDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermYRTGDLARWLPDGNIEYLGRIDHQVKIRGYR 7844
Cdd:PRK07059  394 RDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFN 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7845 IELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV-ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:PRK07059  468 VYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVkKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKI 547

                  ....*
gi 386647928 7924 DRNAL 7928
Cdd:PRK07059  548 LRREL 552
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5030-5381 1.45e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 106.70  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 PHDLaYVIYTSGTTGRPKGVMiehrslvntaagyrreYRLDQFPVRLLQLASFSFDVFVGDI------------------ 5091
Cdd:cd05924     3 ADDL-YILYTGGTTGMPKGVM----------------WRQEDIFRMLMGGADFGTGEFTPSEdahkaaaaaagtvmfpap 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5092 ----------ARTLYNGGTMVICPkDDRIDPARLHYWISEEKIT-IFESTPALIIPFMD-YVAEHGLDMSSMVLLITSSD 5159
Cdd:cd05924    66 plmhgtgswtAFGGLLGGQTVVLP-DDRFDPEEVWRTIEKHKVTsMTIVGDAMARPLIDaLRDAGPYDLSSLFAISSGGA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5160 SCSVTDYRVLQERFgSQFRIINAYGVTEAAIDSSLYdePLAKLPEAGNvpigKAALNAKFYIVDAHLNPVPVGVLGELCI 5239
Cdd:cd05924   145 LLSPEVKQGLLELV-PNITLVDAFGSSETGFTGSGH--SAGSGPETGP----FTRANPDTVVLDDDGRVVPPGSGGVGWI 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5240 GGIG-VARGYLNRPELTEEKFvdsPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVR 5318
Cdd:cd05924   218 ARRGhIPLGYYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVY 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 5319 EAVVVVREDAK-GQKVLC-AHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKID 5381
Cdd:cd05924   295 DVLVVGRPDERwGQEVVAvVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
5526-5901 1.46e-23

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 107.91  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5526 DRGKLE---EAFRQLIARHETLRTGFeLVNG--EPVQRVYKEVNFAVEHYRTSEAE-AGEVVRGFV----RTFDLAKPPL 5595
Cdd:cd19544    34 SRARLDaflAALQQVIDRHDILRTAI-LWEGlsEPVQVVWRQAELPVEELTLDPGDdALAQLRARFdprrYRLDLRQAPL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5596 LRVGLVE-LAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMYNGE--SLAPLrIQYKDY-ATWQQSEAQQEqmkrQEAYwl 5671
Cdd:cd19544   113 LRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRaaALPPP-VPYRNFvAQARLGASQAE----HEAF-- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5672 dmFRGELPVLELPTdYPrpavrkF-------EGSLLQ---RQLEPKLGEGLQRIAAESGATLYMVLLAAYKVLLQKYTGQ 5741
Cdd:cd19544   186 --FREMLGDVDEPT-AP------FglldvqgDGSDITearLALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGR 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5742 EDIVVGTPIAGRTH--SDLQPIIGMFVNTLAIRSYPDDkktfRSFLDEVKET-----MLGAYEHQSypfeeLVEkAQPAR 5814
Cdd:cd19544   257 DDVVFGTVLSGRMQggAGADRALGMFINTLPLRVRLGG----RSVREAVRQTharlaELLRHEHAS-----LAL-AQRCS 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5815 DLSRN-PLFDTLF-----ALQNKETGELQLDGLRL------TPYPaehtvakFDLSVDvtEGSEGLELSMEYSTALytre 5882
Cdd:cd19544   327 GVPAPtPLFSALLnyrhsAAAAAAAALAAWEGIELlggeerTNYP-------LTLSVD--DLGDGFSLTAQVVAPI---- 393
                         410
                  ....*....|....*....
gi 386647928 5883 TIERMAKHFEQLLTAIVQA 5901
Cdd:cd19544   394 DAERVCAYMETALEQLVDA 412
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1299-1798 1.51e-23

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 108.54  E-value: 1.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1299 FHALFEKQAERTPEVAAVVYENDR-LTYRELNERANRLARMLRAQGvkpnqLVGILADRSADLLVGALAVWKAGGAYVPL 1377
Cdd:PRK07787    1 LASLNPAAVAAAADIADAVRIGGRvLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1378 DPDYPSDRIQFMLEDSAASVLLTqthlqeRAQQWGQTLQAV---LCLDDEAAYAEDAsnvanvnePHDLAYVIYTSGTTG 1454
Cdd:PRK07787   76 PPDSGVAERRHILADSGAQAWLG------PAPDDPAGLPHVpvrLHARSWHRYPEPD--------PDAPALIVYTSGTTG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1455 RPKGVMIEHRSLVNT------AAGYRRE----YRLDQFPV---------------RLLQLASFSFDVFvgdiARTLYNGG 1509
Cdd:PRK07787  142 PPKGVVLSRRAIAADldalaeAWQWTADdvlvHGLPLFHVhglvlgvlgplrignRFVHTGRPTPEAY----AQALSEGG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1510 TMVI-CPkddridparlhywiseekiTIFESTPAliipfmdyVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSqfR 1588
Cdd:PRK07787  218 TLYFgVP-------------------TVWSRIAA--------DPEAARALRGARLLVSGSAALPVPVFDRLAALTGH--R 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1589 IINAYGVTEAAID-SSLYDEPlaklPEAGNVpiGKAALNAKFYIVDAHLNPVPVGV--LGELCIGGIGVARGYLNRPELT 1665
Cdd:PRK07787  269 PVERYGMTETLITlSTRADGE----RRPGWV--GLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDAT 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1666 EEKFVDSPFvegerlYRTGDLARWMPDGNVDFIGRidnQA----KIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-G 1740
Cdd:PRK07787  343 AAAFTADGW------FRTGDVAVVDPDGMHRIVGR---EStdliKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDlG 413
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 1741 QKVLcAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 1798
Cdd:PRK07787  414 QRIV-AYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
276-747 1.73e-23

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 107.95  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  276 AVAVTFEDRQLTYGELNERANRLARTLRNAGVQA-DQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLE 354
Cdd:cd05958     1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  355 DSGTQVLLsqghlqervsfsgtwirLDDEEAYHEDGSNLEsvngpehltyviYTSGTTGKPKGNLTTHRNIIRVVK--NT 432
Cdd:cd05958    81 KARITVAL-----------------CAHALTASDDICILA------------FTSGTTGAPKATMHFHRDPLASADryAV 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  433 NYIDVTGQDKLLQLSSYSFdgsTFDIFGALL----NGAKLVLVPKETVldvAKLAGLIEKQQisvmfiTTAFFNVlvdmn 508
Cdd:cd05958   132 NVLRLREDDRFVGSPPLAF---TFGLGGVLLfpfgVGASGVLLEEATP---DLLLSAIARYK------PTVLFTA----- 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  509 PDCLRHARAILFGGERvSVSHVRKAL--GHLGPGKIKHVY------------GPTESTVFATSYDVHEVEEGAVsipiGG 574
Cdd:cd05958   195 PTAYRAMLAHPDAAGP-DLSSLRKCVsaGEALPAALHRAWkeatgipiidgiGSTEMFHIFISARPGDARPGAT----GK 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  575 PISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGylnrpdlTAEKFADNPFAPGERMyrTGDLARWLPDGTIEYVGRID 654
Cdd:cd05958   270 PVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRY-------LADKRQRTYVQGGWNI--TGDTYSRDPDGYFRHQGRSD 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  655 DQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYV-----ADRSLPANEVRSTLSQELPAYMLPSYFV 729
Cdd:cd05958   341 DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIE 420
                         490
                  ....*....|....*...
gi 386647928  730 QLEQMPLTTNGKVDRRAL 747
Cdd:cd05958   421 FVTELPRTATGKLQRFAL 438
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
6523-6949 1.83e-23

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 107.67  E-value: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6523 LTPIQRWFFDQSLADLH---HFNQaFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENG----YAAWNRAIgegel 6595
Cdd:cd19543     4 LSPMQEGMLFHSLLDPGsgaYVEQ-MVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGeplqVVLKDRKL----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6596 ySLEVADFRDVKSAEQAVEA---KANEIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYE 6671
Cdd:cd19543    78 -PWRELDLSHLSEAEQEAELealAEEDRERGFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKELFAIYA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6672 QAAKGEEVRLPAkTDSFRTWSEQLAAYAQSPAmeneRAYW-EQIAQ-TAVAPLPKDKQSDRSLQQDSESITIQWSRKETE 6749
Cdd:cd19543   157 ALGEGQPPSLPP-VRPYRDYIAWLQRQDKEAA----EAYWrEYLAGfEEPTPLPKELPADADGSYEPGEVSFELSAELTA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6750 QLLKKVhRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDitRTVGWFTSKYPVLLQMEPGRSLSTRI 6829
Cdd:cd19543   232 RLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIE--TMVGLFINTLPVRVRLDPDQTVLELL 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6830 KKVKEDLrripnkgigyglcryLSAQPDGTV-------WGAEPEISFNYLGQFDQDLSNNDIGLSPYSSGLEMSDRQAR- 6901
Cdd:cd19543   309 KDLQAQQ---------------LELREHEYVplyeiqaWSEGKQALFDHLLVFENYPVDESLEEEQDEDGLRITDVSAEe 373
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928 6902 --SFilDINGMIT-DGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAH 6949
Cdd:cd19543   374 qtNY--PLTVVAIpGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
4892-5383 1.93e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 109.70  E-value: 1.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4892 LFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 4971
Cdd:PRK05605   37 LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLY 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4972 PSDRIQFMLEDSAASVLL-------TQTHLQE-----------------RAQQWGQTL--------QAALC--------- 5010
Cdd:PRK05605  117 TAHELEHPFEDHGARVAIvwdkvapTVERLRRttpletivsvnmiaampLLQRLALRLpipalrkaRAALTgpapgtvpw 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5011 ---LDDEAAYAEDASNVANVnEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA---------GYRREYRLDQFPVrllq 5078
Cdd:PRK05605  197 etlVDAAIGGDGSDVSHPRP-TPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkawvpglGDGPERVLAALPM---- 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5079 lasfsFDVFVGDIARTL--YNGGTMVICPkddRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLIT 5156
Cdd:PRK05605  272 -----FHAYGLTLCLTLavSIGGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFS 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5157 SSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAidsslydePLAklpeAGNvPIGKAAL---------NAKFYIVDAHlN 5227
Cdd:PRK05605  344 GAMALPVSTVELWEKLTGG--LLVEGYGLTETS--------PII----VGN-PMSDDRRpgyvgvpfpDTEVRIVDPE-D 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5228 P---VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIET 5304
Cdd:PRK05605  408 PdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYP 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5305 GEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSE--LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 5382
Cdd:PRK05605  481 AEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560

                  .
gi 386647928 5383 K 5383
Cdd:PRK05605  561 R 561
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
7439-7928 2.16e-23

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 109.20  E-value: 2.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7439 AAEYAREQ--TIHGLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFA 7515
Cdd:PRK08751   16 AAEIDLEQfrTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7516 IMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRHLQECVSfdgKVIAAD---------------------------- 7567
Cdd:PRK08751   96 VLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQ---QVIADTpvkqvittglgdmlgfpkaalvnfvvky 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7568 -----------------DEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRIT---EE 7627
Cdd:PRK08751  173 vkklvpeyringairfrEALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTgklEE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7628 DRVVQFASLSFdascWEIF----KALFFgatLYIPAKDTIL----DYPLFESYMNENGITAAILPPTY--AIYLSP--DR 7695
Cdd:PRK08751  253 GCEVVITALPL----YHIFaltaNGLVF---MKIGGCNHLIsnprDMPGFVKELKKTRFTAFTGVNTLfnGLLNTPgfDQ 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7696 L--PSLKKLITGGSAASVEFVQQWKD--KVRYFNAYGPTEASIVTSVwaaSPDGLDLRSVPIGRPIANHQIFIVDSQNHM 7771
Cdd:PRK08751  326 IdfSSLKMTLGGGMAVQRSVAERWKQvtGLTLVEAYGLTETSPAACI---NPLTLKEYNGSIGLPIPSTDACIKDDAGTV 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7772 LPVGVAGELCISGAGLARGYLNRPELTAEkfvdnpFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIE 7851
Cdd:PRK08751  403 LAIGEIGELCIKGPQVMKGYWKRPEETAK------VMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIE 476
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7852 EQLLKIASVQETIVIARGDANGQQQLCAYFV-ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK08751  477 DVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVkKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1901-2312 2.78e-23

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 106.61  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1901 YPVSSAQKRLYIL--HQlegaEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGF-ELVNGEPVQRVYKEVNFAV 1977
Cdd:cd19545     2 YPCTPLQEGLMALtaRQ----PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPISW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1978 EhYRTSEAEAGEVVRGfvRTFDLaKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGESLATlRIQY 2057
Cdd:cd19545    78 T-ESTSLDEYLEEDRA--APMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2058 KDY--AVWQQSEEQLERvkrqeaYWLDMFRGELpvlemPTDYPR-PAVRRF--EGSTLSFRLDAGLNealkrvaAESGAT 2132
Cdd:cd19545   153 SRFvkYLRQLDDEAAAE------FWRSYLAGLD-----PAVFPPlPSSRYQprPDATLEHSISLPSS-------ASSGVT 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2133 LYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTH---GDLQpLIGMFVNTLAIRNYPAGGKTFRSFLEEVKETTlgayeHQ 2209
Cdd:cd19545   215 LATVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvpGIEQ-IVGPTIATVPLRVRIDPEQSVEDFLQTVQKDL-----LD 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2210 TYPFEE--LVEKLQVPRDLSRNPIFDAMFVLQnTENEELQLDGLKLAPYPSGNTIARFD---LTLDVTETGSGLECNLEY 2284
Cdd:cd19545   289 MIPFEHtgLQNIRRLGPDARAACNFQTLLVVQ-PALPSSTSESLELGIEEESEDLEDFSsygLTLECQLSGSGLRVRARY 367
                         410       420
                  ....*....|....*....|....*...
gi 386647928 2285 ATSLYARETIARMAKHLEQLLTAIAKAP 2312
Cdd:cd19545   368 DSSVISEEQVERLLDQFEHVLQQLASAP 395
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
886-1108 3.33e-23

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 106.95  E-value: 3.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  886 ALDRNRLEEAFRALIARHETLRTGIEMVGGEPMQRIYPEVE--FAVEHIRANEEEADAAVKQFI----RAFDLAKPPLLR 959
Cdd:cd19534    33 GLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelFRLEVVDLSSLAQAAAIEALAaeaqSSLDLEEGPLLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  960 VGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYGGE---DLPAL--RIQYKDYAVWQQSEAQKEQLKRQEAYWLE 1034
Cdd:cd19534   113 AALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQAlagEPIPLpsKTSFQTWAELLAEYAQSPALLEELAYWRE 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 1035 VFRGELPvlEMPTDyaRPAVQSYAGNaLRFELDAQKREGLQRIASEN-GATLYMVLLAAYTILLQKYTGQEDVVI 1108
Cdd:cd19534   193 LPAADYW--GLPKD--PEQTYGDART-VSFTLDEEETEALLQEANAAyRTEINDLLLAALALAFQDWTGRAPPAI 262
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
3859-4337 3.49e-23

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 108.60  E-value: 3.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLR-DAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPE 3937
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3938 YPEDRIRYMLEDSGAQALL---------------TQ-RH-----LRERVSFA-GTFV------------------AVDDE 3977
Cdd:PRK08974  108 YTPRELEHQLNDSGAKAIVivsnfahtlekvvfkTPvKHviltrMGDQLSTAkGTLVnfvvkyikrlvpkyhlpdAISFR 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3978 QAYHAdGSNLE---PVVGPNHLAYVIYTSGTTGKPKGVMVEHHGlcslklMFANTLQ--------MTEQDRVVQFAslsf 4046
Cdd:PRK08974  188 SALHK-GRRMQyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRN------MLANLEQakaaygplLHPGKELVVTA---- 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4047 dASCWEIFkALFFGATLYIPTSTTIL------DYPLFESYMNENGITA-TILPPTYAAYLNPDRMPSLK----KLITGGS 4115
Cdd:PRK08974  257 -LPLYHIF-ALTVNCLLFIELGGQNLlitnprDIPGFVKELKKYPFTAiTGVNTLFNALLNNEEFQELDfsslKLSVGGG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4116 AAsvefVQQ-----WKD--KVLYFNAYGPTEAS-IVTsiwdeASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAG 4187
Cdd:PRK08974  335 MA----VQQavaerWVKltGQYLLEGYGLTECSpLVS-----VNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4188 ELCISGVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKID 4267
Cdd:PRK08974  406 ELWVKGPQVMLGYWQRPEATDEVIKDG-------WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 4268 AVQE-AIVLAREDANGqqQLVAYFVAQRE--LTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK08974  479 KVLEvAAVGVPSEVSG--EAVKIFVVKKDpsLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
5937-6422 3.79e-23

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 109.12  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5937 IHQLFEEQAERIPDHLAVTFED-----KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGA 6011
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6012 YVPIDPDYPEDRIRYMLEDSGAKLLLVQGHLLDRasfaDKLVNLND--DGAYHED------------GSNLEPVNG---- 6073
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTRR----GREVNLKEeaDKACAQCptvekvvvvrhlGNDFTPAKGrdls 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6074 ----------------PEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVELNeqthiLQTGAVVFDAST------- 6130
Cdd:cd05968   219 ydeeketagdgaerteSEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFD-----LKPGDLLTWFTDlgwmmgp 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6131 FEIWGALLNGGRlyVVRNETILD---AVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFA--GLKTLIVGGDVLSV--P 6203
Cdd:cd05968   294 WLIFGGLILGAT--MVLYDGAPDhpkADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNahDLSSLRVLGSTGEPwnP 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6204 HINRVLREHAGLS---IVNGYGPTEnttfstthtIVGEQKEAVPIgKPINNST---------AYIVDSKLSLLPVGVwGE 6271
Cdd:cd05968   372 EPWNWLFETVGKGrnpIINYSGGTE---------ISGGILGNVLI-KPIKPSSfngpvpgmkADVLDESGKPARPEV-GE 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6272 LIVGGD--GVARGYLNRPeltaEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKV 6349
Cdd:cd05968   441 LVLLAPwpGMTRGFWRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAH 516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6350 ASVKE-ATVIVREDESGQKQLCayFV------AERELTIGELRAALSQELPNYMIPS--HFVPleRMPLTPNGKIDRRAL 6420
Cdd:cd05968   517 PAVLEsAAIGVPHPVKGEAIVC--FVvlkpgvTPTEALAEELMERVADELGKPLSPEriLFVK--DLPKTRNAKVMRRVI 592

                  ..
gi 386647928 6421 PA 6422
Cdd:cd05968   593 RA 594
PRK13382 PRK13382
bile acid CoA ligase;
5894-6423 3.84e-23

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 108.31  E-value: 3.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5894 LLTAIVQAPEAPLASLEMITAEEKEHIqrvfnateakypsdkTIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRL 5973
Cdd:PRK13382   17 LRRAGLIAPMRPDRYLRIVAAMRREGM---------------GPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5974 ARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQGH---LLDRAsFAD 6050
Cdd:PRK13382   82 AAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEfsaTVDRA-LAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6051 -----KLVNLNDDGAYH------EDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVmvehrnvvRLVKNTNYVELN---EQT 6116
Cdd:PRK13382  161 cpqatRIVAWTDEDHDLtvevliAAHAGQRPEPTGRKGRVILLTSGTTGTPKGA--------RRSGPGGIGTLKailDRT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6117 HILQTGAVVFDASTFEIWG------ALLNGGRLYVVRNETILDAVSLKNAIQQYGI--------NTMWLTAPLYNQLSQQ 6182
Cdd:PRK13382  233 PWRAEEPTVIVAPMFHAWGfsqlvlAASLACTIVTRRRFDPEATLDLIDRHRATGLavvpvmfdRIMDLPAEVRNRYSGR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6183 dsgmfaGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTEnTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLS 6262
Cdd:PRK13382  313 ------SLRFAAASGSRMR-PDVVIAFMDQFGDVIYNNYNATE-AGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFR 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6263 LLPVGVWGELIVGGDGVARGYLNrpelTAEKFVESSFLPgercyrTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEI 6342
Cdd:PRK13382  385 EVPTGEVGTIFVRNDTQFDGYTS----GSTKDFHDGFMA------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEV 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6343 EEQLLKVASVKEATVIVREDESGQKQLCAYFV--AERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK13382  455 EKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVlkPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534

                  ...
gi 386647928 6421 PAP 6423
Cdd:PRK13382  535 QAR 537
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
274-747 3.93e-23

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 108.00  E-value: 3.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  274 PDAVAVT--FEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRY 351
Cdd:cd17642    31 PGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDH 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  352 MLEDSGTQVLLSQG-------HLQERVSFSGTWIRLDDEEAYHE-----------DGSNL-------ESVNGPEHLTYVI 406
Cdd:cd17642   111 SLNISKPTIVFCSKkglqkvlNVQKKLKIIKTIIILDSKEDYKGyqclytfitqnLPPGFneydfkpPSFDRDEQVALIM 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  407 YTSGTTGKPKGNLTTHRNIirVVKNTNYID------VTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPK---ETVL 477
Cdd:cd17642   191 NSSGSTGLPKGVQLTHKNI--VARFSHARDpifgnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKfeeELFL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  478 DVaklaglIEKQQI-SVMFITT--AFFNVLVDMNPDCLRHARAILFGGERVS--VSHVRKALGHLgPGkIKHVYGPTEST 552
Cdd:cd17642   269 RS------LQDYKVqSALLVPTlfAFFAKSTLVDKYDLSNLHEIASGGAPLSkeVGEAVAKRFKL-PG-IRQGYGLTETT 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  553 VFATSYDVHEVEEGAVsipiGGPISNTAIYIVNAQN-KLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapger 631
Cdd:cd17642   341 SAILITPEGDDKPGAV----GKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGW----- 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  632 mYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEkqLCAYYV---ADRSLP 707
Cdd:cd17642   412 -LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAgIPDEDAGE--LPAAVVvleAGKTMT 488
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928  708 ANEVRSTL-SQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd17642   489 EKEVMDYVaSQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
4885-5385 4.04e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 108.58  E-value: 4.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4885 ENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAY 4964
Cdd:PRK06710   22 DIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4965 VPLDPDYPSDRIQFMLEDSAASVLLTQ-------THLQERAQ---------------------QWGQTLQAALCLDDEAA 5016
Cdd:PRK06710  102 VQTNPLYTERELEYQLHDSGAKVILCLdlvfprvTNVQSATKiehvivtriadflpfpknllyPFVQKKQSNLVVKVSES 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5017 YA---------EDASNVANVNEP-HDLAYVIYTSGTTGRPKGVMIEHRSLV-NTAAGYRREYRLDQFPVRLLQLASFsFD 5085
Cdd:PRK06710  182 ETihlwnsvekEVNTGVEVPCDPeNDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVVLGVLPF-FH 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5086 VF--VGDIARTLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSV 5163
Cdd:PRK06710  261 VYgmTAVMNLSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPV 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5164 TdyrvLQERFG--SQFRIINAYGVTEAA--IDSSLYDEplAKLPEAGNVPIGkaalNAKFYIVDAHLNPV-PVGVLGELC 5238
Cdd:PRK06710  338 E----VQEKFEtvTGGKLVEGYGLTESSpvTHSNFLWE--KRVPGSIGVPWP----DTEAMIMSLETGEAlPPGEIGEIV 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5239 IGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVR 5318
Cdd:PRK06710  408 VKGPQIMKGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5319 EAVVVVREDA-KGQKVLCAHFTAE-SELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK06710  481 EVVTIGVPDPyRGETVKAFVVLKEgTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1936-2307 4.39e-23

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 106.37  E-value: 4.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1936 DRGKLE---EAFRQLIARHETLRTGFeLVNG--EPVQRVYKEVNFAVEHYRTSEAE-AGEVVRGFV----RTFDLAKPPL 2005
Cdd:cd19544    34 SRARLDaflAALQQVIDRHDILRTAI-LWEGlsEPVQVVWRQAELPVEELTLDPGDdALAQLRARFdprrYRLDLRQAPL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2006 LRVGLVE-LAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGE--SLATLrIQYKDY--AVWQQSEEQlervkRQEAYw 2080
Cdd:cd19544   113 LRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRaaALPPP-VPYRNFvaQARLGASQA-----EHEAF- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2081 ldmFRGELPVLEMPTdYP--RPAVRRfEGSTL---SFRLDAGLNEALKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIV 2155
Cdd:cd19544   186 ---FREMLGDVDEPT-APfgLLDVQG-DGSDIteaRLALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVV 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2156 IGTPIAGRTHG--DLQPLIGMFVNTLAIRnYPAGGKTFRSFLEEVKE--TTLGAYEHQTypfeeLVEKLQ---VPRDLsr 2228
Cdd:cd19544   261 FGTVLSGRMQGgaGADRALGMFINTLPLR-VRLGGRSVREAVRQTHArlAELLRHEHAS-----LALAQRcsgVPAPT-- 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2229 nPIFDAMF-----VLQNTENEELQLDGLKLAP------YPsgntiarfdLTLDVTETGSGLECNLEYATSLYARETIARM 2297
Cdd:cd19544   333 -PLFSALLnyrhsAAAAAAAALAAWEGIELLGgeertnYP---------LTLSVDDLGDGFSLTAQVVAPIDAERVCAYM 402
                         410
                  ....*....|
gi 386647928 2298 AKHLEQLLTA 2307
Cdd:cd19544   403 ETALEQLVDA 412
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
7463-7931 5.04e-23

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 107.48  E-value: 5.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7463 AAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDS 7542
Cdd:PRK12406    3 ATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7543 GAQVLLTQ----RHLQECVSFDGKVIA----ADDEQAYGEDGSNLEPVVG--------PNHLAY----------VIYTSG 7596
Cdd:PRK12406   83 GARVLIAHadllHGLASALPAGVTVLSvptpPEIAAAYRISPALLTPPAGaidwegwlAQQEPYdgppvpqpqsMIYTSG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7597 TTGKPKGVMvehhglcslklmfaetlriteedrvvQFASLSFDASCWEIFKALFFGatlYIPAKDTILDYPLFESYMNEN 7676
Cdd:PRK12406  163 TTGHPKGVR--------------------------RAAPTPEQAAAAEQMRALIYG---LKPGIRALLTGPLYHSAPNAY 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7677 GITAA------ILPPTY---------------AIYLSPD------RLP----------SLKKLITGGSAASVEFVQQ--- 7716
Cdd:PRK12406  214 GLRAGrlggvlVLQPRFdpeellqlierhritHMHMVPTmfirllKLPeevrakydvsSLRHVIHAAAPCPADVKRAmie 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7717 WKDKVRYfNAYGPTEASIVTsvWAASPDGLDlRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLAR-GYLNRP 7795
Cdd:PRK12406  294 WWGPVIY-EYYGSTESGAVT--FATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKP 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7796 ELTAEKFVDNPFLAGERMYRTGDLARWLPDgnieylgRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQ 7875
Cdd:PRK12406  370 EKRAEIDRGGFITSGDVGYLDADGYLFLCD-------RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGE 442
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7876 QLCAYF--VADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAP 7931
Cdd:PRK12406  443 ALMAVVepQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
5928-6420 5.89e-23

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 107.77  E-value: 5.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5928 EAKYPSDKTIHQLFEEQAEriPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILK 6007
Cdd:PRK10946   18 EKGYWQDLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6008 AGgaYVPIDPDYPEDRIR---YMLEDSGAKLLLVQGH-LLDRASFADKLVN----------LNDDGAY------HEDGSN 6067
Cdd:PRK10946   96 LG--VAPVNALFSHQRSElnaYASQIEPALLIADRQHaLFSDDDFLNTLVAehsslrvvllLNDDGEHslddaiNHPAED 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6068 LEPVNGP-EHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYV-ELNEQTHILQT--GAVVFDASTFEIWGALLNGGRL 6143
Cdd:PRK10946  174 FTATPSPaDEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEIcGFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6144 YVVRNETILDAVSLknaIQQYGIN---------TMWLTAPLYNQLSQQdsgmFAGLKTLIVGGDVLSvPHINRVLREHAG 6214
Cdd:PRK10946  254 VLAPDPSATLCFPL---IEKHQVNvtalvppavSLWLQAIAEGGSRAQ----LASLKLLQVGGARLS-ETLARRIPAELG 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6215 LSIVNGYGPTE---NTTF---STTHTIVGEqkeavpiGKPI-NNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRP 6287
Cdd:PRK10946  326 CQLQQVFGMAEglvNYTRlddSDERIFTTQ-------GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSP 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6288 ELTAEKFVESSFlpgercYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDES-GQ 6366
Cdd:PRK10946  399 QHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGE 472
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6367 KQlCAYFVAERELTIGELRAAL-SQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK10946  473 KS-CAFLVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
4476-4698 5.92e-23

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 106.18  E-value: 5.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4476 ALDRERFEETFRKLIARHETLRTGFELIDGEPVQRIYPEVD----FAVETVQASEQEAK--AIVRDFIRPFDLAKPPLLR 4549
Cdd:cd19534    33 GLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelfrLEVVDLSSLAQAAAieALAAEAQSSLDLEEGPLLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4550 VGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYSGEElPGLRIQ------YKDYAVWQQSEAQKEQLKRQEAYWL 4623
Cdd:cd19534   113 AALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQAL-AGEPIPlpsktsFQTWAELLAEYAQSPALLEELAYWR 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 4624 EAFRGELPvlEMPTDYarpaVQSYAG-DTLDFRMNSEISEGLKRIAAES-GATLYMVLLAAYTVLLQKYTAQEDVIV 4698
Cdd:cd19534   192 ELPAADYW--GLPKDP----EQTYGDaRTVSFTLDEEETEALLQEANAAyRTEINDLLLAALALAFQDWTGRAPPAI 262
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
4473-4753 6.15e-23

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 106.03  E-value: 6.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4473 LEGA-LDRERFEETFRKLIARHETLRTGFeLIDGEpvQRIYPEV--------DFAVETVQASEQEAKAIvRDFI--RPFD 4541
Cdd:cd19535    32 FDGEdLDPDRLERAWNKLIARHPMLRAVF-LDDGT--QQILPEVpwygitvhDLRGLSEEEAEAALEEL-RERLshRVLD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4542 LAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLY--SGEELPGLRIQYKDYaVWQQSEAQKEQLKRQE 4619
Cdd:cd19535   108 VERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYedPGEPLPPLELSFRDY-LLAEQALRETAYERAR 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4620 AYW---LEAFRG--ELPVLEMPTDYARPAVQsyagdTLDFRMNSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYTAQE 4694
Cdd:cd19535   187 AYWqerLPTLPPapQLPLAKDPEEIKEPRFT-----RREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQP 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 4695 DVIVGTPIAGR--THADLQSLIGMFVNT--LAIRnyPAADKTFLSYLEDVKETTLGAFEHQTY 4753
Cdd:cd19535   262 RFLLNLTLFNRlpLHPDVNDVVGDFTSLllLEVD--GSEGQSFLERARRLQQQLWEDLDHSSY 322
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
1442-1790 6.47e-23

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 104.12  E-value: 6.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR--EYRLDQfpvRLLQLASF--SFDVFVGDIArTLYNGGTMVicPKD 1517
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADcaDLTEDD---RYLIINPFfhTFGYKAGIVA-CLLTGATVV--PVA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1518 DRIDPARLHYwISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTE 1597
Cdd:cd17638    75 VFDVDAILEA-IERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE-TVLTAYGLTE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1598 AAIdsslydeplAKLPEAGNVPI------GKAALNAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPELTEEKfvd 1671
Cdd:cd17638   153 AGV---------ATMCRPGDDAEtvattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEA--- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1672 spfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAE 1751
Cdd:cd17638   211 ---IDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 386647928 1752 SELKLSE--LRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:cd17638   288 PGVTLTEedVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK13382 PRK13382
bile acid CoA ligase;
2336-2831 6.66e-23

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 107.54  E-value: 6.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2336 ATAADYEADKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAV 2415
Cdd:PRK13382   34 IVAAMRREGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2416 LKAGGAYVPIDPEYPEDRISYMLEDSSAQVL--------LAQRRLQERVSFAGTVVTVDDEQAYAGDG-----SNLESAV 2482
Cdd:PRK13382  114 NRIGADILLLNTSFAGPALAEVVTREGVDTViydeefsaTVDRALADCPQATRIVAWTDEDHDLTVEVliaahAGQRPEP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2483 GPNDLAYIIYTSGTTGKPKGVM-VEHHGLCSLKQMFANTlQINAQDRVV---------QFASLSFDAS--CWEVFQTLFF 2550
Cdd:PRK13382  194 TGRKGRVILLTSGTTGTPKGARrSGPGGIGTLKAILDRT-PWRAEEPTVivapmfhawGFSQLVLAASlaCTIVTRRRFD 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2551 -GATL-----YIPTKETILDYQwFERYMSdngittatLPPTYavyLNPDHMPDFKRLIAAGSASSLELLQQWKDK---VK 2621
Cdd:PRK13382  273 pEATLdlidrHRATGLAVVPVM-FDRIMD--------LPAEV---RNRYSGRSLRFAAASGSRMRPDVVIAFMDQfgdVI 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2622 YfNAYGPTEDSICTTIwTPstEDisqLKSVP--IGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYlnrpdlTA 2699
Cdd:PRK13382  341 Y-NNYNATEAGMIATA-TP--AD---LRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------TS 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2700 EKfvDNPFEPGerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCA 2779
Cdd:PRK13382  408 GS--TKDFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAA 483
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2780 YFV--ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALPAP 2831
Cdd:PRK13382  484 FVVlkPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
405-747 7.28e-23

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 103.95  E-value: 7.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 VIYTSGTTGKPKGNLTTHRNIIRVVKNTN-YIDVTGQDK-LLQLSSYSFDGSTFdIFGALLNGAKLVLVPKetvldvaKL 482
Cdd:cd17630     5 VILTSGSTGTPKAVVHTAANLLASAAGLHsRLGFGGGDSwLLSLPLYHVGGLAI-LVRSLLAGAELVLLER-------NQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  483 AGLIEKQQISVMFIT---TAFFNVLV-DMNPDCLRHARAILFGGERVSVSHVRKALGHLGPgkIKHVYGPTE--STVFAT 556
Cdd:cd17630    77 ALAEDLAPPGVTHVSlvpTQLQRLLDsGQGPAALKSLRAVLLGGAPIPPELLERAADRGIP--LYTTYGMTEtaSQVATK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  557 SYDVHEVEEGAVSIPiggpisNTAIYIVNAqnklqpigvaGELCVAGDGLARGYLNRPdlTAEKFADNPFapgermYRTG 636
Cdd:cd17630   155 RPDGFGRGGVGVLLP------GRELRIVED----------GEIWVGGASLAMGYLRGQ--LVPEFNEDGW------FTTK 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  637 DLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKqLCAYYVADRSLPANEVRSTL 715
Cdd:cd17630   211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgVPDEELGQR-PVAVIVGRGPADPAELRAWL 289
                         330       340       350
                  ....*....|....*....|....*....|..
gi 386647928  716 SQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd17630   290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1440-1791 8.18e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 104.39  E-value: 8.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1440 PHDLaYVIYTSGTTGRPKGVMiehrslvntaagyrreYRLDQFPVRLLQLASFSFDVFVGDI------------------ 1501
Cdd:cd05924     3 ADDL-YILYTGGTTGMPKGVM----------------WRQEDIFRMLMGGADFGTGEFTPSEdahkaaaaaagtvmfpap 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1502 ----------ARTLYNGGTMVICPkDDRIDPARLHYWISEEKIT-IFESTPALIIPFMD-YVAEHGLDMSSMELLITSSD 1569
Cdd:cd05924    66 plmhgtgswtAFGGLLGGQTVVLP-DDRFDPEEVWRTIEKHKVTsMTIVGDAMARPLIDaLRDAGPYDLSSLFAISSGGA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1570 SCSVTDYRVLQERFgSQFRIINAYGVTEAAIDSSLYdePLAKLPEAGNvpigKAALNAKFYIVDAHLNPVPVGVLGELCI 1649
Cdd:cd05924   145 LLSPEVKQGLLELV-PNITLVDAFGSSETGFTGSGH--SAGSGPETGP----FTRANPDTVVLDDDGRVVPPGSGGVGWI 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1650 GGIG-VARGYLNRPELTEEKFvdsPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVR 1728
Cdd:cd05924   218 ARRGhIPLGYYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVY 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1729 EAVVVVREDAK-GQKVLcAYFTAE--SELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKID 1791
Cdd:cd05924   295 DVLVVGRPDERwGQEVV-AVVQLRegAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK09274 PRK09274
peptide synthase; Provisional
2353-2739 8.51e-23

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 107.29  E-value: 8.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2353 EQAERIPDHPAVVFEG----------QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAY 2422
Cdd:PRK09274   14 RAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2423 VPIDPEYPEDRISYMLEDSSAQVL----LAQ--RRLQeRVSFAG--TVVTVDDEQAYAG--------DGSNLESA---VG 2483
Cdd:PRK09274   94 VLVDPGMGIKNLKQCLAEAQPDAFigipKAHlaRRLF-GWGKPSvrRLVTVGGRLLWGGttlatllrDGAAAPFPmadLA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2484 PNDLAYIIYTSGTTGKPKGVMVEHhglcslkQMFANtlQINAQDRVVQFASLSFDASCWEVFqTLF---FGATLYIP--- 2557
Cdd:PRK09274  173 PDDMAAILFTSGSTGTPKGVVYTH-------GMFEA--QIEALREDYGIEPGEIDLPTFPLF-ALFgpaLGMTSVIPdmd 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2558 -TKETILDYQWFERYMSDNGITTATLPPTYAVYL------NPDHMPDFKRLIAAG---SASSLELLQQW-KDKVKYFNAY 2626
Cdd:PRK09274  243 pTRPATVDPAKLFAAIERYGVTNLFGSPALLERLgrygeaNGIKLPSLRRVISAGapvPIAVIERFRAMlPPDAEILTPY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2627 GPTED-SICT----TIWTPSTEDISQLKSVPIGGPIVNHRIYIVD------AHYQ---PVPVGVAGELCIAGVGLARGYL 2692
Cdd:PRK09274  323 GATEAlPISSiesrEILFATRAATDNGAGICVGRPVDGVEVRIIAisdapiPEWDdalRLATGEIGEIVVAGPMVTRSYY 402
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 2693 NRPDLTAE-KFVDnpfEPGERMYRTGDLAkWL-PDGTIEYLGRIDHQVK 2739
Cdd:PRK09274  403 NRPEATRLaKIPD---GQGDVWHRMGDLG-YLdAQGRLWFCGRKAHRVE 447
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
6080-6417 1.01e-22

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 103.88  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6080 VIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVELN---EQTHILQTGAvvfdASTFEIWGA---LLNGGRLYVVRNETILD 6153
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNwvvGDVTYLPLPA----THIGGLWWIltcLIHGGLCVTGGENTTYK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6154 avSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTL---IVGGDvLSVPHINRVLREHAGLSIVNGYGPTENTT-- 6228
Cdd:cd17635    82 --SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLrliGYGGS-RAIAADVRFIEATGLTNTAQVYGLSETGTal 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6229 FSTTHTivgEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRT 6308
Cdd:cd17635   159 CLPTDD---DSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------NT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6309 GDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAEREL---TIGELR 6385
Cdd:cd17635   229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELdenAIRALK 308
                         330       340       350
                  ....*....|....*....|....*....|..
gi 386647928 6386 AALSQELPNYMIPSHFVPLERMPLTPNGKIDR 6417
Cdd:cd17635   309 HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
6076-6417 1.11e-22

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 103.25  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTYVIYTSGTTGRPKGVMVEHRN-VVRLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNetiLDA 6154
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSwIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK---FNP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6155 VSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAgLKTLIVGGDVLSvPHINRVLREHA-GLSIVNGYGPTEnTTFsTTH 6233
Cdd:cd17633    78 KSWIRKINQYNATVIYLVPTMLQALARTLEPESK-IKSIFSSGQKLF-ESTKKKLKNIFpKANLIEFYGTSE-LSF-ITY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6234 TIVGEQKEAVPIGKPINNSTAYIVDSKlsllpVGVWGELIVGGDGVARGYLNRPELTAEKFvessflpgercYRTGDLAR 6313
Cdd:cd17633   154 NFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIGY 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6314 WLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAErELTIGELRAALSQELP 6393
Cdd:cd17633   218 VDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKRFLKQKLS 296
                         330       340
                  ....*....|....*....|....
gi 386647928 6394 NYMIPSHFVPLERMPLTPNGKIDR 6417
Cdd:cd17633   297 RYEIPKKIIFVDSLPYTSSGKIAR 320
PRK07470 PRK07470
acyl-CoA synthetase; Validated
4901-5385 1.32e-22

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 106.66  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:PRK07470   21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTQTHLQERA---QQWGQTLQAALCLDD-------EAAYAEDA-SNVANVNEPHD-LAYVIYTSGTTGRPKG 5048
Cdd:PRK07470  101 EASGARAMICHADFPEHAaavRAASPDLTHVVAIGGaragldyEALVARHLgARVANAAVDHDdPCWFFFTSGTTGRPKA 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5049 VMIEHRSLvntaaGYRREYRL-DQFPV-----RLLQLASFSFDVFVG---DIARtlynGGTMVICPKDdRIDPARLHYWI 5119
Cdd:PRK07470  181 AVLTHGQM-----AFVITNHLaDLMPGtteqdASLVVAPLSHGAGIHqlcQVAR----GAATVLLPSE-RFDPAEVWALV 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5120 SEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCsvtdYRVLQER----FGSqfRIINAYGVTEA------- 5188
Cdd:PRK07470  251 ERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPM----YRADQKRalakLGK--VLVQYFGLGEVtgnitvl 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5189 -AIDSSLYDEPLAKLPEAGNVPIGkaalnAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFveg 5267
Cdd:PRK07470  325 pPALHDAEDGPDARIGTCGFERTG-----MEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF--- 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5268 erlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLS 5347
Cdd:PRK07470  397 ----RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 386647928 5348 --ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK07470  473 eaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
286-747 1.46e-22

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 105.29  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSqg 365
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  366 hlqervsfsgtwirlddeeayheDGSNLESVNgpEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTNY-IDVTGQDKLL 444
Cdd:cd05973    79 -----------------------DAANRHKLD--SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDaVDLRPEDSFW 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  445 QLS----SYsfdGSTFDIFGALLNGAKLVLV----PKETVLDVaklaglIEKQQI-SVMFITTAFFNVLVDMNPDCLR-- 513
Cdd:cd05973   134 NAAdpgwAY---GLYYAITGPLALGHPTILLeggfSVESTWRV------IERLGVtNLAGSPTAYRLLMAAGAEVPARpk 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  514 -HARAILFGGERVSVSHVRKALGHLGPGKIKHvYGPTESTVFATSY--DVHEVEEGAVSIPIGGpisntaiYIVN----A 586
Cdd:cd05973   205 gRLRRVSSAGEPLTPEVIRWFDAALGVPIHDH-YGQTELGMVLANHhaLEHPVHAGSAGRAMPG-------WRVAvlddD 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  587 QNKLQPiGVAGELC--VAGDGLA--RGYLNRPDLtaekfadnpfAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGF 662
Cdd:cd05973   277 GDELGP-GEPGRLAidIANSPLMwfRGYQLPDTP----------AIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  663 RIELGEIEAHLLKLEAIEKATVVVR------ESANGEKQLCAYYVADRSLpANEVRSTLSQELPAYMLPSYFVQLEQMPL 736
Cdd:cd05973   346 RIGPFDVESALIEHPAVAEAAVIGVpdpertEVVKAFVVLRGGHEGTPAL-ADELQLHVKKRLSAHAYPRTIHFVDELPK 424
                         490
                  ....*....|.
gi 386647928  737 TTNGKVDRRAL 747
Cdd:cd05973   425 TPSGKIQRFLL 435
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
4887-5504 1.78e-22

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 107.87  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4887 EAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVP 4966
Cdd:COG3319     1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4967 LDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAALCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRP 5046
Cdd:COG3319    81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5047 KGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITI 5126
Cdd:COG3319   161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5127 FESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAG 5206
Cdd:COG3319   241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5207 NVPIGKAALnakfYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVD 5286
Cdd:COG3319   321 GPGLLVLLV----LLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLL 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5287 FIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYF 5366
Cdd:COG3319   397 GLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPAL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5367 VQLEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEAKLVSIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVH 5446
Cdd:COG3319   477 LLLLLLLLLLLLAALLLAAAAPAAA-AAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLL 555
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 5447 KEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEEReyypvSSAQKRLYILH 5504
Cdd:COG3319   556 ALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRA-----GGSGPPLFCVH 608
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1446-1792 1.83e-22

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 102.73  E-value: 1.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1446 VIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIArTLYNGGTMVICpkdDRIDPARL 1525
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALA-TFHAGGANVVM---EKFDPAEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1526 HYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELlITSSDSCSVTdyRVLQERFGSQFRIinAYGVTEAA--IDSS 1603
Cdd:cd17637    81 LELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRH-VLGLDAPETI--QRFEETTGATFWS--LYGQTETSglVTLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1604 LYDEplaklpEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRT 1683
Cdd:cd17637   156 PYRE------RPGSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHT 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1684 GDLARWMPDGNVDFIGRIDNQAKIR--GYRIETGEIETQLLKAEGVREAVVVVREDAK---GQKVLCAyFTAESELKLSE 1758
Cdd:cd17637   221 GDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDPKwgeGIKAVCV-LKPGATLTADE 299
                         330       340       350
                  ....*....|....*....|....*....|....
gi 386647928 1759 LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 1792
Cdd:cd17637   300 LIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1323-1703 1.98e-22

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 106.15  E-value: 1.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVK--PNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLT 1400
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1401 QTHLQeraqqwgqtlqaVLCLDDeaayAED--ASNVANVN--EPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGY--- 1473
Cdd:cd05927    86 DAGVK------------VYSLEE----FEKlgKKNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfki 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1474 -RREYRLDQFPV------------RLLQLASFSFDVFVGdiartLYNGGTMVICpkDD------RIDPA------RLH-- 1526
Cdd:cd05927   150 lEILNKINPTDVyisylplahifeRVVEALFLYHGAKIG-----FYSGDIRLLL--DDikalkpTVFPGvprvlnRIYdk 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1527 ----------------YWISEEKITIFESTPALIIPFMDYVAEHGLDMS---SMELLITSSDSCSVTDYRVLQERFGSQF 1587
Cdd:cd05927   223 ifnkvqakgplkrklfNFALNYKLAELRSGVVRASPFWDKLVFNKIKQAlggNVRLMLTGSAPLSPEVLEFLRVALGCPV 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1588 RiiNAYGVTE--AAIDSSLYDEPLaklpeAGNVpiGKAALNAKFYIVDA------HLNPVPVgvlGELCIGGIGVARGYL 1659
Cdd:cd05927   303 L--EGYGQTEctAGATLTLPGDTS-----VGHV--GGPLPCAEVKLVDVpemnydAKDPNPR---GEVCIRGPNVFSGYY 370
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 386647928 1660 NRPELTEEKFVdspfVEGerLYRTGDLARWMPDGNVDFIGRIDN 1703
Cdd:cd05927   371 KDPEKTAEALD----EDG--WLHTGDIGEWLPNGTLKIIDRKKN 408
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
3868-4332 2.29e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 105.48  E-value: 2.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKS--QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRY 3945
Cdd:PRK13390   11 PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3946 MLEDSGAQALLTQRHL-----------RERVSFAGTFVAVDD-EQAYHADGSNL-EPVVGpnhlAYVIYTSGTTGKPKGV 4012
Cdd:PRK13390   91 IVGDSGARVLVASAALdglaakvgadlPLRLSFGGEIDGFGSfEAALAGAGPRLtEQPCG----AVMLYSSGTTGFPKGI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4013 MVEHHGlcslklmfantlQMTEQ--DRVVQFASLSFDASCWEIFKA---LFFGATL------YIPTSTTIL----DYPLF 4077
Cdd:PRK13390  167 QPDLPG------------RDVDApgDPIVAIARAFYDISESDIYYSsapIYHAAPLrwcsmvHALGGTVVLakrfDAQAT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4078 ESYMNENGITATILPPTYAAY---LNPD-----RMPSLKKLITGGSAASVEFVQ---QWKDKVLYfNAYGPTEASIVTSI 4146
Cdd:PRK13390  235 LGHVERYRITVTQMVPTMFVRllkLDADvrtryDVSSLRAVIHAAAPCPVDVKHamiDWLGPIVY-EYYSSTEAHGMTFI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4147 wdEASDSLGDRKSVpiGRPLANhRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEkfVDNPFEPgerMYRT- 4225
Cdd:PRK13390  314 --DSPDWLAHPGSV--GRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP---FWTTv 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4226 GDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN-GQQ-----QLVAYFVAQRELtAA 4299
Cdd:PRK13390  384 GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEmGEQvkaviQLVEGIRGSDEL-AR 462
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 4300 ELRATMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK13390  463 ELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
2359-2828 2.53e-22

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 106.56  E-value: 2.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2359 PDHPAVVFEG------QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI----DPE 2428
Cdd:TIGR02188   71 PDKVAIIWEGdepgevRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVfggfSAE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2429 YPEDRIsymlEDSSAQVLL---AQRR------LQERVSFA-----GTVVTV---------------------DDEQAYAG 2473
Cdd:TIGR02188  151 ALADRI----NDAGAKLVItadEGLRggkvipLKAIVDEAlekcpVSVEHVlvvrrtgnpvvpwvegrdvwwHDLMAKAS 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2474 DGSNLESaVGPNDLAYIIYTSGTTGKPKGVMveH-------HGLCSLKQMF-----------ANTLQINAQDRVVqFASL 2535
Cdd:TIGR02188  227 AYCEPEP-MDSEDPLFILYTSGSTGKPKGVL--HttggyllYAAMTMKYVFdikdgdifwctADVGWITGHSYIV-YGPL 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2536 SFDAScwevfQTLFFGATLYiPTK----ETIldyqwfERYmsdnGITTATLPPTyAVYLnpdhmpdfkrLIAAGSA---- 2607
Cdd:TIGR02188  303 ANGAT-----TVMFEGVPTY-PDPgrfwEII------EKH----KVTIFYTAPT-AIRA----------LMRLGDEwvkk 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2608 ---SSLELL---------QQWKdkvKYFNAYGPTEDSICTTIWtpSTEDISQLKSvPIGG-----------PIVNHRIYI 2664
Cdd:TIGR02188  356 hdlSSLRLLgsvgepinpEAWM---WYYKVVGKERCPIVDTWW--QTETGGIMIT-PLPGatptkpgsatlPFFGIEPAV 429
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2665 VDAHYQPVP-VGVAGELCIAGV--GLARGYLNRPdltaEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIR 2741
Cdd:TIGR02188  430 VDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVS 505
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  2742 GYRIELGEIEEQLLKVASVQEAIVIA-HDDASGQkQLCAYFVADRTMT-----VGELRGELSGELPGYMIPAHFVQLERM 2815
Cdd:TIGR02188  506 GHRLGTAEIESALVSHPAVAEAAVVGiPDDIKGQ-AIYAFVTLKDGYEpddelRKELRKHVRKEIGPIAKPDKIRFVPGL 584
                          570
                   ....*....|...
gi 386647928  2816 PLTPNGKIDRKAL 2828
Cdd:TIGR02188  585 PKTRSGKIMRRLL 597
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
4465-4724 2.60e-22

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 104.06  E-value: 2.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4465 YNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFeLIDG--EPVQRIYPEVDFAVETVQASEQE-AKAIVRDFIRP-- 4539
Cdd:cd19544    24 YLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAI-LWEGlsEPVQVVWRQAELPVEELTLDPGDdALAQLRARFDPrr 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4540 --FDLAKPPLLRVGLIELAP-ERCILMLDMHHIVSDGVSADVLVEEFARLYSGE--ELPGLrIQYKDYaVWQQSEAQKEQ 4614
Cdd:cd19544   103 yrLDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRaaALPPP-VPYRNF-VAQARLGASQA 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4615 lkRQEAYwleaFRGELPVLEMPT-DYARPAVQSYAGDTLDFRM--NSEISEGLKRIAAESGATLYMVLLAAYTVLLQKYT 4691
Cdd:cd19544   181 --EHEAF----FREMLGDVDEPTaPFGLLDVQGDGSDITEARLalDAELAQRLRAQARRLGVSPASLFHLAWALVLARCS 254
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 386647928 4692 AQEDVIVGTPIAGRTHA--DLQSLIGMFVNTLAIR 4724
Cdd:cd19544   255 GRDDVVFGTVLSGRMQGgaGADRALGMFINTLPLR 289
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
853-1264 2.62e-22

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 104.32  E-value: 2.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  853 YPLSSAQKRLYILHQLEGAEQSYNLPGVTLLEGALDRNRLEEAFRALIARHETLRTGIEMVG-GEPMQRIYPEVEFAVEH 931
Cdd:cd19547     2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  932 IRANEEEADAAVKQFIR--------AFDLAKPPLLRVGLIELAPERHLLMFDMHHIVSDGISMDVLVEEFARLYggEDL- 1002
Cdd:cd19547    82 LDWSGEDPDRRAELLERlladdraaGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVY--EELa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1003 ----PALRI--QYKDYAVWQQseAQKEQLKRQEAYWLEVFRgELPvlemPTDYAR-PAVQSYAGNALRFELDAQKREGLQ 1075
Cdd:cd19547   160 hgrePQLSPcrPYRDYVRWIR--ARTAQSEESERFWREYLR-DLT----PSPFSTaPADREGEFDTVVHEFPEQLTRLVN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1076 RIASENGATLYMVLLAAYTILLQKYTGQEDVVIGTPIAGRT---HGDLHpLIGMFVNTLAIRNYPAADKTFLSYLEDVKE 1152
Cdd:cd19547   233 EAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPpelEGSEH-MVGIFINTIPLRIRLDPDQTVTGLLETIHR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1153 TTLGAFERQDYPFEELVDKLKLARdLSRNPLFDTMFTLQNTenKEFRLPGLQLTPYPVEEHT---SKFDLSLdIMESGDG 1229
Cdd:cd19547   312 DLATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENY--PEDNLPGDDLSIQIIDLHAqekTEYPIGL-IVLPLQK 387
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 386647928 1230 FLCGIEYATALYKRETIERMAKHFEQLLTAIVNNP 1264
Cdd:cd19547   388 LAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
7473-7928 2.70e-22

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 105.69  E-value: 2.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7473 TYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQR- 7551
Cdd:cd17642    46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKk 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 ------HLQECVSFDGKVIAAD---DEQAYGEDGSNLEPVVGPNHLAY---------------VIYTSGTTGKPKGVMVE 7607
Cdd:cd17642   126 glqkvlNVQKKLKIIKTIIILDskeDYKGYQCLYTFITQNLPPGFNEYdfkppsfdrdeqvalIMNSSGSTGLPKGVQLT 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7608 HHGLCSlklMFAETL------RITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKdtiLDYPLFESYMNENGITAA 7681
Cdd:cd17642   206 HKNIVA---RFSHARdpifgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYK---FEEELFLRSLQDYKVQSA 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7682 ILPPTYAIYLSPDR------LPSLKKLITGGSAASVEFVQQWKDK-----VRyfNAYGPTEAsivTSVWAASPDGlDLRS 7750
Cdd:cd17642   280 LLVPTLFAFFAKSTlvdkydLSNLHEIASGGAPLSKEVGEAVAKRfklpgIR--QGYGLTET---TSAILITPEG-DDKP 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7751 VPIGRPIANHQIFIVD-SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIE 7829
Cdd:cd17642   354 GAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWL------HSGDIAYYDEDGHFF 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7830 YLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTL-SQELPGYMIP 7906
Cdd:cd17642   428 IVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVleAGKTMTEKEVMDYVaSQVSTAKRLR 507
                         490       500
                  ....*....|....*....|..
gi 386647928 7907 SYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd17642   508 GGVKFVDEVPKGLTGKIDRRKI 529
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
5036-5382 2.81e-22

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 102.35  E-value: 2.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5036 VIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIArTLYNGGTMVICpkdDRIDPARL 5115
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALA-TFHAGGANVVM---EKFDPAEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5116 HYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSM--VLLITSSDSCsvtdyRVLQERFGSQFRIinAYGVTEAA--ID 5191
Cdd:cd17637    81 LELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrhVLGLDAPETI-----QRFEETTGATFWS--LYGQTETSglVT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5192 SSLYDEplaklpEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLY 5271
Cdd:cd17637   154 LSPYRE------RPGSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WH 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5272 RTGDLARWMPDGNVDFIGRIDNQAKIR--GYRIETGEIETQLLKAEGVREAVVVVREDAK---GQKVLC---AHFTAESE 5343
Cdd:cd17637   219 HTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDPKwgeGIKAVCvlkPGATLTAD 298
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 386647928 5344 lklsELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 5382
Cdd:cd17637   299 ----ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
2486-2825 2.82e-22

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 102.34  E-value: 2.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2486 DLAYIIYTSGTTGKPKGVMVEHHGL-CSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETilD 2564
Cdd:cd17635     2 DPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT--T 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2565 YQWFERYMSDNGITTATLPPT---YAVYLNPDHMPDFK--RLIAAGSASSLELLQQ---WKDKVKYFNAYGPTEDSICTT 2636
Cdd:cd17635    80 YKSLFKILTTNAVTTTCLVPTllsKLVSELKSANATVPslRLIGYGGSRAIAADVRfieATGLTNTAQVYGLSETGTALC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2637 IwtPSTEDISQLKSVpiGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermyRT 2716
Cdd:cd17635   160 L--PTDDDSIEINAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------NT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2717 GDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGELRG-- 2794
Cdd:cd17635   229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRAlk 308
                         330       340       350
                  ....*....|....*....|....*....|..
gi 386647928 2795 -ELSGELPGYMIPAHFVQLERMPLTPNGKIDR 2825
Cdd:cd17635   309 hTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK07638 PRK07638
acyl-CoA synthetase; Validated
5936-6420 2.87e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 104.86  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQmVGLMVERSLEMVVGMIAILKAGGAYVPI 6015
Cdd:PRK07638    2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6016 DPDYPEDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDgaYHEDGSN----LEPVNGPEHLT-YVIYTSGTTGRP 6090
Cdd:PRK07638   81 DIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDE--WKRMIEKylptYAPIENVQNAPfYMGFTSGSTGKP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6091 KGVMVEHRNVVRLVK-NTNYVELNEQTHILQTGAVVfdASTFeIWGA---LLNGGRLYVVRNET---ILDAVSLKNAIQQ 6163
Cdd:PRK07638  159 KAFLRAQQSWLHSFDcNVHDFHMKREDSVLIAGTLV--HSLF-LYGAistLYVGQTVHLMRKFIpnqVLDKLETENISVM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6164 YGINTMwlTAPLYNQLSQQDSGMfaglkTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTEnttFSTTHTIVGEQKEAV 6243
Cdd:PRK07638  236 YTVPTM--LESLYKENRVIENKM-----KIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE---LSFVTALVDEESERR 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6244 P--IGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEkfvessfLPGERCYRTGDLARWLPDGTLE 6321
Cdd:PRK07638  306 PnsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-------LNADGWMTVRDVGYEDEEGFIY 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6322 YKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFvaERELTIGELRAALSQELPNYMIPSHF 6401
Cdd:PRK07638  379 IVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSATKQQLKSFCLQRLSSFKIPKEW 456
                         490
                  ....*....|....*....
gi 386647928 6402 VPLERMPLTPNGKIDRRAL 6420
Cdd:PRK07638  457 HFVDEIPYTNSGKIARMEA 475
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
4913-5293 3.09e-22

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 105.38  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVK--PNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLT 4990
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4991 QTHLqeRAQQWGQTLQaalclddeaayaEDASNVANVN--EPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGY----R 5064
Cdd:cd05927    86 DAGV--KVYSLEEFEK------------LGKKNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5065 REYRLDQFPV------------RLLQLASFSFDVFVGdiartLYNGGTMVICpkDD------RIDPA------RLH---- 5116
Cdd:cd05927   152 ILNKINPTDVyisylplahifeRVVEALFLYHGAKIG-----FYSGDIRLLL--DDikalkpTVFPGvprvlnRIYdkif 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5117 --------------YWISEEKITIFESTPALIIPFMDYVAEHGLDMS---SMVLLITSSDSCSVTDYRVLQERFGSQFRi 5179
Cdd:cd05927   225 nkvqakgplkrklfNFALNYKLAELRSGVVRASPFWDKLVFNKIKQAlggNVRLMLTGSAPLSPEVLEFLRVALGCPVL- 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5180 iNAYGVTE--AAIDSSLYDEPLaklpeAGNVpiGKAALNAKFYIVDA------HLNPVPVgvlGELCIGGIGVARGYLNR 5251
Cdd:cd05927   304 -EGYGQTEctAGATLTLPGDTS-----VGHV--GGPLPCAEVKLVDVpemnydAKDPNPR---GEVCIRGPNVFSGYYKD 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 386647928 5252 PELTEEKFVdspfVEGerLYRTGDLARWMPDGNVDFIGRIDN 5293
Cdd:cd05927   373 PEKTAEALD----EDG--WLHTGDIGEWLPNGTLKIIDRKKN 408
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
6527-6979 3.57e-22

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 107.25  E-value: 3.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6527 QRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGYAAWNRAIGEGELYSLEVADFRDV 6606
Cdd:COG1020    26 RLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6607 KSAEQAVEAKANEIQSSIDLEVGPLFKAGLFQCADGDHLLLV-IHHGVVDGVSWRILLEDVALGYEQAAKGEEVRLPAKT 6685
Cdd:COG1020   106 LAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLaLHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6686 DSFRTWSEQLAAYAQSPAMENERAYWEQIAQTAVAP--LPKDKQSDRSLQQDSESITIQWSRKETEQLlKKVHRAYNTEM 6763
Cdd:COG1020   186 IQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLleLPTDRPRPAVQSYRGARVSFRLPAELTAAL-RALARRHGVTL 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6764 NDILLTALGMAVQKWSGLDRLLVNLEGHGResimTDIDITRTVGWFTSKYPVLLQMEPGRSLSTRIKKVKEDL------R 6837
Cdd:COG1020   265 FMVLLAAFALLLARYSGQDDVVVGTPVAGR----PRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLlaayahQ 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6838 RIPnkgiGYGLCRYLSAQPDGtvwGAEP--EISFNYLGQFDQDLSNNDIGLSPYSSGLEMSDrqarsFILDINGMITDGS 6915
Cdd:COG1020   341 DLP----FERLVEELQPERDL---SRNPlfQVMFVLQNAPADELELPGLTLEPLELDSGTAK-----FDLTLTVVETGDG 408
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 6916 LALELSYSRKEYHRETVEELAGMLQESLQEIIAHcaakewTELTPSDVQLkgLTVEELEQISAQ 6979
Cdd:COG1020   409 LRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD------PDQPLGDLPL--LTAAERQQLLAE 464
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1319-1797 3.61e-22

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 105.36  E-value: 3.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1319 ENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVL 1398
Cdd:PRK04319   70 RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1399 LTQTHLQER--AQQWgQTLQAVLCLDDEA-------------AYAEDASNVANVnEPHDLAYVIYTSGTTGRPKGV---- 1459
Cdd:PRK04319  150 ITTPALLERkpADDL-PSLKHVLLVGEDVeegpgtldfnalmEQASDEFDIEWT-DREDGAILHYTSGSTGKPKGVlhvh 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 --MIEHRslvntAAGYrreYRLDQFPVrllqlasfsfDVF-------------VGDIArTLYNGGTMVIcpKDDRIDPAR 1524
Cdd:PRK04319  228 naMLQHY-----QTGK---YVLDLHED----------DVYwctadpgwvtgtsYGIFA-PWLNGATNVI--DGGRFSPER 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1525 LHYWISEEKITIFESTPALIIPFM----DYVAEHglDMSSMELLItssdscSVTD----------YRVLQERF------- 1583
Cdd:PRK04319  287 WYRILEDYKVTVWYTAPTAIRMLMgagdDLVKKY--DLSSLRHIL------SVGEplnpevvrwgMKVFGLPIhdnwwmt 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1584 --GSQFrIINAYGVteaAIDSSLYDEPLaklpeagnvPIGKAAlnakfyIVDAHLNPVPVGVLGELCI--GGIGVARGYL 1659
Cdd:PRK04319  359 etGGIM-IANYPAM---DIKPGSMGKPL---------PGIEAA------IVDDQGNELPPNRMGNLAIkkGWPSMMRGIW 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1660 NRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK 1739
Cdd:PRK04319  420 NNPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPV 492
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 1740 GQKVLCAY------FTAESELKLsELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 1797
Cdd:PRK04319  493 RGEIIKAFvalrpgYEPSEELKE-EIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1323-1795 3.63e-22

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 104.14  E-value: 3.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTqt 1402
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 hlqeraqqwgqtlqavlclddeaayaeDASNVANVNEphDLAYVIYTSGTTGRPKGVMIEHRSLV------NTAAGYRRE 1476
Cdd:cd05973    79 ---------------------------DAANRHKLDS--DPFVMMFTSGTTGLPKGVPVPLRALAafgaylRDAVDLRPE 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1477 yrlDQF-----PVRLLQLASFSFDVFVGDIARTLYNGGTMVicPKDDRIdparlhywISEEKITIFESTPALIIPFMDYV 1551
Cdd:cd05973   130 ---DSFwnaadPGWAYGLYYAITGPLALGHPTILLEGGFSV--ESTWRV--------IERLGVTNLAGSPTAYRLLMAAG 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1552 AEHGLDMSsMELLITSSDSCSVTD--YRVLQERFGSQFRiiNAYGVTEAA--IDSSLYDEPLAKLPEAGNVPIGKaalna 1627
Cdd:cd05973   197 AEVPARPK-GRLRRVSSAGEPLTPevIRWFDAALGVPIH--DHYGQTELGmvLANHHALEHPVHAGSAGRAMPGW----- 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1628 KFYIVDAHLNPVPVGVLGELcigGIGVAR-------GYLNRpelteekfvDSPFVEGeRLYRTGDLARWMPDGNVDFIGR 1700
Cdd:cd05973   269 RVAVLDDDGDELGPGEPGRL---AIDIANsplmwfrGYQLP---------DTPAIDG-GYYLTGDTVEFDPDGSFSFIGR 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1701 IDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED------AKGQKVLCAYFTAESELKlSELRSSLSQELPGYMIPS 1774
Cdd:cd05973   336 ADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDpertevVKAFVVLRGGHEGTPALA-DELQLHVKKRLSAHAYPR 414
                         490       500
                  ....*....|....*....|.
gi 386647928 1775 YFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05973   415 TIHFVDELPKTPSGKIQRFLL 435
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
5961-6358 3.82e-22

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 103.80  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPidpdypedrirymledsgAKLLLVQG 6040
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 HLLDRASFADKLVNLNDDGAYHEDgsnlePVngpehLTYviYTSGTTGRPKgvMVEHRNVVRLVKNtnyveLNEQTHI-L 6119
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDENTHADD-----PM-----LLY--FTSGTTSKPK--LVEHTHRSYPVGH-----LSTMYWIgL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6120 QTGAVVFDAST-------FEIWGALLNGGRLYVVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFA-GLK 6191
Cdd:cd05974   124 KPGDVHWNISSpgwakhaWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDvKLR 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6192 TLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTENTTFSTTHTivGEQKEAVPIGKPINNSTAYIVDsklsllPVG---V 6268
Cdd:cd05974   204 EVVGAGEPLN-PEVIEQVRRAWGLTIRDGYGQTETTALVGNSP--GQPVKAGSMGRPLPGYRVALLD------PDGapaT 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6269 WGEL-IVGGD----GVARGYLNRPELTAEKFvessflpGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIE 6343
Cdd:cd05974   275 EGEVaLDLGDtrpvGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
                         410
                  ....*....|....*
gi 386647928 6344 EQLLKVASVKEATVI 6358
Cdd:cd05974   348 SVLIEHPAVAEAAVV 362
PRK09274 PRK09274
peptide synthase; Provisional
5943-6420 3.86e-22

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 105.37  E-value: 3.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5943 EQAERIPDHLAVTFED----------KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAY 6012
Cdd:PRK09274   14 RAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6013 VPIDPDYPEDRIRYMLEDSGAKLLLVQ-----GHLLDRASFADKLVNLNDDGAY------------HEDGSNLEPVN-GP 6074
Cdd:PRK09274   94 VLVDPGMGIKNLKQCLAEAQPDAFIGIpkahlARRLFGWGKPSVRRLVTVGGRLlwggttlatllrDGAAAPFPMADlAP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6075 EHLTYVIYTSGTTGRPKGVMVEHRN---VVRLVKNTNYVELNEqthilqtgavvFDASTFEIWgALLN---GGRLYV--- 6145
Cdd:PRK09274  174 DDMAAILFTSGSTGTPKGVVYTHGMfeaQIEALREDYGIEPGE-----------IDLPTFPLF-ALFGpalGMTSVIpdm 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6146 -------VRNETILDavslknAIQQYGINTMWLTAPLYNQLSQ--QDSGM-FAGLKTLIVGGDVLSVPHINRvLRE--HA 6213
Cdd:PRK09274  242 dptrpatVDPAKLFA------AIERYGVTNLFGSPALLERLGRygEANGIkLPSLRRVISAGAPVPIAVIER-FRAmlPP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6214 GLSIVNGYGPTENTTFST--------THTIVGEQKEAVPIGKPINNSTAYIVD---------SKLSLLPVGVWGELIVGG 6276
Cdd:PRK09274  315 DAEILTPYGATEALPISSiesreilfATRAATDNGAGICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6277 DGVARGYLNRPELTAE-KFVESSflpGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRG---YRIELGEIEEQLLKVAsv 6352
Cdd:PRK09274  395 PMVTRSYYNRPEATRLaKIPDGQ---GDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGgtlYTIPCERIFNTHPGVK-- 469
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 6353 KEATVIVREDESGQKQLC----AYFVAERELTIGELRaALSQELPNYMIPSHFVPLERMPLTP--NGKIDRRAL 6420
Cdd:PRK09274  470 RSALVGVGVPGAQRPVLCvelePGVACSKSALYQELR-ALAAAHPHTAGIERFLIHPSFPVDIrhNAKIFREKL 542
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
3880-4340 4.08e-22

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 104.78  E-value: 4.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERS---LEMVVGIMAImkagGAY-IPIDPEYPEDRIRYMLEDSGAQAL 3955
Cdd:PRK12406   12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDfafFEAAYAAMRL----GAYaVPVNWHFKPEEIAYILEDSGARVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3956 LTQ----RHLRERVSFAGTFVAV----DDEQAYHADGSNLEPVVG--------PNHLAY----------VIYTSGTTGKP 4009
Cdd:PRK12406   88 IAHadllHGLASALPAGVTVLSVptppEIAAAYRISPALLTPPAGaidwegwlAQQEPYdgppvpqpqsMIYTSGTTGHP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4010 KGVMvehhglcslklMFANTlqmTEQdrvvqfaslsfdASCWEIFKALFFGatlYIPTSTTILDYPLFESYMNENGITA- 4088
Cdd:PRK12406  168 KGVR-----------RAAPT---PEQ------------AAAAEQMRALIYG---LKPGIRALLTGPLYHSAPNAYGLRAg 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4089 -----TILPPTYAA---------------YLNPD------RMP----------SLKKLITGGSAASVEFVQQ---WKDKV 4129
Cdd:PRK12406  219 rlggvLVLQPRFDPeellqlierhrithmHMVPTmfirllKLPeevrakydvsSLRHVIHAAAPCPADVKRAmieWWGPV 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4130 LYfNAYGPTEASIVTsiWDEASDSLgdRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLAR-GYLNRPELTA 4208
Cdd:PRK12406  299 IY-EYYGSTESGAVT--FATSEDAL--SHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRA 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4209 EKFVDNPFEPGERMYRTGDLVRWLPDgnleylgRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVA 4288
Cdd:PRK12406  374 EIDRGGFITSGDVGYLDADGYLFLCD-------RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMA 446
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4289 YFVAQ--RELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAP 4340
Cdd:PRK12406  447 VVEPQpgATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1322-1725 4.38e-22

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 103.98  E-value: 4.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 1401
Cdd:cd17640     5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 thlqeraqqwgqtlqavlclddeaayaedasnvanvNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNtaaGYRREYRLDQ 1481
Cdd:cd17640    85 ------------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHANLLH---QIRSLSDIVP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 FPV--RLLQL--------ASFSFDVFVGDIARTLynggTMVICPKDD--RIDParlHYWISEEKitIFESTPALII---- 1545
Cdd:cd17640   126 PQPgdRFLSIlpiwhsyeRSAEYFIFACGCSQAY----TSIRTLKDDlkRVKP---HYIVSVPR--LWESLYSGIQkqvs 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1546 ---PFMDYVAeHGLdMSSMELLITSSDSCSVTDYrvLQERFGS-QFRIINAYGVTEAAIDSSlydepLAKLPEAGNVPIG 1621
Cdd:cd17640   197 kssPIKQFLF-LFF-LSGGIFKFGISGGGALPPH--VDTFFEAiGIEVLNGYGLTETSPVVS-----ARRLKCNVRGSVG 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1622 KAALNAKFYIVDAHLN-PVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEgerlyrTGDLARWMPDGNVDFIGR 1700
Cdd:cd17640   268 RPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFN------TGDLGWLTCGGELVLTGR 341
                         410       420
                  ....*....|....*....|....*.
gi 386647928 1701 IDNQAKIR-GYRIETGEIETQLLKAE 1725
Cdd:cd17640   342 AKDTIVLSnGENVEPQPIEEALMRSP 367
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
261-747 4.87e-22

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 104.96  E-value: 4.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGAYVP 339
Cdd:PRK08751   26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  340 IDPEYPEERIRYMLEDSGTQVLLSQGHLQERVS--FSGTWIR----------LDDEEA----------------YHEDGS 391
Cdd:PRK08751  106 VNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQqvIADTPVKqvittglgdmLGFPKAalvnfvvkyvkklvpeYRINGA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  392 -------------NLESVN-GPEHLTYVIYTSGTTGKPKGNLTTHRNII-RVVKNTNYIDVTGQDK-----------LLQ 445
Cdd:PRK08751  186 irfrealalgrkhSMPTLQiEPDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMQQAHQWLAGTGKLEegcevvitalpLYH 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  446 LSSYSFDGSTFDIFGALlngAKLVLVPKetvlDVAKLAGLIEKQQISVMFITTAFFNVLVDmNP--DCLRHA--RAILFG 521
Cdd:PRK08751  266 IFALTANGLVFMKIGGC---NHLISNPR----DMPGFVKELKKTRFTAFTGVNTLFNGLLN-TPgfDQIDFSslKMTLGG 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  522 GERV--SVSHVRKALGHLgpgKIKHVYGPTESTVFATSYDVHEVEEGAvsiPIGGPISNTAIYIVNAQNKLQPIGVAGEL 599
Cdd:PRK08751  338 GMAVqrSVAERWKQVTGL---TLVEAYGLTETSPAACINPLTLKEYNG---SIGLPIPSTDACIKDDAGTVLAIGEIGEL 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  600 CVAGDGLARGYLNRPDLTAEKFadnpfaPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAI 679
Cdd:PRK08751  412 CIKGPQVMKGYWKRPEETAKVM------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928  680 -EKATVVVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK08751  486 lEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
555-834 5.90e-22

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 100.59  E-value: 5.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  555 ATSYDVHEVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFAPGERMYR 634
Cdd:COG3433     1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  635 TGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKL----EAIEKATVVVRESANGEKQLCAYYVADRSLPANE 710
Cdd:COG3433    81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLraaaVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  711 VRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGVEFVEPRTE---LEAGIVNIWKEILKI--EKIS 785
Cdd:COG3433   161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALEtalTEEELRADVAELLGVdpEEID 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928  786 VKDSFFELGGHSLRATTMVSRLhKELNISLPLRDVFRYPTVEKLAEAIS 834
Cdd:COG3433   241 PDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALLA 288
PRK07787 PRK07787
acyl-CoA synthetase; Validated
4902-5388 5.91e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 103.92  E-value: 5.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4902 EAAAVVYENDRLTYRELNERANRLARTLRAQGvkpnqLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLE 4981
Cdd:PRK07787   15 IADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4982 DSAASVLLTqthlqerAQQWGQtlqAALCLDDEAAYAEDASNVANVNePHDLAYVIYTSGTTGRPKGVMIEHRSLVNT-- 5059
Cdd:PRK07787   90 DSGAQAWLG-------PAPDDP---AGLPHVPVRLHARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADld 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5060 ----AAGYRRE----YRLDQFPV---------------RLLQLASFSFDVFvgdiARTLYNGGTMVI-CPkddridparl 5115
Cdd:PRK07787  159 alaeAWQWTADdvlvHGLPLFHVhglvlgvlgplrignRFVHTGRPTPEAY----AQALSEGGTLYFgVP---------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5116 hywiseekiTIFESTPAliipfmdyVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAID-SSL 5194
Cdd:PRK07787  225 ---------TVWSRIAA--------DPEAARALRGARLLVSGSAALPVPVFDRLAALTGH--RPVERYGMTETLITlSTR 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5195 YDEPlaklPEAGNVpiGKAALNAKFYIVDAHLNPVPVGV--LGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYR 5272
Cdd:PRK07787  286 ADGE----RRPGWV--GLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FR 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5273 TGDLARWMPDGNVDFIGRidnQA----KIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLcAHFTAESELKLS 5347
Cdd:PRK07787  354 TGDVAVVDPDGMHRIVGR---EStdliKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDlGQRIV-AYVVGADDVAAD 429
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928 5348 ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 5388
Cdd:PRK07787  430 ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
3880-4337 6.00e-22

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 104.90  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRD-AGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQ 3958
Cdd:PRK12492   50 LSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3959 RHLRERV----------------------SFAGTFV--AVDDEQ----AYH-------------ADGSNLEPV-VGPNHL 3996
Cdd:PRK12492  130 NMFGKLVqevlpdtgieylieakmgdllpAAKGWLVntVVDKVKkmvpAYHlpqavpfkqalrqGRGLSLKPVpVGLDDI 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3997 AYVIYTSGTTGKPKGVMVEHHGLCslklmfANTLQ--------------MTEQDRVVQFASL------SFDASCweifka 4056
Cdd:PRK12492  210 AVLQYTGGTTGLAKGAMLTHGNLV------ANMLQvraclsqlgpdgqpLMKEGQEVMIAPLplyhiyAFTANC------ 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4057 lffgATLYIPTSTTIL-----DYPLFESYMNENGITATI-LPPTYAAYLN-PD----RMPSLKKLITGGSAASVEFVQQW 4125
Cdd:PRK12492  278 ----MCMMVSGNHNVLitnprDIPGFIKELGKWRFSALLgLNTLFVALMDhPGfkdlDFSALKLTNSGGTALVKATAERW 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4126 KDKV--LYFNAYGPTEASIVTSiwdeaSDSLGDRKSV-PIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLN 4202
Cdd:PRK12492  354 EQLTgcTIVEGYGLTETSPVAS-----TNPYGELARLgTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQ 428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4203 RPELTAEKFvdnpfePGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANG 4282
Cdd:PRK12492  429 QPEATAEAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERS 502
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 4283 QQQlVAYFVAQRE--LTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK12492  503 GEA-VKLFVVARDpgLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2937-3121 6.59e-22

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 102.82  E-value: 6.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2937 WFFEpQFaEPH--HFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHkSENGyTAWNRaIGEGELYGLEVVDLKGI 3014
Cdd:cd19531    12 WFLD-QL-EPGsaAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFV-EVDG-EPVQV-ILPPLPLPLPVVDLSGL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3015 EESAQAVEAKA---NEIQSSIDLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFP 3090
Cdd:cd19531    87 PEAEREAEAQRlarEEARRPFDLARGPLLRATLLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLP 166
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 386647928 3091 AktdayrtWSEQLAAYA-------QSPVIERELAYWKR 3121
Cdd:cd19531   167 P-------LPIQYADYAvwqrewlQGEVLERQLAYWRE 197
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
8063-8289 6.71e-22

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 103.10  E-value: 6.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8063 TIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVE--FAVEY---SKADREEAVE-IAQRFVRPFDLRKP 8136
Cdd:cd19534    29 RVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelFRLEVvdlSSLAQAAAIEaLAAEAQSSLDLEEG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8137 PLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLY----AGEELP-PLRIQYKDYAAWQRSEAYAKRVKQQEG 8211
Cdd:cd19534   109 PLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYeqalAGEPIPlPSKTSFQTWAELLAEYAQSPALLEELA 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 8212 YWLQTLAGELPviELPTDYERTSTRSfegAELEFEADEALTQRL-NELAARHESTLYMVLLSAYTVLLSKYSGQEDIIV 8289
Cdd:cd19534   189 YWRELPAADYW--GLPKDPEQTYGDA---RTVSFTLDEEETEALlQEANAAYRTEINDLLLAALALAFQDWTGRAPPAI 262
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2484-2824 6.72e-22

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 101.69  E-value: 6.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2484 PNDLaYIIYTSGTTGKPKGVMVEHHGLCSLKQMFAN------TLQINAQDRVVQFASLSFDASC--------WEVFQTLF 2549
Cdd:cd05924     3 ADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMGGADfgtgefTPSEDAHKAAAAAAGTVMFPAPplmhgtgsWTAFGGLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2550 FGATLYIPTKETILDYQWfeRYMSDNGITTATL-PPTYAVYL-------NPDHMPDFKRLIAAGSASSLELLQQWKDKVK 2621
Cdd:cd05924    82 GGQTVVLPDDRFDPEEVW--RTIEKHKVTSMTIvGDAMARPLidalrdaGPYDLSSLFAISSGGALLSPEVKQGLLELVP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2622 Y---FNAYGPTEdsicttiwTPSTEDISQLKSVPIGGP--IVNHRIYIVDAHYQPVPVGVAGELCIAGVGL-ARGYLNRP 2695
Cdd:cd05924   160 NitlVDAFGSSE--------TGFTGSGHSAGSGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2696 DLTAEKF--VDnpfepGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDAS- 2772
Cdd:cd05924   232 AKTAETFpeVD-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERw 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 2773 GQKqlCAYFVADRT---MTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKID 2824
Cdd:cd05924   307 GQE--VVAVVQLREgagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
1297-1914 8.10e-22

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 105.56  E-value: 8.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1297 EVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVP 1376
Cdd:COG3319     1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1377 LDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAVLCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRP 1456
Cdd:COG3319    81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1457 KGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDRIDPARLHYWISEEKITI 1536
Cdd:COG3319   161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1537 FESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKLPEAG 1616
Cdd:COG3319   241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1617 NVPIGKAALnakfYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVD 1696
Cdd:COG3319   321 GPGLLVLLV----LLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLL 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1697 FIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYF 1776
Cdd:COG3319   397 GLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPAL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1777 VQLEQLPLTANGKIDRKALPAPDASmQTGMEYVAPRTPQEAKLASIWQEVLGLEKVGVKDNFFELGGHSLRATLLVGKVH 1856
Cdd:COG3319   477 LLLLLLLLLLLLAALLLAAAAPAAA-AAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLL 555
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 1857 KEMNVELPLRDVFRCSTVEEMAQAIARMEEQAYVSIPTVEEReyypvSSAQKRLYILH 1914
Cdd:COG3319   556 ALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRA-----GGSGPPLFCVH 608
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
5032-5380 8.47e-22

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 100.65  E-value: 8.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5032 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR--EYRLDQfpvRLLQLASF--SFDVFVGDIArTLYNGGTMVicPKD 5107
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADcaDLTEDD---RYLIINPFfhTFGYKAGIVA-CLLTGATVV--PVA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5108 DRIDPARLHYwISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfRIINAYGVTE 5187
Cdd:cd17638    75 VFDVDAILEA-IERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE-TVLTAYGLTE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5188 AAIdsslydeplAKLPEAGNVPI------GKAALNAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPELTEEKfvd 5261
Cdd:cd17638   153 AGV---------ATMCRPGDDAEtvattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEA--- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5262 spfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAE 5341
Cdd:cd17638   211 ---IDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 386647928 5342 SELKLSE--LRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:cd17638   288 PGVTLTEedVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
4443-4854 8.67e-22

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 102.77  E-value: 8.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4443 YPVSSAQKRLYILQQLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLRTGFELID-GEPVQRIYPEVDFAVET 4521
Cdd:cd19547     2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4522 VQASEQEA--------KAIVRDFIRPFDLAKPPLLRVGLIELAPERCILMLDMHHIVSDGVSADVLVEEFARLYsgEEL- 4592
Cdd:cd19547    82 LDWSGEDPdrraelleRLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVY--EELa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4593 ----PGLRI--QYKDYAVWQQseAQKEQLKRQEAYWLEAFRgELPvlemPTDYAR-PAVQSYAGDTLdfrmNSEISEGLK 4665
Cdd:cd19547   160 hgrePQLSPcrPYRDYVRWIR--ARTAQSEESERFWREYLR-DLT----PSPFSTaPADREGEFDTV----VHEFPEQLT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4666 RIAAES----GATLYMVLLAAYTVLLQKYTAQEDVIVGTPIAGRTH--ADLQSLIGMFVNTLAIRNYPAADKTFLSYLED 4739
Cdd:cd19547   229 RLVNEAargyGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLET 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4740 VKETTLGAFEHQTYPFEELVDKLQMARdLSRNPLFDTMFSLQNTenKEMHLPGLHLT--------PYPTEYGMSKFDLSL 4811
Cdd:cd19547   309 IHRDLATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENY--PEDNLPGDDLSiqiidlhaQEKTEYPIGLIVLPL 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 386647928 4812 dmmedsEGLECSLEFATALYKRETIERMAKHFEQLLTAIVNDP 4854
Cdd:cd19547   386 ------QKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
4912-5315 9.18e-22

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 103.21  E-value: 9.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 4991
Cdd:cd17640     5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 thlqeraqqwgqtlqaalclddeaayaedasnvanvNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNtaaGYRREYRLDQ 5071
Cdd:cd17640    85 ------------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHANLLH---QIRSLSDIVP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5072 FPV--RLLQL--------ASFSFDVFVGDIARTLynggTMVICPKDD--RIDParlHYWISEEKitIFESTPALII---- 5135
Cdd:cd17640   126 PQPgdRFLSIlpiwhsyeRSAEYFIFACGCSQAY----TSIRTLKDDlkRVKP---HYIVSVPR--LWESLYSGIQkqvs 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5136 ---PFMDYVAEHGLDMSSMVLLITSSDSCS---VTDYRVLqerfgsQFRIINAYGVTEAAIDSSlydepLAKLPEAGNVP 5209
Cdd:cd17640   197 kssPIKQFLFLFFLSGGIFKFGISGGGALPphvDTFFEAI------GIEVLNGYGLTETSPVVS-----ARRLKCNVRGS 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5210 IGKAALNAKFYIVDAHLN-PVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVEgerlyrTGDLARWMPDGNVDFI 5288
Cdd:cd17640   266 VGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFN------TGDLGWLTCGGELVLT 339
                         410       420
                  ....*....|....*....|....*...
gi 386647928 5289 GRIDNQAKIR-GYRIETGEIETQLLKAE 5315
Cdd:cd17640   340 GRAKDTIVLSnGENVEPQPIEEALMRSP 367
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6529-6723 1.04e-21

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 102.15  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6529 WFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGYAAWnRAIGEGELYSLEVadfRDVKS 6608
Cdd:cd19532    12 WFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPM-QGVLASSPLRLEH---VQISD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6609 AEQAVEAkANEIQSSI-DLEVGPLFKAGLFQCADGDHLLLV-IHHGVVDGVSWRILLEDVALGYEQAakgeevRLPAKTD 6686
Cdd:cd19532    88 EAEVEEE-FERLKNHVyDLESGETMRIVLLSLSPTEHYLIFgYHHIAMDGVSFQIFLRDLERAYNGQ------PLLPPPL 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 386647928 6687 SFRTWSE-QLAAYaQSPAMENERAYWEQIAQTAVAPLP 6723
Cdd:cd19532   161 QYLDFAArQRQDY-ESGALDEDLAYWKSEFSTLPEPLP 197
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
8035-8455 1.08e-21

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 105.90  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8035 PVSSAQKRLFILHQLEGAQQSYNIPGFATIEGPLDRDRFEAVFRQLIERHETLRTGFEMANGEPVQRVYSDVEFAV-EYS 8113
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLpEII 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8114 KADREEAVEIAQRFVRPFDLRKP-------PLLRVGLIEVEPERHILMLDMHHIISDGASVGILQEEFSRLYAG------ 8180
Cdd:PRK10252   89 DLRTQPDPHAAAQALMQADLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrgep 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8181 ---EELPPLRIQYKDYAAWQRSEAYAKrvkqQEGYWLQTLAGELPVIEL---PTDYERTSTRSfegAELEFEADEALTQR 8254
Cdd:PRK10252  169 tpaSPFTPFADVVEEYQRYRASEAWQR----DAAFWAEQRRQLPPPASLspaPLPGRSASADI---LRLKLEFTDGAFRQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8255 LneLAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTPVAGRTHADVEPIIGMFVNTLAIRNYPAGDKTFLSYLEEVKET 8334
Cdd:PRK10252  242 L--AAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 8335 TLGAFEHQDYPFEELVERLNvkRDASRNPVFDTMFVLQNTEDR----GIEADAFSLTPFVFDqtvaaqfDLTLSVAED-D 8409
Cdd:PRK10252  320 LKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVFDYQldfpGVQAQTHTLATGPVN-------DLELALFPDeH 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 386647928 8410 GAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLSQIQL 8455
Cdd:PRK10252  391 GGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDI 436
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
3854-4337 1.12e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 104.07  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3854 QTIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRD-AGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYI 3932
Cdd:PRK05677   24 PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3933 PIDPEYPEDRIRYMLEDSGAQALL---TQRHLRERV-------------------SFAGTFV--AVDDEQ----AYH--- 3981
Cdd:PRK05677  104 NTNPLYTAREMEHQFNDSGAKALVclaNMAHLAEKVlpktgvkhvivtevadmlpPLKRLLInaVVKHVKkmvpAYHlpq 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3982 ----------ADGSNLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHGLcslklmFANTLQMT-------EQDRVVQFAS 4043
Cdd:PRK05677  184 avkfndalakGAGQPVTEAnPQADDVAVLQYTGGTTGVAKGAMLTHRNL------VANMLQCRalmgsnlNEGCEILIAP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4044 L------SFDASCweIFKALFFGATLYIPTSTtilDYPLFESYMNENGITATI-LPPTYAAYLNPDRM-----PSLKKLI 4111
Cdd:PRK05677  258 LplyhiyAFTFHC--MAMMLIGNHNILISNPR---DLPAMVKELGKWKFSGFVgLNTLFVALCNNEAFrkldfSALKLTL 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4112 TGGSAASVEFVQQWKD----KVLyfNAYGPTEASIVTSIWDEASDSLGDrksvpIGRPLANHRIYVVDSHNRMLPVGVAG 4187
Cdd:PRK05677  333 SGGMALQLATAERWKEvtgcAIC--EGYGMTETSPVVSVNPSQAIQVGT-----IGIPVPSTLCKVIDDDGNELPLGEVG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4188 ELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKI- 4266
Cdd:PRK05677  406 ELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALp 479
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4267 DAVQEAIVLAREDANGQQqlVAYFVAQRE---LTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK05677  480 GVLQCAAIGVPDEKSGEA--IKVFVVVKPgetLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
PLN02246 PLN02246
4-coumarate--CoA ligase
7454-7930 1.12e-21

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 103.52  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7454 EQAERMPEKAAVVFENT--QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYP 7531
Cdd:PLN02246   31 ERLSEFSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7532 EDRIRYMLEDSGAQVLLTQ-------RHLQEcvSFDGKVIAADD---------EQAYGEDGSNLEPVVGPNHLAYVIYTS 7595
Cdd:PLN02246  111 PAEIAKQAKASGAKLIITQscyvdklKGLAE--DDGVTVVTIDDppegclhfsELTQADENELPEVEISPDDVVALPYSS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7596 GTTGKPKGVMVEHHGLCS--LKLMFAET--LRITEEDRVV----QFASLSFDAScweIFKALFFGATLYIPAK-DTILDY 7666
Cdd:PLN02246  189 GTTGLPKGVMLTHKGLVTsvAQQVDGENpnLYFHSDDVILcvlpMFHIYSLNSV---LLCGLRVGAAILIMPKfEIGALL 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7667 PLFESYmnenGIT-AAILPP-TYAIYLSPD----RLPSLKKLITGGSAASVEFVQQWKDKVRyfNA-----YGPTEASIV 7735
Cdd:PLN02246  266 ELIQRH----KVTiAPFVPPiVLAIAKSPVvekyDLSSIRMVLSGAAPLGKELEDAFRAKLP--NAvlgqgYGMTEAGPV 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7736 TSV---WAASPdgLDLRSVPIGRPIANHQIFIVDSQNHM-LPVGVAGELCISGAGLARGYLNRPELTAekfvdnpflage 7811
Cdd:PLN02246  340 LAMclaFAKEP--FPVKSGSCGTVVRNAELKIVDPETGAsLPRNQPGEICIRGPQIMKGYLNDPEATA------------ 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7812 rmyRTGDLARWLPDGNIEYL---------GRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV 7882
Cdd:PLN02246  406 ---NTIDKDGWLHTGDIGYIddddelfivDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV 482
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7883 --ADRELTVSELRGTLSQELPGY-MIPS-YFVqlEQMPLTPNGKIDRNALPA 7930
Cdd:PLN02246  483 rsNGSEITEDEIKQFVAKQVVFYkRIHKvFFV--DSIPKAPSGKILRKDLRA 532
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1314-1790 1.22e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 103.06  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1314 AAVVYENDR-LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLED 1392
Cdd:PRK08276    2 AVIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1393 SAASVLLTQTHLQERAQQWGQTLQA---VLCLD----------DEAAYAEDASNVANVNEPHDLAyviYTSGTTGRPKGV 1459
Cdd:PRK08276   82 SGAKVLIVSAALADTAAELAAELPAgvpLLLVVagpvpgfrsyEEALAAQPDTPIADETAGADML---YSSGTTGRPKGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 miehrslvntaagyRREY---RLDQFPVRLLQLASFSFDVFVGDI----------ARTLYN------GGTMVIcpkDDRI 1520
Cdd:PRK08276  159 --------------KRPLpglDPDEAPGMMLALLGFGMYGGPDSVylspaplyhtAPLRFGmsalalGGTVVV---MEKF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1521 DPARLHYWISEEKITIFESTPA-----LIIPfmDYVAEhGLDMSSMELLITSSDSCSVTDYRVLQERFGSqfrIINAY-- 1593
Cdd:PRK08276  222 DAEEALALIERYRVTHSQLVPTmfvrmLKLP--EEVRA-RYDVSSLRVAIHAAAPCPVEVKRAMIDWWGP---IIHEYya 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1594 -----GVTeaAIDSslyDEPLAKlpeAGNVpiGKAALnAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEK 1668
Cdd:PRK08276  296 sseggGVT--VITS---EDWLAH---PGSV--GKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1669 FVDSPFVEgerlyrTGDLarwmpdGNVD---FIGRIDNQAkirgYRIETG-------EIETQLLKAEGVREAVVVVREDA 1738
Cdd:PRK08276  365 RNPHGWVT------VGDV------GYLDedgYLYLTDRKS----DMIISGgvniypqEIENLLVTHPKVADVAVFGVPDE 428
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1739 K-GQKVLC----AYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 1790
Cdd:PRK08276  429 EmGERVKAvvqpADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
3879-4323 1.40e-21

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 102.43  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3879 QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLtq 3958
Cdd:cd05940     3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3959 rhlrervsfagtfvaVDdeqayhadgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRV 4038
Cdd:cd05940    81 ---------------VD--------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4039 VQFASLSFDAS---CWEifKALFFGATLYIPTSTTILDyplFESYMNENgiTATILPptYAA----YL--NP----DRMP 4105
Cdd:cd05940   126 YTCLPLYHSTAlivGWS--ACLASGATLVIRKKFSASN---FWDDIRKY--QATIFQ--YIGelcrYLlnQPpkptERKH 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4106 SLKKLITGGSAASV--EFVQQWKD-KVLYFnaYGPTEASIvtsiwdeasdSLGDRKSVP--IGR------PLANHRIYVV 4174
Cdd:cd05940   197 KVRMIFGNGLRPDIweEFKERFGVpRIAEF--YAATEGNS----------GFINFFGKPgaIGRnpsllrKVAPLALVKY 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4175 DSHN-----------RMLPVGVAGELC--ISGVGLARGYLNrPELTAEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLG 4241
Cdd:cd05940   265 DLESgepirdaegrcIKVPRGEPGLLIsrINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVD 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4242 RIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLARE--DANGQQQLVAYFVAQ-RELTAAELRATMSQELPNYMIPsYF 4318
Cdd:cd05940   344 RLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpGTDGRAGMAAIVLQPnEEFDLSALAAHLEKNLPGYARP-LF 422

                  ....*
gi 386647928 4319 VQLAQ 4323
Cdd:cd05940   423 LRLQP 427
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4913-5385 1.42e-21

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 102.21  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTqt 4992
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 hlqeraqqwgqtlqaalclddeaayaeDASNVANVNEphDLAYVIYTSGTTGRPKGVMIEHRSLV------NTAAGYRRE 5066
Cdd:cd05973    79 ---------------------------DAANRHKLDS--DPFVMMFTSGTTGLPKGVPVPLRALAafgaylRDAVDLRPE 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5067 yrlDQF-----PVRLLQLASFSFDVFVGDIARTLYNGGTMVicPKDDRIdparlhywISEEKITIFESTPALIIPFMDYV 5141
Cdd:cd05973   130 ---DSFwnaadPGWAYGLYYAITGPLALGHPTILLEGGFSV--ESTWRV--------IERLGVTNLAGSPTAYRLLMAAG 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5142 AEHGLDMSSMVLLITSSDSCSVTDY-RVLQERFGSQFRiiNAYGVTEAA--IDSSLYDEPLAKLPEAGNVPIGKaalnaK 5218
Cdd:cd05973   197 AEVPARPKGRLRRVSSAGEPLTPEViRWFDAALGVPIH--DHYGQTELGmvLANHHALEHPVHAGSAGRAMPGW-----R 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5219 FYIVDAHLNPVPVGVLGELcigGIGVAR-------GYLNRpelteekfvDSPFVEGeRLYRTGDLARWMPDGNVDFIGRI 5291
Cdd:cd05973   270 VAVLDDDGDELGPGEPGRL---AIDIANsplmwfrGYQLP---------DTPAIDG-GYYLTGDTVEFDPDGSFSFIGRA 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5292 DNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED------AKGQKVLCAHFTAESELKlSELRSSLSQELPGYMIPSY 5365
Cdd:cd05973   337 DDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDpertevVKAFVVLRGGHEGTPALA-DELQLHVKKRLSAHAYPRT 415
                         490       500
                  ....*....|....*....|
gi 386647928 5366 FVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05973   416 IHFVDELPKTPSGKIQRFLL 435
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1307-1797 1.54e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 103.15  E-value: 1.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 1386
Cdd:PRK13383   45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QFMLEDSAASVLLTQthlQERAQQWGQTLQAVLCLDDEAAYAEDASNVANVNEPHDLayVIYTSGTTGRPKGVmiEHRSL 1466
Cdd:PRK13383  125 AAALRAHHISTVVAD---NEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRI--VLLTSGTTGKPKGV--PRAPQ 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1467 VNTAAGYRREYrLDQFPVRLLQLASFSFDVF----VGDIARTLYNGGTMVICPKDD---RIDPARLHywiSEEKITIFES 1539
Cdd:PRK13383  198 LRSAVGVWVTI-LDRTRLRTGSRISVAMPMFhglgLGMLMLTIALGGTVLTHRHFDaeaALAQASLH---RADAFTAVPV 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1540 TPALIIPFMDYVAEHGlDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDSSLYDEPLAKLPEAgnvp 1619
Cdd:PRK13383  274 VLARILELPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTYGDI--LYNGYGSTEVGIGALATPADLRDAPET---- 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1620 IGKAALNAKFYIVDAHLNPVPVGVLGELCIGGigvargylnrpELTEEKFVD---SPFVEGerLYRTGDLARWMPDGNVD 1696
Cdd:PRK13383  347 VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG-----------ELAGTRYTDgggKAVVDG--MTSTGDMGYLDNAGRLF 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1697 FIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAE--SELKLSELRSSLSQELPGYMIPS 1774
Cdd:PRK13383  414 IVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHpgSGVDAAQLRDYLKDRVSRFEQPR 493
                         490       500
                  ....*....|....*....|...
gi 386647928 1775 YFVQLEQLPLTANGKIDRKALPA 1797
Cdd:PRK13383  494 DINIVSSIPRNPTGKVLRKELPG 516
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
405-744 2.11e-21

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 100.03  E-value: 2.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 VIYTSGTTGKPKGNLTTHRNIIRVVKN--TNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKL 482
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKTFFAVPDIlqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSLFK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  483 AGLIEKQQISVMFITTafFNVLVDMNPDCLRHA---RAILFGGERVSVSHVRKALGHlGPGKIKHVYGPTE-STVFATSY 558
Cdd:cd17635    86 ILTTNAVTTTCLVPTL--LSKLVSELKSANATVpslRLIGYGGSRAIAADVRFIEAT-GLTNTAQVYGLSEtGTALCLPT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  559 DVHEVEEGAVsipiGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDL 638
Cdd:cd17635   163 DDDSIEINAV----GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------NTGDL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  639 ARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSLPANEVRS---TL 715
Cdd:cd17635   232 GERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRAlkhTI 311
                         330       340
                  ....*....|....*....|....*....
gi 386647928  716 SQELPAYMLPSYFVQLEQMPLTTNGKVDR 744
Cdd:cd17635   312 RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
4903-5380 2.74e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 102.29  E-value: 2.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4903 AAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLED 4982
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4983 SAASVLLTQTHLQERAQQWGQTLQAAlcLDDEAAYAEDASNVANVNE------PHDLAYVI------YTSGTTGRPKGVm 5050
Cdd:PRK08276   82 SGAKVLIVSAALADTAAELAAELPAG--VPLLLVVAGPVPGFRSYEEalaaqpDTPIADETagadmlYSSGTTGRPKGI- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5051 iehrslvntaagyRREY---RLDQFPVRLLQLASFSFDVFVGDI----------ARTLYN------GGTMVIcpkDDRID 5111
Cdd:PRK08276  159 -------------KRPLpglDPDEAPGMMLALLGFGMYGGPDSVylspaplyhtAPLRFGmsalalGGTVVV---MEKFD 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5112 PARLHYWISEEKITIFESTPA-----LIIPfmDYVAEhGLDMSSMVLLITSSDSCSVTDYRVLQERFGSqfrIINAY--- 5183
Cdd:PRK08276  223 AEEALALIERYRVTHSQLVPTmfvrmLKLP--EEVRA-RYDVSSLRVAIHAAAPCPVEVKRAMIDWWGP---IIHEYyas 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5184 ----GVTeaAIDSslyDEPLAKlpeAGNVpiGKAALnAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKF 5259
Cdd:PRK08276  297 seggGVT--VITS---EDWLAH---PGSV--GKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAAR 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5260 VDSPFVEgerlyrTGDLarwmpdGNVD---FIGRIDNQAkirgYRIETG-------EIETQLLKAEGVREAVVVVREDAK 5329
Cdd:PRK08276  366 NPHGWVT------VGDV------GYLDedgYLYLTDRKS----DMIISGgvniypqEIENLLVTHPKVADVAVFGVPDEE 429
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 5330 -GQKVLC----AHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:PRK08276  430 mGERVKAvvqpADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1303-1726 3.20e-21

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 102.65  E-value: 3.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1303 FEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 1382
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLEDSAASVLL-----------TQTHLQERAQQW---GQTLQAVLCLDDEAAYAEDASNVANVNEPH----DLA 1444
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIvgeelveafeeARADLARPPRLWvagGDTLDDPEGYEDLAAAAAGAPTTNPASRSGvtakDTA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1445 YVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL---DQFPVRLLQLASFSFDVFVGDiarTLYNGGTMVICPKDDrid 1521
Cdd:PRK08279  203 FYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLtpdDVLYCCLPLYHNTGGTVAWSS---VLAAGATLALRRKFS--- 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1522 pARlHYW--ISEEKITIFEstpaliipfmdYVAehgldmssmEL---LITSSDSCSVTDYRV---------------LQE 1581
Cdd:PRK08279  277 -AS-RFWddVRRYRATAFQ-----------YIG---------ELcryLLNQPPKPTDRDHRLrlmignglrpdiwdeFQQ 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1582 RFGSQfRIINAYGVTEAAIdsSLYDEpLAKLPEAGNVPigkAALNAKFYIV-------------DAHLNPVPVGVLGELc 1648
Cdd:PRK08279  335 RFGIP-RILEFYAASEGNV--GFINV-FNFDGTVGRVP---LWLAHPYAIVkydvdtgepvrdaDGRCIKVKPGEVGLL- 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1649 IGGIGVAR---GYlNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAE 1725
Cdd:PRK08279  407 IGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFP 485

                  .
gi 386647928 1726 G 1726
Cdd:PRK08279  486 G 486
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
5953-6438 3.21e-21

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 102.78  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5953 AVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGL---MVErslEMVVGMIAILKAG-------GAYVP------ID 6016
Cdd:cd05967    75 PVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympMIP---EAAIAMLACARIGaihsvvfGGFAAkelasrID 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6017 ---------PDY---PEDRIRYM-LEDSGAKLLLVQGH---LLDRASFADKLVNLNDDGAYHEDGSNLEPVN----GPEH 6076
Cdd:cd05967   152 dakpklivtASCgiePGKVVPYKpLLDKALELSGHKPHhvlVLNRPQVPADLTKPGRDLDWSELLAKAEPVDcvpvAATD 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6077 LTYVIYTSGTTGRPKGvmvehrnVVRlvKNTNY-VELN-EQTHI--LQTGAVVFDAS--------TFEIWGALLNGgrly 6144
Cdd:cd05967   232 PLYILYTSGTTGKPKG-------VVR--DNGGHaVALNwSMRNIygIKPGDVWWAASdvgwvvghSYIVYGPLLHG---- 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6145 vvrNETIL---------DAVSLKNAIQQYGINTMWlTAPL-YNQLSQQDSGMFAG-------LKTLIVGGDVLSVPHINR 6207
Cdd:cd05967   299 ---ATTVLyegkpvgtpDPGAFWRVIEKYQVNALF-TAPTaIRAIRKEDPDGKYIkkydlssLRTLFLAGERLDPPTLEW 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6208 VlREHAGLSIVNGYGPTEnTTFSTTHTIVGEQKEAVPIGKPINNSTAY---IVDSKLSLLPVGVWGELIVGGDgVARGYL 6284
Cdd:cd05967   375 A-ENTLGVPVIDHWWQTE-TGWPITANPVGLEPLPIKAGSPGKPVPGYqvqVLDEDGEPVGPNELGNIVIKLP-LPPGCL 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6285 NRPELTAEKFVESSF--LPGerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VRE 6361
Cdd:cd05967   452 LTLWKNDERFKKLYLskFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVgVRD 529
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6362 DESGQKQLCaYFVAERELTI------GELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPAPQGnapvGAEYVA 6435
Cdd:cd05967   530 ELKGQVPLG-LVVLKEGVKItaeeleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIAD----GEDYTI 604

                  ...
gi 386647928 6436 PRT 6438
Cdd:cd05967   605 PST 607
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
7472-7828 3.21e-21

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 102.29  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGV--QADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLlt 7549
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIV-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7550 qrhlqeCVSFDGKVIAADDEQAYGEDgsNLEPVV--GPNHLAYVIYTSGTTGKPKGVMVEHHGLCS----LKLMFAETLR 7623
Cdd:cd05927    84 ------FCDAGVKVYSLEEFEKLGKK--NKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEILNK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7624 ITEEDRVVQFASLS--FDASCWEIFkaLFFGA---------------------TLYI--P--------------AKDTIL 7664
Cdd:cd05927   156 INPTDVYISYLPLAhiFERVVEALF--LYHGAkigfysgdirlllddikalkpTVFPgvPrvlnriydkifnkvQAKGPL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7665 DYPLF-------ESYMNENGITAailpptyaiylSP--DRL----------PSLKKLITGGSAASVEFVqqwkDKVRY-- 7723
Cdd:cd05927   234 KRKLFnfalnykLAELRSGVVRA-----------SPfwDKLvfnkikqalgGNVRLMLTGSAPLSPEVL----EFLRVal 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7724 ----FNAYGPTEASIVTSVwaASPDGLDLRSVpiGRPIANHQIFIVDSQN----HMLPVGvAGELCISGAGLARGYLNRP 7795
Cdd:cd05927   299 gcpvLEGYGQTECTAGATL--TLPGDTSVGHV--GGPLPCAEVKLVDVPEmnydAKDPNP-RGEVCIRGPNVFSGYYKDP 373
                         410       420       430
                  ....*....|....*....|....*....|...
gi 386647928 7796 ELTAEKFVDNPFLagermyRTGDLARWLPDGNI 7828
Cdd:cd05927   374 EKTAEALDEDGWL------HTGDIGEWLPNGTL 400
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
6080-6415 4.22e-21

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 98.73  E-value: 4.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6080 VIYTSGTTGRPKGVMVEHRNVVRLVK----------NTNYVELNEQTHIL--QTGAVVfdastfeiwgALLNGGRLYvvr 6147
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHRQTLRAAAawadcadlteDDRYLIINPFFHTFgyKAGIVA----------CLLTGATVV--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6148 NETILDAVSLKNAIQQYGInTMWLTAP-LYNQL---SQQDSGMFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGP 6223
Cdd:cd17638    72 PVAVFDVDAILEAIERERI-TVLPGPPtLFQSLldhPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6224 TENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSklsllpvgvwGELIVGGDGVARGYLNRPELTAEKFVESSFLpge 6303
Cdd:cd17638   151 TEAGVATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL--- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6304 rcyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIGE 6383
Cdd:cd17638   218 ---HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTE 294
                         330       340       350
                  ....*....|....*....|....*....|....
gi 386647928 6384 --LRAALSQELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:cd17638   295 edVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
5525-5801 4.41e-21

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 100.26  E-value: 4.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5525 LDRGKLEEAFRQLIARHETLRTGFeLVNGEpvQRVYKEVN---FAVEHYRTSEAEAGEV----VRGFV--RTFDLAKPPL 5595
Cdd:cd19535    37 LDPDRLERAWNKLIARHPMLRAVF-LDDGT--QQILPEVPwygITVHDLRGLSEEEAEAaleeLRERLshRVLDVERGPL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5596 LRVGLVELAEDLHILLLDMHHIVSDGVSTDVLTEEFGRMY--NGESLAPLRIQYKDYATWQQSEAQQEQmKRQEAYW--- 5670
Cdd:cd19535   114 FDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYedPGEPLPPLELSFRDYLLAEQALRETAY-ERARAYWqer 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5671 LDMFRG--ELPVLELPTDYPRPAVRKfegslLQRQLEPKLGEGLQRIAAESGATLYMVLLAAYKVLLQKYTGQEDIVVGT 5748
Cdd:cd19535   193 LPTLPPapQLPLAKDPEEIKEPRFTR-----REHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNL 267
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 5749 PIAGR--THSDLQPIIGMFVNT--LAIRsyPDDKKTFRSFLDEVKETMLGAYEHQSY 5801
Cdd:cd19535   268 TLFNRlpLHPDVNDVVGDFTSLllLEVD--GSEGQSFLERARRLQQQLWEDLDHSSY 322
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1302-1795 5.04e-21

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 101.61  E-value: 5.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1302 LFEKQAErtPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGgaYVPLDPDY 1381
Cdd:PRK10946   30 ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALF 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1382 PSDRIQF-----------MLEDSAASVLLTQTHLQERAQQWGqTLQAVLCLDD------EAAYAEDASNVANVNEPHD-L 1443
Cdd:PRK10946  106 SHQRSELnayasqiepalLIADRQHALFSDDDFLNTLVAEHS-SLRVVLLLNDdgehslDDAINHPAEDFTATPSPADeV 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1444 AYVIYTSGTTGRPKGVMIEH--------RSlvNTAAGYRREYRL-------DQFPvrllqLAS-FSFDVFvgdiartlYN 1507
Cdd:PRK10946  185 AFFQLSGGSTGTPKLIPRTHndyyysvrRS--VEICGFTPQTRYlcalpaaHNYP-----MSSpGALGVF--------LA 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1508 GGTMVICPkddriDPARLHYW--ISEEKITIFESTPALIIPFMDYVAE--HGLDMSSMELLITSSDSCSVTDYRVLQERF 1583
Cdd:PRK10946  250 GGTVVLAP-----DPSATLCFplIEKHQVNVTALVPPAVSLWLQAIAEggSRAQLASLKLLQVGGARLSETLARRIPAEL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1584 GSQFRiiNAYGVTEAAIDSSLYDEPLAKLPEAGNVPIgkaALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPE 1663
Cdd:PRK10946  325 GCQLQ--QVFGMAEGLVNYTRLDDSDERIFTTQGRPM---SPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1664 LTEEKFvDSpfvegERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQK 1742
Cdd:PRK10946  400 HNASAF-DA-----NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEK 473
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 1743 VlCAYFTAESELKLSELRSSL-SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK10946  474 S-CAFLVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
4909-5387 5.17e-21

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 101.90  E-value: 5.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4909 ENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVL 4988
Cdd:PRK04319   70 RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4989 LTQTHLQER--AQQWgQTLQAALCLDDEA-------------AYAEDASNVANVnEPHDLAYVIYTSGTTGRPKGV---- 5049
Cdd:PRK04319  150 ITTPALLERkpADDL-PSLKHVLLVGEDVeegpgtldfnalmEQASDEFDIEWT-DREDGAILHYTSGSTGKPKGVlhvh 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5050 --MIEHRslvntAAGYrreYRLDQFPVrllqlasfsfDVF-------------VGDIArTLYNGGTMVIcpKDDRIDPAR 5114
Cdd:PRK04319  228 naMLQHY-----QTGK---YVLDLHED----------DVYwctadpgwvtgtsYGIFA-PWLNGATNVI--DGGRFSPER 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5115 LHYWISEEKITIFESTPALIIPFMdyvaEHGLDMssmvllitssdscsVTDYRVlqerfgSQFRIINAYGvteaaidssl 5194
Cdd:PRK04319  287 WYRILEDYKVTVWYTAPTAIRMLM----GAGDDL--------------VKKYDL------SSLRHILSVG---------- 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5195 ydEPLAklPEAgnVPIGKAALNAKFY------------------------------------IVDAHLNPVPVGVLGELC 5238
Cdd:PRK04319  333 --EPLN--PEV--VRWGMKVFGLPIHdnwwmtetggimianypamdikpgsmgkplpgieaaIVDDQGNELPPNRMGNLA 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5239 I--GGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEG 5316
Cdd:PRK04319  407 IkkGWPSMMRGIWNNPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPA 479
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 5317 VREAVVVVREDA-KGQKV-----LCAHFTAESELKLsELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 5387
Cdd:PRK04319  480 VAEAGVIGKPDPvRGEIIkafvaLRPGYEPSEELKE-EIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
3847-4337 6.19e-21

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 101.49  E-value: 6.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3847 AAEYQQEQ--TIHGLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLAR-TLRDAGVRPDQLVGLMVERSLEMVVGIMA 3923
Cdd:PRK08751   16 AAEIDLEQfrTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3924 IMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRHL-----------------------------RERVSFAGTFVA- 3973
Cdd:PRK08751   96 VLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFgttvqqviadtpvkqvittglgdmlgfpkAALVNFVVKYVKk 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3974 -VDDeqaYHADGS-------------NLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMT---EQ 4035
Cdd:PRK08751  176 lVPE---YRINGAirfrealalgrkhSMPTLqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTgklEE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4036 DRVVQFASLSFdascWEIFkALFFGATLYIPTS------TTILDYPLFESYMNENGITA-TILPPTYAAYLNP---DRM- 4104
Cdd:PRK08751  253 GCEVVITALPL----YHIF-ALTANGLVFMKIGgcnhliSNPRDMPGFVKELKKTRFTAfTGVNTLFNGLLNTpgfDQId 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4105 -PSLKKLITGGSAASVEFVQQWKD--KVLYFNAYGPTEASIVTSI----WDEASDSlgdrksvpIGRPLANHRIYVVDSH 4177
Cdd:PRK08751  328 fSSLKMTLGGGMAVQRSVAERWKQvtGLTLVEAYGLTETSPAACInpltLKEYNGS--------IGLPIPSTDACIKDDA 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4178 NRMLPVGVAGELCISGVGLARGYLNRPELTAeKFVDnpfepGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELG 4257
Cdd:PRK08751  400 GTVLAIGEIGELCIKGPQVMKGYWKRPEETA-KVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPN 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4258 EVETQLAKIDAVQE-AIVLAREDANGQQQLVAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKA 4336
Cdd:PRK08751  474 EIEDVIAMMPGVLEvAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRE 553

                  .
gi 386647928 4337 L 4337
Cdd:PRK08751  554 L 554
PRK08315 PRK08315
AMP-binding domain protein; Validated
254-742 6.41e-21

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 101.43  E-value: 6.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  254 TDYP-RDTTIHRLFEEQAERRPDAVAVTFEDRQL--TYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGI 330
Cdd:PRK08315    9 TDVPlLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFAT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  331 LKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLS------------------------QGHLQ-ERVSFSGTWIRLDDEE- 384
Cdd:PRK08315   89 AKIGAILVTINPAYRLSELEYALNQSGCKALIAadgfkdsdyvamlyelapelatcePGQLQsARLPELRRVIFLGDEKh 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  385 ------------AYHEDGSNLESVNGPEHLTYVI---YTSGTTGKPKGNLTTHRNIIrvvkNTNY-----IDVTGQDKL- 443
Cdd:PRK08315  169 pgmlnfdellalGRAVDDAELAARQATLDPDDPIniqYTSGTTGFPKGATLTHRNIL----NNGYfigeaMKLTEEDRLc 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  444 LQLSSYSFDGSTFDIFGALLNGAKLVLV-----PKETVLDVAK-----LAGliekqqISVMFIttAFFNvlvdmNPD--- 510
Cdd:PRK08315  245 IPVPLYHCFGMVLGNLACVTHGATMVYPgegfdPLATLAAVEEerctaLYG------VPTMFI--AELD-----HPDfar 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  511 ----CLRhaRAILFGgervSVSHV---RKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAVSIpIGGPISNTAIYI 583
Cdd:PRK08315  312 fdlsSLR--TGIMAG----SPCPIevmKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLEKRVTT-VGRALPHLEVKI 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  584 VN-AQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADnpfapgERMYRTGDLARWLPDGTIEYVGRIDDQVkIRGf 662
Cdd:PRK08315  385 VDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDA------DGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG- 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  663 rielG------EIEAHLLKLEAIEKATVV-VRESANGEkQLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQ 733
Cdd:PRK08315  457 ----GeniyprEIEEFLYTHPKIQDVQVVgVPDEKYGE-EVCAWIIlrPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDE 531

                  ....*....
gi 386647928  734 MPLTTNGKV 742
Cdd:PRK08315  532 FPMTVTGKI 540
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
6523-6838 6.46e-21

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 99.87  E-value: 6.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6523 LTPIQRWFF-----DQSLADLH-HFNQAFmlhRKDRFDEAALRQVLQKLAEHHDALRTVFrkSENGYaawNRAIGEGELY 6596
Cdd:cd19535     4 LTDVQYAYWigrqdDQELGGVGcHAYLEF---DGEDLDPDRLERAWNKLIARHPMLRAVF--LDDGT---QQILPEVPWY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6597 SLEVADFRDVksAEQAVEAKANEIQSS-----IDLEVGPLFKAGLFQCADGDHLLLV-IHHGVVDGVSWRILLEDVALGY 6670
Cdd:cd19535    76 GITVHDLRGL--SEEEAEAALEELRERlshrvLDVERGPLFDIRLSLLPEGRTRLHLsIDLLVADALSLQILLRELAALY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6671 EQAakgeEVRLPAKTDSFRTWSEQLAAYAQSpAMENERAYW-EQIAQTAVAP-LPkdkqsdrsLQQDSESIT-IQWSRKE 6747
Cdd:cd19535   154 EDP----GEPLPPLELSFRDYLLAEQALRET-AYERARAYWqERLPTLPPAPqLP--------LAKDPEEIKePRFTRRE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6748 TE------QLLKKVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDitRTVGWFTSkyPVLLQMEP 6821
Cdd:cd19535   221 HRlsaeqwQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVN--DVVGDFTS--LLLLEVDG 296
                         330
                  ....*....|....*....
gi 386647928 6822 --GRSLSTRIKKVKEDLRR 6838
Cdd:cd19535   297 seGQSFLERARRLQQQLWE 315
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
405-742 6.67e-21

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 97.96  E-value: 6.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 VIYTSGTTGKPKGNLTTHRNIIRVVKN-TNYIDVTGQDKLLQLSSY--SFdGSTFDIFGALLNGAKLVlvpKETVLDVAK 481
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHRQTLRAAAAwADCADLTEDDRYLIINPFfhTF-GYKAGIVACLLTGATVV---PVAVFDVDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  482 LAGLIEKQQISVMFITTAFFNVLVDmNPDC----LRHARAILFGGERVSVSHVRKALGHLGPGKIKHVYGPTESTVFATS 557
Cdd:cd17638    81 ILEAIERERITVLPGPPTLFQSLLD-HPGRkkfdLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  558 YDVHEVEEgaVSIPIGGPISNTAIYIVNaqnklqpigvAGELCVAGDGLARGYLNRPDLTAEKF-ADNpfapgerMYRTG 636
Cdd:cd17638   160 RPGDDAET--VATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIdADG-------WLHTG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  637 DLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKQlCAYYVA--DRSLPANEVRS 713
Cdd:cd17638   221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgVPDERMGEVG-KAFVVArpGVTLTEEDVIA 299
                         330       340
                  ....*....|....*....|....*....
gi 386647928  714 TLSQELPAYMLPSYFVQLEQMPLTTNGKV 742
Cdd:cd17638   300 WCRERLANYKVPRFVRFLDELPRNASGKV 328
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
286-685 6.82e-21

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 99.95  E-value: 6.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPidpeypeerirymledsgTQVLLSQG 365
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  366 HLQERVSfSGTWIRLDDEEAYHEDGSNLesvngpehltyVIYTSGTTGKPKGNLTTHRNIIRVVKNTNY-IDVTGQDKLL 444
Cdd:cd05974    63 DLRDRVD-RGGAVYAAVDENTHADDPML-----------LYFTSGTTSKPKLVEHTHRSYPVGHLSTMYwIGLKPGDVHW 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  445 QLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRHA-RAILFGGE 523
Cdd:cd05974   131 NISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKlREVVGAGE 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  524 RVS---VSHVRKALGHlgpgKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGGpisntaiYIVNAqnkLQPIGVA---G 597
Cdd:cd05974   211 PLNpevIEQVRRAWGL----TIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPG-------YRVAL---LDPDGAPateG 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  598 ELC-VAGD----GLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAH 672
Cdd:cd05974   277 EVAlDLGDtrpvGLMKGYAGDPDKTAHAMRGG-------YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESV 349
                         410
                  ....*....|...
gi 386647928  673 LLKLEAIEKATVV 685
Cdd:cd05974   350 LIEHPAVAEAAVV 362
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
3869-4337 6.98e-21

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 101.06  E-value: 6.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3869 DAVAVVfeksQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLE 3948
Cdd:cd17642    38 DAHTGV----NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLN 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3949 DSGAQALLTQRHLRERV-------SFAGTFVAVD---DEQAYHADGSNLEPVVGPNHLAY---------------VIYTS 4003
Cdd:cd17642   114 ISKPTIVFCSKKGLQKVlnvqkklKIIKTIIILDskeDYKGYQCLYTFITQNLPPGFNEYdfkppsfdrdeqvalIMNSS 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4004 GTTGKPKGVMVEHHGLCS-----LKLMFANtlQMTEQDRVVQFASLSFDASCWEIFKALFFGATL-YIPTsttiLDYPLF 4077
Cdd:cd17642   194 GSTGLPKGVQLTHKNIVArfshaRDPIFGN--QIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVvLMYK----FEEELF 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4078 ESYMNENGITATILPPTYAAYLNPDR------MPSLKKLITGGSAASVEFVQQWKDKV-LYF--NAYGPTEASIVTSIWD 4148
Cdd:cd17642   268 LRSLQDYKVQSALLVPTLFAFFAKSTlvdkydLSNLHEIASGGAPLSKEVGEAVAKRFkLPGirQGYGLTETTSAILITP 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4149 EasdslGDRKSVPIGRPLANHRIYVVD-SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGD 4227
Cdd:cd17642   348 E-----GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGW------LHSGD 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4228 LVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQ--RELTAAEL---- 4301
Cdd:cd17642   417 IAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEagKTMTEKEVmdyv 496
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 386647928 4302 --RATMSQELPNYMIpsyFVQlaQMPLTPNGKIDRKAL 4337
Cdd:cd17642   497 asQVSTAKRLRGGVK---FVD--EVPKGLTGKIDRRKI 529
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2369-2738 7.63e-21

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 100.23  E-value: 7.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2369 QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVlla 2448
Cdd:cd05910     1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDA--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2449 qrrlqervsFAGtvVTVDDEQAYagdgsnlesavgpndlayIIYTSGTTGKPKGVMVEHhglcslkQMFANtlQINAQDR 2528
Cdd:cd05910    78 ---------FIG--IPKADEPAA------------------ILFTSGSTGTPKGVVYRH-------GTFAA--QIDALRQ 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2529 VVQFASLSFDASCWEVFqTLF---FGATLYIP----TKETILDYQWFERYMSDNGITTATLPP------TYAVYLNPDHM 2595
Cdd:cd05910   120 LYGIRPGEVDLATFPLF-ALFgpaLGLTSVIPdmdpTRPARADPQKLVGAIRQYGVSIVFGSPallervARYCAQHGITL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2596 PDFKRLIAAGSASSLELLQQWK----DKVKYFNAYGPTEDSICTTI-----WTPSTEDISQLKSVPIGGPIVNHRIYIVD 2666
Cdd:cd05910   199 PSLRRVLSAGAPVPIALAARLRkmlsDEAEILTPYGATEALPVSSIgsrelLATTTAATSGGAGTCVGRPIPGVRVRIIE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2667 AHYQP---------VPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfEPGERM-YRTGDLAKWLPDGTIEYLGRIDH 2736
Cdd:cd05910   279 IDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKID---DNSEGFwHRMGDLGYLDDEGRLWFCGRKAH 355

                  ..
gi 386647928 2737 QV 2738
Cdd:cd05910   356 RV 357
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
5956-6420 8.12e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 100.75  E-value: 8.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5956 FEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKL 6035
Cdd:PRK08276    7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6036 LLVQGHLLDRASFADKL------VNLNDDGA------YHEDGSNLEPVNGPEHL--TYVIYTSGTTGRPKGVMVEHRNVV 6101
Cdd:PRK08276   87 LIVSAALADTAAELAAElpagvpLLLVVAGPvpgfrsYEEALAAQPDTPIADETagADMLYSSGTTGRPKGIKRPLPGLD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6102 RLVKNTNYVELNEQTHILQTGAVVFDASTF-----EIWG--ALLNGGRLYVVRNetiLDAVSLKNAIQQYGINTmwltap 6174
Cdd:PRK08276  167 PDEAPGMMLALLGFGMYGGPDSVYLSPAPLyhtapLRFGmsALALGGTVVVMEK---FDAEEALALIERYRVTH------ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6175 lynqlSQQDSGMFAGLKTLI----VGGDVLSV-----------PHINRVLREHAGLSIVNGYGPTE--NTTFSTThtivg 6237
Cdd:PRK08276  238 -----SQLVPTMFVRMLKLPeevrARYDVSSLrvaihaaapcpVEVKRAMIDWWGPIIHEYYASSEggGVTVITS----- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6238 EQKEAVP--IGKPInNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGDLArWL 6315
Cdd:PRK08276  308 EDWLAHPgsVGKAV-LGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW------VTVGDVG-YL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6316 -PDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQK-----QLCAYFVAERELTiGELRAAL 6388
Cdd:PRK08276  380 dEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgVPDEEMGERvkavvQPADGADAGDALA-AELIAWL 458
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 6389 SQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK08276  459 RGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
6992-7412 8.14e-21

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 99.18  E-value: 8.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAGAyfeqmrFTV------QGSLDAEQFARSWNDLVARHAILRTNFFSGPRGepLQIVYRDKRI 7065
Cdd:cd19537     4 LSPIEREWWHKYQLSTGTSS------FNVsfacrlSGDVDRDRLASAWNTVLARHRILRSRYVPRDGG--LRRSYSSSPP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7066 gfvyedlshlpaderqaSVERLEQEDIA----RGFDLEQDALVRVAVirTQETsyrVLWSFHHILMDGWCLPLVVKELFE 7141
Cdd:cd19537    76 -----------------RVQRVDTLDVWkeinRPFDLEREDPIRVFI--SPDT---LLVVMSHIICDLTTLQLLLREVSA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7142 TYeayvQGDRPEQkAAPAYSQYIEWlENQDSAAASAYWSNYLAGYEgqtaLPQEKAQKRSEGYVAEHVVCELDKELSERM 7221
Cdd:cd19537   134 AY----NGKLLPP-VRREYLDSTAW-SRPASPEDLDFWSEYLSGLP----LLNLPRRTSSKSYRGTSRVFQLPGSLYRSL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7222 NRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEipGIEEMIGLFINTIPVRV--ACQPEESFADVMGRM 7299
Cdd:cd19537   204 LQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSE--EDMETVGLFLEPLPIRIrfPSSSDASAADFLRAV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7300 QEAalesgrydfyplyeiqTQSAQK-----QELINHLLV---FENYPM---------DEQVEQAggddsgtLSITDVDVa 7362
Cdd:cd19537   282 RRS----------------SQAALAhaipwHQLLEHLGLppdSPNHPLfdvmvtfhdDRGVSLA-------LPIPGVEP- 337
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 7363 EHTNYN-------FTVTVFPGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVAD 7412
Cdd:cd19537   338 LYTWAEgakfplmFEFTALSDDSLLLRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
PRK05850 PRK05850
acyl-CoA synthetase; Validated
265-661 8.23e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 101.17  E-value: 8.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  265 LFEEQAERRPDAVAVTFED---------RQLTYGELNERANRLARTLRNAGVQADQLVGLmVERSLEMIVGIMGILKAGG 335
Cdd:PRK05850    6 LLRERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGSTGDRAVIL-APQGLEYIVAFLGALQAGL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  336 AYVPIDPEYP---EERIRYMLEDSGTQVLLSQ----GHLQERVSFSGTW-----IRLD--DEEAyhEDGSNLESVNGPEh 401
Cdd:PRK05850   85 IAVPLSVPQGgahDERVSAVLRDTSPSVVLTTsavvDDVTEYVAPQPGQsappvIEVDllDLDS--PRGSDARPRDLPS- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  402 LTYVIYTSGTTGKPKGNLTTHRNIIRVVKN--TNYIDVTGQDKLLQLSSYSF-----D-GSTFDIFGALLNGAKLVLVPK 473
Cdd:PRK05850  162 TAYLQYTSGSTRTPAGVMVSHRNVIANFEQlmSDYFGDTGGVPPPDTTVVSWlpfyhDmGLVLGVCAPILGGCPAVLTSP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  474 ETVLdvAKLAGLIEKQQISVMFITTA--F-FNVLV------DMNPDCLRHARAILFGGERVSVSHVRK-----ALGHLGP 539
Cdd:PRK05850  242 VAFL--QRPARWMQLLASNPHAFSAApnFaFELAVrktsddDMAGLDLGGVLGIISGSERVHPATLKRfadrfAPFNLRE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  540 GKIKHVYGPTESTVF-ATS----------YDVHEVEEGAVS----------IPIGGPISNTaIYIVNAQNKLQ-PIGVAG 597
Cdd:PRK05850  320 TAIRPSYGLAEATVYvATRepgqppesvrFDYEKLSAGHAKrcetgggtplVSYGSPRSPT-VRIVDPDTCIEcPAGTVG 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928  598 ELCVAGDGLARGYLNRPDLTAEKFA---DNPFA--PGERMYRTGDLArWLPDGTIEYVGRIDDQVKIRG 661
Cdd:PRK05850  399 EIWVHGDNVAAGYWQKPEETERTFGatlVDPSPgtPEGPWLRTGDLG-FISEGELFIVGRIKDLLIVDG 466
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
5032-5382 8.30e-21

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 97.48  E-value: 8.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5032 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpkDDRID 5111
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISG-EDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5112 PARLHYWISEEKITIFESTPALIipfmDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTEAAID 5191
Cdd:cd17633    77 PKSWIRKINQYNATVIYLVPTML----QALARTLEPESKIKSIFSSGQKLFESTKKKLKNIF-PKANLIEFYGTSELSFI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5192 SSLYDEPLAKLPEAGNVpigkaalnakFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTeekfVDSPFVegerly 5271
Cdd:cd17633   152 TYNFNQESRPPNSVGRP----------FPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSN----PDGWMS------ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5272 rTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAEsELKLSELRS 5351
Cdd:cd17633   212 -VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKR 289
                         330       340       350
                  ....*....|....*....|....*....|.
gi 386647928 5352 SLSQELPGYMIPSYFVQLEQLPLTANGKIDR 5382
Cdd:cd17633   290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
1442-1792 8.94e-21

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 97.48  E-value: 8.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpkDDRID 1521
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISG-EDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1522 PARLHYWISEEKITIFESTPALIipfmDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFgSQFRIINAYGVTEAAID 1601
Cdd:cd17633    77 PKSWIRKINQYNATVIYLVPTML----QALARTLEPESKIKSIFSSGQKLFESTKKKLKNIF-PKANLIEFYGTSELSFI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1602 SSLYDEPLAKLPEAGNVpigkaalnakFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTeekfVDSPFVegerly 1681
Cdd:cd17633   152 TYNFNQESRPPNSVGRP----------FPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSN----PDGWMS------ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1682 rTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAEsELKLSELRS 1761
Cdd:cd17633   212 -VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKR 289
                         330       340       350
                  ....*....|....*....|....*....|.
gi 386647928 1762 SLSQELPGYMIPSYFVQLEQLPLTANGKIDR 1792
Cdd:cd17633   290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
7472-7932 9.53e-21

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 99.56  E-value: 9.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPidpeypedrirymledsgAQVLLTQR 7551
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 HLQECVSFDGKVIAADDEQAYGEDgsnlePVvgpnhLAYviYTSGTTGKPKgvMVEH----HGLCSLKLMFAETLRitEE 7627
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDENTHADD-----PM-----LLY--FTSGTTSKPK--LVEHthrsYPVGHLSTMYWIGLK--PG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7628 DRVVQFASLSFDASCWEIFKA-LFFGATLYIpakdtiLDYPLFES-----YMNENGITAAILPPTYAIYLSPDRLPS--- 7698
Cdd:cd05974   127 DVHWNISSPGWAKHAWSCFFApWNAGATVFL------FNYARFDAkrvlaALVRYGVTTLCAPPTVWRMLIQQDLASfdv 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7699 -LKKLITGGSAASVEFVQQ----WKDKVRyfNAYGPTEasivTSVWAASPDGLDLRSVPIGRPIANHQIFIVDsqnhmlP 7773
Cdd:cd05974   201 kLREVVGAGEPLNPEVIEQvrraWGLTIR--DGYGQTE----TTALVGNSPGQPVKAGSMGRPLPGYRVALLD------P 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7774 VGVA---GELCIS-----GAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRI 7845
Cdd:cd05974   269 DGAPateGEVALDlgdtrPVGLMKGYAGDPDKTAHAMRGG-------YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRI 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7846 ELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV------ADRELTVSELRGTLSQELPGYMIPSyfVQLEQMPLTP 7919
Cdd:cd05974   342 SPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyePSPETALEIFRFSRERLAPYKRIRR--LEFAELPKTI 419
                         490
                  ....*....|...
gi 386647928 7920 NGKIDRNALPAPE 7932
Cdd:cd05974   420 SGKIRRVELRRRE 432
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
2360-2935 1.03e-20

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 101.65  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2360 DHPAVvFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLE 2439
Cdd:PRK06060   21 DRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAAR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2440 DSSAQVLLAQRRLQERvsFAGTvvTVDDEQAYAGDGSNLESA----VGPNDLAYIIYTSGTTGKPKGVMVEHH------- 2508
Cdd:PRK06060  100 NTEPALVVTSDALRDR--FQPS--RVAEAAELMSEAARVAPGgyepMGGDALAYATYTSGTTGPPKAAIHRHAdpltfvd 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2509 --------------GLCSLKQMFANTLQIN-----AQDRVVQFASLSFDASCWEVFQTLFFGATLY-IPTketildyqWF 2568
Cdd:PRK06060  176 amcrkalrltpedtGLCSARMYFAYGLGNSvwfplATGGSAVINSAPVTPEAAAILSARFGPSVLYgVPN--------FF 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2569 ERYMSDngittatlpptyavyLNPDHMPDFKRLIAAGSASSLELLQQWkdkVKYFNAYgPTEDSICTTI--WTPSTEDIS 2646
Cdd:PRK06060  248 ARVIDS---------------CSPDSFRSLRCVVSAGEALELGLAERL---MEFFGGI-PILDGIGSTEvgQTFVSNRVD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2647 QLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPD--LTAEKFVDnpfepgermyrTGDLAKWLP 2724
Cdd:PRK06060  309 EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------TRDRVCIDS 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2725 DGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVGE-----LRGELSGE 2799
Cdd:PRK06060  378 DGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNR 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2800 LPGYMIPAHFVQLERMPLTPNGKIDRKAL----PA----------------------PQGNASAGADYVAPRSEEEKVLA 2853
Cdd:PRK06060  458 LSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsPTkpiwelsltepgsgvraqrddlSASNMTIAGGNDGGATLRERLVA 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2854 -------DVWQAVLG--AERVGATD--------HFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTVAQLSKHIRP 2915
Cdd:PRK06060  538 lrqerqrLVVDAVCAeaAKMLGEPDpwsvdqdlAFSELGFDSQMTVTLCKRLAAVtGLRLPETVGWDYGSISGLAQYLEA 617
                         650       660
                  ....*....|....*....|....*.
gi 386647928 2916 VARMAD------QGEVSGDVSLTPIQ 2935
Cdd:PRK06060  618 ELAGGHgrlksaGPVNSGATGLWAIE 643
PRK08162 PRK08162
acyl-CoA synthetase; Validated
2351-2840 1.03e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 100.79  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2351 FEEQAERI-PDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEY 2429
Cdd:PRK08162   23 FLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2430 PEDRISYMLEDSSAQVLLAQRRLQERVSFAG--------TVVTVDDEQAYAGD--GS-NLESAVGPNDLAY--------- 2489
Cdd:PRK08162  103 DAASIAFMLRHGEAKVLIVDTEFAEVAREALallpgpkpLVIDVDDPEYPGGRfiGAlDYEAFLASGDPDFawtlpadew 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2490 ----IIYTSGTTGKPKGVmVEHHGLCSLKQMfANTLQINAQDRVVQFASLS-FDASCWEVFQTLFFGATLYIPTK----E 2560
Cdd:PRK08162  183 daiaLNYTSGTTGNPKGV-VYHHRGAYLNAL-SNILAWGMPKHPVYLWTLPmFHCNGWCFPWTVAARAGTNVCLRkvdpK 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2561 TILDyqwferYMSDNGIT-TATLPPTYAVYLN-PDHMpdfKRLIA-------AGSASSLELLQQWKDK-VKYFNAYGPTE 2630
Cdd:PRK08162  261 LIFD------LIREHGVThYCGAPIVLSALINaPAEW---RAGIDhpvhamvAGAAPPAAVIAKMEEIgFDLTHVYGLTE 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2631 D----SICTtiWTPSTEDIS-----QLKS---VPIggPIVNhRIYIVD-AHYQPVPVG--VAGELCIAGVGLARGYLNRP 2695
Cdd:PRK08162  332 TygpaTVCA--WQPEWDALPlderaQLKArqgVRY--PLQE-GVTVLDpDTMQPVPADgeTIGEIMFRGNIVMKGYLKNP 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2696 DLTAEKFVDNPFEpgermyrTGDLAKWLPDGTIeylgridhQVKIR--------GYRIELGEIEEQLLKVASVQEAIVIA 2767
Cdd:PRK08162  407 KATEEAFAGGWFH-------TGDLAVLHPDGYI--------KIKDRskdiiisgGENISSIEVEDVLYRHPAVLVAAVVA 471
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 2768 HDDASGQKQLCAyFVADR---TMTVGELRGELSGELPGYMIPAHFVqLERMPLTPNGKIDRKALPAPQGNASAGAD 2840
Cdd:PRK08162  472 KPDPKWGEVPCA-FVELKdgaSATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVLREQAKSLKAIDL 545
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
6524-6949 1.19e-20

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 98.92  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6524 TPIQRWFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSEngyaawnraiGEGELY-----SL 6598
Cdd:cd19542     5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESS----------AEGTFLqvvlkSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6599 EVaDFRDVKSAEQAVEAKANEIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQaakge 6677
Cdd:cd19542    75 DP-PIEEVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVyLVLRISHALYDGVSLPIILRDLAAAYNG----- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6678 evRLPAKTDSFRtwseQLAAYAQSPAMENERAYWEQIAQTAVAPLPKDKQSDRSlqqDSESITiqwSRKETEQLLKKVHR 6757
Cdd:cd19542   149 --QLLPPAPPFS----DYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRP---AERSLS---STRRSLAKLEAFCA 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6758 AYNTEMNDILLTALGMAVQKWSGLDRLLVnleGH---GRESIMTDIDitRTVGWFTSKYPVLLQMEPGRSLSTRIKKVKE 6834
Cdd:cd19542   217 SLGVTLASLFQAAWALVLARYTGSRDVVF---GYvvsGRDLPVPGID--DIVGPCINTLPVRVKLDPDWTVLDLLRQLQQ 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6835 D-LRRIPNKGIGyglcryLSA-QPDGTVWGAEPEisFNYLGQFdQDLSNNDIGLSPYSSGLEMSDRQARS-FILDINGMI 6911
Cdd:cd19542   292 QyLRSLPHQHLS------LREiQRALGLWPSGTL--FNTLVSY-QNFEASPESELSGSSVFELSAAEDPTeYPVAVEVEP 362
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 386647928 6912 TDGSLALELSYSRKEYHRETVEELAGMLQESLQEIIAH 6949
Cdd:cd19542   363 SGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
7455-7928 1.22e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 100.08  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7455 QAERMPEKAAVVFENT--QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPE 7532
Cdd:PRK13390    6 HAQIAPDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7533 DRIRYMLEDSGAQVLLTQRHLQECV-----------SFDGKVIA-ADDEQAYGEDGSNL-EPVVGpnhlAYVIYTSGTTG 7599
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAALDGLAakvgadlplrlSFGGEIDGfGSFEAALAGAGPRLtEQPCG----AVMLYSSGTTG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7600 KPKGVMVEHHGlcslklmfaetlRITEE--DRVVQFASLSFDASCWEIFkalFFGATLYIPAK-----------DTILDY 7666
Cdd:PRK13390  162 FPKGIQPDLPG------------RDVDApgDPIVAIARAFYDISESDIY---YSSAPIYHAAPlrwcsmvhalgGTVVLA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7667 PLFES-----YMNENGITAAILPPTYAIYL--------SPDRLPSLKKLITGGSAASVEFVQ---QWKDKVRYfNAYGPT 7730
Cdd:PRK13390  227 KRFDAqatlgHVERYRITVTQMVPTMFVRLlkldadvrTRYDVSSLRAVIHAAAPCPVDVKHamiDWLGPIVY-EYYSST 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7731 EASIVTSV----WAASPDGldlrsvpIGRPIANhQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAE-KFVDN 7805
Cdd:PRK13390  306 EAHGMTFIdspdWLAHPGS-------VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAH 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7806 PFLAgermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDAN-GQQ-----QLCA 7879
Cdd:PRK13390  378 PFWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEmGEQvkaviQLVE 452
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 7880 YFVADRELTvSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK13390  453 GIRGSDELA-RELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
4912-5371 1.35e-20

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 99.35  E-value: 1.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAyvpldpdypsdriqfmledsAAsvlLTQ 4991
Cdd:cd05940     3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--------------------AA---LIN 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 THLQeraqqwGQTLqaALCLDDEAAYAEDAsnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 5071
Cdd:cd05940    60 YNLR------GESL--AHCLNVSSAKHLVV----------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5072 FPVRLLQLASF-SFDVFVGdIARTLYNGGTMVICPKDDridpARlHYW--ISEEKITIFESTPALIIPFMDyVAEHGLDM 5148
Cdd:cd05940   122 SDVLYTCLPLYhSTALIVG-WSACLASGATLVIRKKFS----AS-NFWddIRKYQATIFQYIGELCRYLLN-QPPKPTER 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5149 SSMVLLItSSDSCSVTDYRVLQERFGSQfRIINAYGVTEAAIDSSLYD-EPLA------KLPEAGNVPIGKAALNAKFYI 5221
Cdd:cd05940   195 KHKVRMI-FGNGLRPDIWEEFKERFGVP-RIAEFYAATEGNSGFINFFgKPGAigrnpsLLRKVAPLALVKYDLESGEPI 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5222 VDAH--LNPVPVGVLGELC--IGGIGVARGYLNrPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKI 5297
Cdd:cd05940   273 RDAEgrCIKVPRGEPGLLIsrINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW 351
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 5298 RGYRIETGEIETQLLKAEGVREAVV--VVREDAKGqKVLCAHFT--AESELKLSELRSSLSQELPGYMIPsYFVQLEQ 5371
Cdd:cd05940   352 KGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDG-RAGMAAIVlqPNEEFDLSALAAHLEKNLPGYARP-LFLRLQP 427
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
7468-7928 1.37e-20

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 100.63  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7468 ENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQV 7546
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7547 LLTQ--------RHLQECVSFDGKVIAADD--EQAYGEDGSNLE-----------------PVVGPNHLAYVIYTSGTTG 7599
Cdd:PRK05620  115 IVADprlaeqlgEILKECPCVRAVVFIGPSdaDSAAAHMPEGIKvysyealldgrstvydwPELDETTAAAICYSTGTTG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7600 KPKGVMVEHHGLC--SLKLMFAETLRITEEDR----VVQFASLSfdascWEI-FKALFFGATLYIPAKDtiLDYPLFESy 7672
Cdd:PRK05620  195 APKGVVYSHRSLYlqSLSLRTTDSLAVTHGESflccVPIYHVLS-----WGVpLAAFMSGTPLVFPGPD--LSAPTLAK- 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 mnengITAAILP------PTYAIYL-------SPDRLpSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEASIVTS 7737
Cdd:PRK05620  267 -----IIATAMPrvahgvPTLWIQLmvhylknPPERM-SLQEIYVGGSAVPPILIKAWEERygVDVVHVWGMTETSPVGT 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7738 VwAASPDGL-----DLRSVPIGRPIANHQIFIVDSQNHMLPVGV-AGELCISGAGLARGYLNRP---------------- 7795
Cdd:PRK05620  341 V-ARPPSGVsgearWAYRVSQGRFPASLEYRIVNDGQVMESTDRnEGEIQVRGNWVTASYYHSPteegggaastfrgedv 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7796 ELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDAN-GQ 7874
Cdd:PRK05620  420 EDANDRFTADGWL------RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGE 493
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7875 QQLCAYFVAD----RELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK05620  494 RPLAVTVLAPgiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
4893-5316 1.45e-20

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 100.72  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4893 FEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 4972
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLEDSAASVLL-----------TQTHLQERAQQW---GQTLQAALCLDDEAAYAEDASNVANVNEPH----DLA 5034
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIvgeelveafeeARADLARPPRLWvagGDTLDDPEGYEDLAAAAAGAPTTNPASRSGvtakDTA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5035 YVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL---DQFPVRLLQLASFSFDVFVGDiarTLYNGGTMVICPKDDrid 5111
Cdd:PRK08279  203 FYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLtpdDVLYCCLPLYHNTGGTVAWSS---VLAAGATLALRRKFS--- 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5112 pARlHYW--ISEEKITIFEstpaliipfmdYVAEhgldmssmvL---LITSSDSCSVTDYRV---------------LQE 5171
Cdd:PRK08279  277 -AS-RFWddVRRYRATAFQ-----------YIGE---------LcryLLNQPPKPTDRDHRLrlmignglrpdiwdeFQQ 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5172 RFGSQfRIINAYGVTEAAIdsSLYDEpLAKLPEAGNVPigkAALNAKFYIV-------------DAHLNPVPVGVLGELc 5238
Cdd:PRK08279  335 RFGIP-RILEFYAASEGNV--GFINV-FNFDGTVGRVP---LWLAHPYAIVkydvdtgepvrdaDGRCIKVKPGEVGLL- 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5239 IGGIGVAR---GYlNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAE 5315
Cdd:PRK08279  407 IGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFP 485

                  .
gi 386647928 5316 G 5316
Cdd:PRK08279  486 G 486
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2914-3357 1.45e-20

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 101.86  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2914 RPVARMADQGEVSGDVSLTPIQHWFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHKSENGYTA 2993
Cdd:COG1020     5 AAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2994 WNRAIGEGELYGLEVVDLKGIEESAQAVEAKANEIQSSIDLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLE 3072
Cdd:COG1020    85 VIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLlLLLALHHIISDGLSDGLLLA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3073 DLAIGYEQAVKGEELRFPAKTDAYRTWSEQLAAYAQSPVIERELAYWKRVAQTE--VQPLPKDEQVDVSLQQDSESISIE 3150
Cdd:COG1020   165 ELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLppLLELPTDRPRPAVQSYRGARVSFR 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3151 WTREETEQLlKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGResimTDIDITRTVGWFTSKYPVVLELEQG 3230
Cdd:COG1020   245 LPAELTAAL-RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGR----PRPELEGLVGFFVNTLPLRVDLSGD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3231 KDISYLLKKTKEDLRGI-PNKGIGYG-ICRYLSAAKNDiawGAEP--EVSFNYLGQFDQDLQNSDIGVSAHTGGKQSSDr 3306
Cdd:COG1020   320 PSFAELLARVRETLLAAyAHQDLPFErLVEELQPERDL---SRNPlfQVMFVLQNAPADELELPGLTLEPLELDSGTAK- 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928 3307 qkriFVLDINGMIADGTLSLELSYNGKEYRRETMERLAASLQESLRVIIAH 3357
Cdd:COG1020   396 ----FDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD 442
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1322-1781 1.52e-20

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 99.35  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAyvpldpdypsdriqfmledsAAsvlLTQ 1401
Cdd:cd05940     3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--------------------AA---LIN 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 THLQeraqqwGQTLqaVLCLDDEAAYAEDAsnvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 1481
Cdd:cd05940    60 YNLR------GESL--AHCLNVSSAKHLVV----------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 FPVRLLQLASF-SFDVFVGdIARTLYNGGTMVICPKDDridpARlHYW--ISEEKITIFESTPALI-----IPFMDYVAE 1553
Cdd:cd05940   122 SDVLYTCLPLYhSTALIVG-WSACLASGATLVIRKKFS----AS-NFWddIRKYQATIFQYIGELCryllnQPPKPTERK 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1554 HGLDMSSMELLITSSdscsvtdYRVLQERFGSQfRIINAYGVTEAAIDSSLYD-EPLA------KLPEAGNVPIGKAALN 1626
Cdd:cd05940   196 HKVRMIFGNGLRPDI-------WEEFKERFGVP-RIAEFYAATEGNSGFINFFgKPGAigrnpsLLRKVAPLALVKYDLE 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1627 AKFYIVDAH--LNPVPVGVLGELC--IGGIGVARGYLNrPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRID 1702
Cdd:cd05940   268 SGEPIRDAEgrCIKVPRGEPGLLIsrINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLG 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1703 NQAKIRGYRIETGEIETQLLKAEGVREAVV--VVREDAKGQKVLCAYFTAES-ELKLSELRSSLSQELPGYMIPsYFVQL 1779
Cdd:cd05940   347 DTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLQPNeEFDLSALAAHLEKNLPGYARP-LFLRL 425

                  ..
gi 386647928 1780 EQ 1781
Cdd:cd05940   426 QP 427
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
3881-4337 1.67e-20

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 100.05  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3881 TYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQRH 3960
Cdd:PLN02330   57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3961 LRERVSFAGTFVAVDDEQ--------------AYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHH----GLCSl 4022
Cdd:PLN02330  137 NYGKVKGLGLPVIVLGEEkiegavnwkelleaADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRnlvaNLCS- 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4023 kLMFANTLQMTEQdrVVQFASLSFdascWEIFKAL-FFGATLYIPTSTTILDYPLFESYMN----ENGITATILPPTYAA 4097
Cdd:PLN02330  216 -SLFSVGPEMIGQ--VVTLGLIPF----FHIYGITgICCATLRNKGKVVVMSRFELRTFLNalitQEVSFAPIVPPIILN 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4098 YL-NP--DRMP----SLKKLITGGSAASVEFVQQWKDK---VLYFNAYGPTEASIVTSIWDEASDSLGDRKSVPIGRPLA 4167
Cdd:PLN02330  289 LVkNPivEEFDlsklKLQAIMTAAAPLAPELLTAFEAKfpgVQVQEAYGLTEHSCITLTHGDPEKGHGIAKKNSVGFILP 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4168 NHRIYVVDSHN-RMLPVGVAGELCISGVGLARGYLNRPELTAeKFVDNpfepgERMYRTGDLVRWLPDGNLEYLGRIDHQ 4246
Cdd:PLN02330  369 NLEVKFIDPDTgRSLPKNTPGELCVRSQCVMQGYYNNKEETD-RTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKEL 442
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4247 VKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAElratmsQELPNYM---IPSY----FV 4319
Cdd:PLN02330  443 IKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE------EDILNFVaanVAHYkkvrVV 516
                         490
                  ....*....|....*....
gi 386647928 4320 QLA-QMPLTPNGKIDRKAL 4337
Cdd:PLN02330  517 QFVdSIPKSLSGKIMRRLL 535
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1323-1706 1.68e-20

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 99.60  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGgayVPLDPDYPSdriqfmLEDSAASVLLTQT 1402
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAT------LGEDALIHSLNET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 HLQeraqqwgqtlqAVLClddeaayaedasnvanVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYrrEYRLDQF 1482
Cdd:cd17639    77 ECS-----------AIFT----------------DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGL--GDRVPEL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1483 PVR------LLQLA----------SFSFDVFVG-DIARTLynggTMVIC--PKDDridparlhywISEEKITIFESTPAL 1543
Cdd:cd17639   128 LGPddrylaYLPLAhifelaaenvCLYRGGTIGyGSPRTL----TDKSKrgCKGD----------LTEFKPTLMVGVPAI 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1544 I----------IPFMDYVA----EHGLDmSSMELLITSSDSC-----------SVTDYRVLQ------------ERFGSQ 1586
Cdd:cd17639   194 WdtirkgvlakLNPMGGLKrtlfWTAYQ-SKLKALKEGPGTPlldelvfkkvrAALGGRLRYmlsggaplsadtQEFLNI 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1587 F--RIINAYGVTE---AAIDSSLYD-------EPL----AKL---PEAGnvpigkaalnakfYIVDAHlNPvpvgvLGEL 1647
Cdd:cd17639   273 VlcPVIQGYGLTEtcaGGTVQDPGDletgrvgPPLpcceIKLvdwEEGG-------------YSTDKP-PP-----RGEI 333
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 1648 CIGGIGVARGYLNRPELTEEKFvdspfvEGERLYRTGDLARWMPDGNVDFIGRIDNQAK 1706
Cdd:cd17639   334 LIRGPNVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVK 386
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2371-2771 1.77e-20

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 98.79  E-value: 1.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPidpeypedrisymledssAQVLLAQR 2450
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2451 RLQERVSFAGTVVTVDDEQAYAgdgsnlesavgpNDLAYIIYTSGTTGKPKgvMVEH----HGLCSLKQMFANTLQinAQ 2526
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDENTHA------------DDPMLLYFTSGTTSKPK--LVEHthrsYPVGHLSTMYWIGLK--PG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2527 DRVVQFASLSFDASCWE-VFQTLFFGATLYIpTKETILDYQWFERYMSDNGITTATLPPTYAVYLNPDHMPDFK----RL 2601
Cdd:cd05974   127 DVHWNISSPGWAKHAWScFFAPWNAGATVFL-FNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDvklrEV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2602 IAAGSASSLELLQQ----WKDKVKyfNAYGPTEdSICTTIWTPStediSQLKSVPIGGPIVNHRIYIVDAHYQPVPvgvA 2677
Cdd:cd05974   206 VGAGEPLNPEVIEQvrraWGLTIR--DGYGQTE-TTALVGNSPG----QPVKAGSMGRPLPGYRVALLDPDGAPAT---E 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2678 GELCIA-----GVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEE 2752
Cdd:cd05974   276 GEVALDlgdtrPVGLMKGYAGDPDKTAHAMRGG-------YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
                         410
                  ....*....|....*....
gi 386647928 2753 QLLKVASVQEAIVIAHDDA 2771
Cdd:cd05974   349 VLIEHPAVAEAAVVPSPDP 367
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2932-3357 2.08e-20

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 98.15  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2932 TPIQHWFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHKSEngytawnraiGEGELYG--LEVV 3009
Cdd:cd19542     5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESS----------AEGTFLQvvLKSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3010 D--LKGIEESAQAVEAKANEIQSSIDLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAvkgEE 3086
Cdd:cd19542    75 DppIEEVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVyLVLRISHALYDGVSLPIILRDLAAAYNGQ---LL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3087 LRFPaktdayrTWSEQLaAYAQSPVIERELAYWKRVAQ-TEVQPLPkdeqvdVSLQQDSESISIEWTReETEQLLKGVHR 3165
Cdd:cd19542   152 PPAP-------PFSDYI-SYLQSQSQEESLQYWRKYLQgASPCAFP------SLSPKRPAERSLSSTR-RSLAKLEAFCA 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3166 AYNTEMNDILLAALGMAVQKWSGLDRVLVnleGH---GRESIMTDIDitRTVGWFTSKYPVVLELEQGKDISYLLKKTKE 3242
Cdd:cd19542   217 SLGVTLASLFQAAWALVLARYTGSRDVVF---GYvvsGRDLPVPGID--DIVGPCINTLPVRVKLDPDWTVLDLLRQLQQ 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3243 D-LRGIPNkgigygicRYLSAAknDIA-----WGAEPEVS--FNYLGQFDQDLQNSDIGVSAHTggkqsSDRQKRI-FVL 3313
Cdd:cd19542   292 QyLRSLPH--------QHLSLR--EIQralglWPSGTLFNtlVSYQNFEASPESELSGSSVFEL-----SAAEDPTeYPV 356
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 386647928 3314 DINGMIADGTLSLELSYNGKEYRRETMERLAASLQESLRVIIAH 3357
Cdd:cd19542   357 AVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
5965-6420 2.11e-20

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 99.46  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5965 ELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKL-------- 6035
Cdd:cd05928    46 ELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCivtsdela 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6036 ----------------LLVQGHLLDRASFADKLVNLNDDGAYHEDGSNLEPVngpehltyVIY-TSGTTGRPKgvMVEHR 6098
Cdd:cd05928   126 pevdsvasecpslktkLLVSEKSRDGWLNFKELLNEASTEHHCVETGSQEPM--------AIYfTSGTTGSPK--MAEHS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6099 NV---VRLVKNTNY-VELNEQT---HILQTGAVVFDAST-FEIW--GALLNGGRLYVVRNETILDAVSlknaiqQYGINT 6168
Cdd:cd05928   196 HSslgLGLKVNGRYwLDLTASDimwNTSDTGWIKSAWSSlFEPWiqGACVFVHHLPRFDPLVILKTLS------SYPITT 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6169 MWLTAPLYNQLSQQD--SGMFAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTEntTFSTTHTIVGEQKEAVPIG 6246
Cdd:cd05928   270 FCGAPTVYRMLVQQDlsSYKFPSLQHCVTGGEPLN-PEVLEKWKAQTGLDIYEGYGQTE--TGLICANFKGMKIKPGSMG 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6247 KPINNSTAYIVDSKLSLLPVGVWGELI--VGGD---GVARGYLNRPELTAEKFvESSFlpgercYRTGDLARWLPDGTLE 6321
Cdd:cd05928   347 KASPPYDVQIIDDNGNVLPPGTEGDIGirVKPIrpfGLFSGYVDNPEKTAATI-RGDF------YLTGDRGIMDEDGYFW 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6322 YKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFV-------AERELTIGELRAALSQELPN 6394
Cdd:cd05928   420 FMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqflsHDPEQLTKELQQHVKSVTAP 499
                         490       500
                  ....*....|....*....|....*.
gi 386647928 6395 YMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05928   500 YKYPRKVEFVQELPKTVTGKIQRNEL 525
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
5-246 2.52e-20

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 98.56  E-value: 2.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928     5 AFERETAFWNKIFEGEEnPPTALPYSKAQKQAPALVR-RMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTS 83
Cdd:pfam00668  190 DYQKDAAYWLEQLEGEL-PVLQLPKDYARPADRSFKGdRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTG 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    84 SSSILVGMPVVTKPNENRRP-----VNQLVIlREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYADGV- 157
Cdd:pfam00668  269 QDDIVVGTPGSGRPSPDIERmvgmfVNTLPL-RIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRLPRDLSRh 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   158 PVVNTLVALK---------QLHITDYRQSAVSDVLFE---FELD------KDEVRLHLTYNGNLYTESFIAQAVDHLNRL 219
Cdd:pfam00668  348 PLFDPMFSFQnylgqdsqeEEFQLSELDLSVSSVIEEeakYDLSltaserGGGLTIKIDYNTSLFDEETIERFAEHFKEL 427
                          250       260
                   ....*....|....*....|....*..
gi 386647928   220 FSVVLFQPDLALGQADLLSEAEKHQLL 246
Cdd:pfam00668  428 LEQAIAHPSQPLSELDLLSDAEKQKLL 454
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
283-750 2.55e-20

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 99.00  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  283 DRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERS---LEMIVGIMGIlkagGAY-VPIDPEYPEERIRYMLEDSGT 358
Cdd:PRK12406    9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDfafFEAAYAAMRL----GAYaVPVNWHFKPEEIAYILEDSGA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  359 QVLLSQGHLQERVS---FSGTWI-------------RLDDEEAYHEDG--------SNLESVNGP--EHLTYVIYTSGTT 412
Cdd:PRK12406   85 RVLIAHADLLHGLAsalPAGVTVlsvptppeiaaayRISPALLTPPAGaidwegwlAQQEPYDGPpvPQPQSMIYTSGTT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  413 GKPKG--------NLTTHRNIIRVvknTNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLnGAKLVLVPKetvLDVAKLAG 484
Cdd:PRK12406  165 GHPKGvrraaptpEQAAAAEQMRA---LIYGLKPGIRALLTGPLYHSAPNAYGLRAGRL-GGVLVLQPR---FDPEELLQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  485 LIEKQQISVMFITTAFFNVLVDMnPDCLRHA------RAILFGGERVSVSHVRKALGHLGPgKIKHVYGPTES--TVFAT 556
Cdd:PRK12406  238 LIERHRITHMHMVPTMFIRLLKL-PEEVRAKydvsslRHVIHAAAPCPADVKRAMIEWWGP-VIYEYYGSTESgaVTFAT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  557 SydvheveEGAVSIP--IGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLAR-GYLNRPDLTAEKFADNPFAPGERMY 633
Cdd:PRK12406  316 S-------EDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGY 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  634 RTGDLARWLPDgtieyvgRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKqLCAYY--VADRSLPANE 710
Cdd:PRK12406  389 LDADGYLFLCD-------RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFgIPDAEFGEA-LMAVVepQPGATLDEAD 460
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 386647928  711 VRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAP 750
Cdd:PRK12406  461 IRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PRK07529 PRK07529
AMP-binding domain protein; Validated
260-747 2.78e-20

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 100.03  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  260 TTIHRLFEEQAERRPDAVAVTF--------EDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGIL 331
Cdd:PRK07529   25 ASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  332 KAGGAyVPIDPEYPEERIRYMLEDSGTQVLLSQG-------------------------------HLQERVSFSGTWIRL 380
Cdd:PRK07529  105 AAGIA-NPINPLLEPEQIAELLRAAGAKVLVTLGpfpgtdiwqkvaevlaalpelrtvvevdlarYLPGPKRLAVPLIRR 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  381 DDEEAYH--------EDGSNLES--VNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIrvvkntnyidvtGQDKLLQLSSYS 450
Cdd:PRK07529  184 KAHARILdfdaelarQPGDRLFSgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEV------------ANAWLGALLLGL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  451 FDGST-------FDIFG-------ALLNGAKLVLVP-----KETVldVAKLAGLIEKQQISVMFITTAFFNVLVDMNPD- 510
Cdd:PRK07529  252 GPGDTvfcglplFHVNAllvtglaPLARGAHVVLATpqgyrGPGV--IANFWKIVERYRINFLSGVPTVYAALLQVPVDg 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  511 ----CLRHAraiLFGGERVSVSHVRKALGHLGPgKIKHVYGPTEST-VFATSYDVHEVEEGAVSIPIggPISNTAIYIVN 585
Cdd:PRK07529  330 hdisSLRYA---LCGAAPLPVEVFRRFEAATGV-RIVEGYGLTEATcVSSVNPPDGERRIGSVGLRL--PYQRVRVVILD 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  586 AQNKLQ---PIGVAGELCVAGDGLARGYLNrpdltAEKFADnPFApGERMYRTGDLARWLPDGTIEYVGRIDDQVkIR-G 661
Cdd:PRK07529  404 DAGRYLrdcAVDEVGVLCIAGPNVFSGYLE-----AAHNKG-LWL-EDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgG 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  662 FRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAY--YVADRSLPANEVRSTLSQELP---AymLPSYFVQLEQMPL 736
Cdd:PRK07529  476 HNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYvqLKPGASATEAELLAFARDHIAeraA--VPKHVRILDALPK 553
                         570
                  ....*....|.
gi 386647928  737 TTNGKVDRRAL 747
Cdd:PRK07529  554 TAVGKIFKPAL 564
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
4899-5385 3.13e-20

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 99.29  E-value: 3.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4899 CTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGgaYVPLDPDYPSDRIQF 4978
Cdd:PRK10946   35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSEL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4979 -----------MLEDSAASVLLTQTHLQERAQQWGqTLQAALCLDD------EAAYAEDASNVANVNEPHD-LAYVIYTS 5040
Cdd:PRK10946  113 nayasqiepalLIADRQHALFSDDDFLNTLVAEHS-SLRVVLLLNDdgehslDDAINHPAEDFTATPSPADeVAFFQLSG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5041 GTTGRPKGVMIEH--------RSlvNTAAGYRREYRL-------DQFPvrllqLAS-FSFDVFvgdiartlYNGGTMVIC 5104
Cdd:PRK10946  192 GSTGTPKLIPRTHndyyysvrRS--VEICGFTPQTRYlcalpaaHNYP-----MSSpGALGVF--------LAGGTVVLA 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5105 PkddriDPARLHYW--ISEEKITIFESTPALIIPFMDYVAE--HGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQFRii 5180
Cdd:PRK10946  257 P-----DPSATLCFplIEKHQVNVTALVPPAVSLWLQAIAEggSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQ-- 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5181 NAYGVTEAAIDSSLYDEPLAKLPEAGNVPIgkaALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFv 5260
Cdd:PRK10946  330 QVFGMAEGLVNYTRLDDSDERIFTTQGRPM---SPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF- 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5261 DSpfvegERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVlCAHFT 5339
Cdd:PRK10946  406 DA-----NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEKS-CAFLV 479
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 5340 AESELKLSELRSSL-SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK10946  480 VKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1442-1795 3.86e-20

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 99.13  E-value: 3.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYR---REYRLDQFP-------VRLLQLASFSFDVFVGDIARTLYNGGTM 1511
Cdd:PRK12492  208 DIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRaclSQLGPDGQPlmkegqeVMIAPLPLYHIYAFTANCMCMMVSGNHN 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1512 VIC--PKDDRIDPARLHYWiseeKITIFESTPALIIPFMDYVAEHGLDMSSMELliTSSDSCSVTdyRVLQERFGSQF-- 1587
Cdd:PRK12492  288 VLItnPRDIPGFIKELGKW----RFSALLGLNTLFVALMDHPGFKDLDFSALKL--TNSGGTALV--KATAERWEQLTgc 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1588 RIINAYGVTEAAIDSSLydEPLAKLPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEE 1667
Cdd:PRK12492  360 TIVEGYGLTETSPVAST--NPYGELARLGTV--GIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAE 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1668 KfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCA 1746
Cdd:PRK12492  436 A------LDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERsGEAVKLF 509
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 1747 YFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK12492  510 VVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PLN02574 PLN02574
4-coumarate--CoA ligase-like
3880-4337 4.26e-20

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 98.76  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDA-GVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQ 3958
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3959 RHLRERVSFAGTFVAVDDEQAYHADGSN----------------LEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSL 4022
Cdd:PLN02574  147 PENVEKLSPLGVPVIGVPENYDFDSKRIefpkfyelikedfdfvPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAM 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4023 KLMFantlqmteqdrvVQF-ASLSFDASCWEIFKALF-----FGATLY----IPTSTTILDYPLFES-----YMNENGIT 4087
Cdd:PLN02574  227 VELF------------VRFeASQYEYPGSDNVYLAALpmfhiYGLSLFvvglLSLGSTIVVMRRFDAsdmvkVIDRFKVT 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4088 A-TILPPTYAAYLNPDR------MPSLKKLITGGSAASVEFVQQWKD---KVLYFNAYGPTEAsivTSIWDEASDSLGDR 4157
Cdd:PLN02574  295 HfPVVPPILMALTKKAKgvcgevLKSLKQVSCGAAPLSGKFIQDFVQtlpHVDFIQGYGMTES---TAVGTRGFNTEKLS 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4158 KSVPIGRPLANHRIYVVD-SHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDnpfepgERMYRTGDLVRWLPDGN 4236
Cdd:PLN02574  372 KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDK------DGWLRTGDIAYFDEDGY 445
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4237 LEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRE--LTAAELRATMSQELPNYMI 4314
Cdd:PLN02574  446 LYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGstLSQEAVINYVAKQVAPYKK 525
                         490       500
                  ....*....|....*....|...
gi 386647928 4315 PSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PLN02574  526 VRKVVFVQSIPKSPAGKILRREL 548
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
2354-2823 4.44e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 98.54  E-value: 4.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2354 QAERIPDHPAVVFE--GQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPE 2431
Cdd:PRK13390    6 HAQIAPDRPAVIVAetGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2432 DRISYMLEDSSAQVLLAQRRL-----------QERVSFAGTVVTVDD-EQAYAGDGSNL-ESAVGpndlAYIIYTSGTTG 2498
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAALdglaakvgadlPLRLSFGGEIDGFGSfEAALAGAGPRLtEQPCG----AVMLYSSGTTG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2499 KPKGVMVEHHGLcSLKQmfantlqinAQDRVVQFASLSFDASCWEVFqtlFFGATLY--IPTK---------ETILDYQW 2567
Cdd:PRK13390  162 FPKGIQPDLPGR-DVDA---------PGDPIVAIARAFYDISESDIY---YSSAPIYhaAPLRwcsmvhalgGTVVLAKR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2568 FE-----RYMSDNGITTATLPPTYAVY---LNPD-----HMPDFKRLIAAGSASSLELLQ---QWKDKVKYfNAYGPTED 2631
Cdd:PRK13390  229 FDaqatlGHVERYRITVTQMVPTMFVRllkLDADvrtryDVSSLRAVIHAAAPCPVDVKHamiDWLGPIVY-EYYSSTEA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2632 SICTTIWTPstEDISQLKSVpigGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEkfVDNPFEPge 2711
Cdd:PRK13390  308 HGMTFIDSP--DWLAHPGSV---GRSVLGDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP-- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2712 rMYRT-GDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFvadrTMTVG 2790
Cdd:PRK13390  379 -FWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVI----QLVEG 453
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 386647928 2791 eLRG--ELSGELPGYMIP--AHFVQ------LERMPLTPNGKI 2823
Cdd:PRK13390  454 -IRGsdELARELIDYTRSriAHYKAprsvefVDELPRTPTGKL 495
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
265-747 4.47e-20

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 98.81  E-value: 4.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  265 LFEEQAERRPDAVAVTFEDRQ--LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDP 342
Cdd:PRK05852   21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  343 EYPEERIRYMLEDSGTQVLL--SQGHLQERVSFSGTW------------------IRLDDEEAYHEDGSNLESVNGPEHL 402
Cdd:PRK05852  101 ALPIAEQRVRSQAAGARVVLidADGPHDRAEPTTRWWpltvnvggdsgpsggtlsVHLDAATEPTPATSTPEGLRPDDAM 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  403 tyVIYTSGTTGKPKGNLTTHRNIIRVVKN--TNYIDVTGQDKLLQLSSYSFDGSTFDIFGALLNGAKlVLVPKEtvldvA 480
Cdd:PRK05852  181 --IMFTGGTTGLPKMVPWTHANIASSVRAiiTGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA-VLLPAR-----G 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  481 KLAGLIEKQQISVMFITtaFFNVLVDMNPDCLRHARAILFGGERVSVSHVRKALGHLGP-----------GKIKHVYGPT 549
Cdd:PRK05852  253 RFSAHTFWDDIKAVGAT--WYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAetaqalqtefaAPVVCAFGMT 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  550 ESTVFATSYDVH---EVEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPF 626
Cdd:PRK05852  331 EATHQVTTTQIEgigQTENPVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  627 apgermyRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSL 706
Cdd:PRK05852  411 -------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESA 483
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 386647928  707 P--ANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK05852  484 PptAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK07529 PRK07529
AMP-binding domain protein; Validated
4879-5385 4.56e-20

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 99.26  E-value: 4.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4879 AAPDAPENeaFHALFEKQAECTPEAAAVVY--------ENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADL 4950
Cdd:PRK07529   19 AARDLPAS--TYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPET 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4951 LVgalAVW--KAGGAYVPLDPDYPSDRIQFMLEDSAASVLLT-----QTHLQERAQQW---GQTLQAALCLD-------- 5012
Cdd:PRK07529   97 HF---ALWggEAAGIANPINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVlaaLPELRTVVEVDlarylpgp 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5013 --------------------DE-AAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 5071
Cdd:PRK07529  174 krlavplirrkaharildfdAElARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGP 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5072 FPVRLLQLASFS-FDVFVGDIArTLYNGGTMVI-CPKDDRIDPARLHYW--ISEEKITIFESTPALIIPFMDyVAEHGLD 5147
Cdd:PRK07529  254 GDTVFCGLPLFHvNALLVTGLA-PLARGAHVVLaTPQGYRGPGVIANFWkiVERYRINFLSGVPTVYAALLQ-VPVDGHD 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5148 MSSMVLLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAAIDSSLYdeplaklPEAGNVPIGKAAL-----NAKFYIV 5222
Cdd:PRK07529  332 ISSLRYALCGAAPLPVEVFRRFEAATG--VRIVEGYGLTEATCVSSVN-------PPDGERRIGSVGLrlpyqRVRVVIL 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5223 D---AHLNPVPVGVLGELCIGGIGVARGYLNrpeltEEKfvDSPFVEGERLYRTGDLARWMPDGNVDFIGRidnqAK--- 5296
Cdd:PRK07529  403 DdagRYLRDCAVDEVGVLCIAGPNVFSGYLE-----AAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGR----AKdli 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5297 IR-GYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFT--AESELKLSELRSSLSQELPG-YMIPSYFVQLEQL 5372
Cdd:PRK07529  472 IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQlkPGASATEAELLAFARDHIAErAAVPKHVRILDAL 551
                         570
                  ....*....|...
gi 386647928 5373 PLTANGKIDRKAL 5385
Cdd:PRK07529  552 PKTAVGKIFKPAL 564
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
5958-6423 4.59e-20

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 98.23  E-value: 4.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5958 DKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERS---LEMVVGMIAIlkagGAY-VPIDPDYPEDRIRYMLEDSGA 6033
Cdd:PRK12406    9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDfafFEAAYAAMRL----GAYaVPVNWHFKPEEIAYILEDSGA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6034 KLLLVQGHLLdrASFADKL------------------VNLNDD------GAYHEDG--SNLEPVNGP--EHLTYVIYTSG 6085
Cdd:PRK12406   85 RVLIAHADLL--HGLASALpagvtvlsvptppeiaaaYRISPAlltppaGAIDWEGwlAQQEPYDGPpvPQPQSMIYTSG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6086 TTGRPKGV-----MVEHRNVVRLVKNTNYvELNEQTHILQTGAVVFDASTfeIWGalLNGGRL-YVVRNETILDAVSLKN 6159
Cdd:PRK12406  163 TTGHPKGVrraapTPEQAAAAEQMRALIY-GLKPGIRALLTGPLYHSAPN--AYG--LRAGRLgGVLVLQPRFDPEELLQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6160 AIQQYGINTMWLTAPLYNQLSQQDSGMFAG--LKTL--IVGGDVLSVPHINRVLREHAGLSIVNGYGPTEnTTFSTTHTi 6235
Cdd:PRK12406  238 LIERHRITHMHMVPTMFIRLLKLPEEVRAKydVSSLrhVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFAT- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6236 vGEQKEAVP--IGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVAR-GYLNRPELTAE----KFVESsflpgercyrt 6308
Cdd:PRK12406  316 -SEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFITS----------- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6309 GDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYF--VAERELTIGELRA 6386
Cdd:PRK12406  384 GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVepQPGATLDEADIRA 463
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 6387 ALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPAP 6423
Cdd:PRK12406  464 QLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PRK09274 PRK09274
peptide synthase; Provisional
1307-1700 5.35e-20

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 98.43  E-value: 5.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVV----------YENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVP 1376
Cdd:PRK09274   16 AQERPDQLAVAvpggrgadgkLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1377 LDPDYPSDRIQFMLEDSAASVLLTQT--HLQERAQQWGQ-TLQAVLCLDD------------EAAYAEDASNVANVnEPH 1441
Cdd:PRK09274   96 VDPGMGIKNLKQCLAEAQPDAFIGIPkaHLARRLFGWGKpSVRRLVTVGGrllwggttlatlLRDGAAAPFPMADL-APD 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLqlasfSFDVFVgdiartLYN---GGTMVICPKDD 1518
Cdd:PRK09274  175 DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP-----TFPLFA------LFGpalGMTSVIPDMDP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1519 R----IDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLItsSDSCSVTdyRVLQERFGSQF----RII 1590
Cdd:PRK09274  244 TrpatVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVI--SAGAPVP--IAVIERFRAMLppdaEIL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1591 NAYGVTEA----AIDSslyDEPLAKLPEA----GNVPIGKAALNAKFYIVDAHLNP---------VPVGVLGELCIGGIG 1653
Cdd:PRK09274  320 TPYGATEAlpisSIES---REILFATRAAtdngAGICVGRPVDGVEVRIIAISDAPipewddalrLATGEIGEIVVAGPM 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 1654 VARGYLNRPELTEE-KFVDSpfvEGERLYRTGDLARWMPDGNVDFIGR 1700
Cdd:PRK09274  397 VTRSYYNRPEATRLaKIPDG---QGDVWHRMGDLGYLDAQGRLWFCGR 441
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
6523-6948 6.13e-20

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 96.75  E-value: 6.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6523 LTPIQRWFFDQSLADLhhfNQAFMLHR-----KDRFDEAALRQVLQKLAEHHDALRTVFRksENGYAAWNRAIGEGELYS 6597
Cdd:cd19536     4 LSSLQEGMLFHSLLNP---GGSVYLHNytytvGRRLNLDLLLEALQVLIDRHDILRTSFI--EDGLGQPVQVVHRQAQVP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6598 LEVADFRDVKSAEQAVEA-KANEIQSSIDLEVGPLFKAGLFQCADGDHLLLVI--HHGVVDGVSWRILLEDVALGYEQAA 6674
Cdd:cd19536    79 VTELDLTPLEEQLDPLRAyKEETKIRRFDLGRAPLVRAALVRKDERERFLLVIsdHHSILDGWSLYLLVKEILAVYNQLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6675 KGEEVRLPaKTDSFRTWSEQLAAYAQSPAMEnerAYWEQI---AQTAVAPLPKDKQSDrSLQQDSESITIQWSRKETEQL 6751
Cdd:cd19536   159 EYKPLSLP-PAQPYRDFVAHERASIQQAASE---RYWREYlagATLATLPALSEAVGG-GPEQDSELLVSVPLPVRSRSL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6752 LKKVHraynTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDIDitRTVGWFTSKYPVLLQMePGRSLSTRIKK 6831
Cdd:cd19536   234 AKRSG----IPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRVTL-SEETVEDLLKR 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6832 VKEDLRRIpnkgigyglcryLS--------AQPDGTvwgAEPEIS--FNYLgQFDQDLSNNDIGLspySSGLEMSDRQAR 6901
Cdd:cd19536   307 AQEQELES------------LSheqvpladIQRCSE---GEPLFDsiVNFR-HFDLDFGLPEWGS---DEGMRRGLLFSE 367
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 6902 S-FILDINGMITD--GSLALELSYSRKEYHRETVEELAGMLQESLQEIIA 6948
Cdd:cd19536   368 FkSNYDVNLSVLPkqDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELAT 417
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
4913-5296 6.15e-20

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 98.06  E-value: 6.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGgayVPLDPDYPS---DRIQFMLEDSAASVLL 4989
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYATlgeDALIHSLNETECSAIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4990 TqthlqeraqqwgqtlqaalclddeaayaedasnvanVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYrrEYRL 5069
Cdd:cd17639    83 T------------------------------------DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGL--GDRV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5070 DQFPVR------LLQLA----------SFSFDVFVG-DIARTLynggTMVIC--PKDDridparlhywISEEKITIFEST 5130
Cdd:cd17639   125 PELLGPddrylaYLPLAhifelaaenvCLYRGGTIGyGSPRTL----TDKSKrgCKGD----------LTEFKPTLMVGV 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5131 PALI----------IPFMDYVA----EHGldMSSMVLLITSSDSCSVTDYRVLQ------------------------ER 5172
Cdd:cd17639   191 PAIWdtirkgvlakLNPMGGLKrtlfWTA--YQSKLKALKEGPGTPLLDELVFKkvraalggrlrymlsggaplsadtQE 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5173 FGSQF--RIINAYGVTE---AAIDSSLYD-------EPL----AKL---PEAGnvpigkaalnakfYIVDAHlNPvpvgv 5233
Cdd:cd17639   269 FLNIVlcPVIQGYGLTEtcaGGTVQDPGDletgrvgPPLpcceIKLvdwEEGG-------------YSTDKP-PP----- 329
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 5234 LGELCIGGIGVARGYLNRPELTEEKFvdspfvEGERLYRTGDLARWMPDGNVDFIGRIDNQAK 5296
Cdd:cd17639   330 RGEILIRGPNVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVK 386
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
2354-2828 7.31e-20

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 98.40  E-value: 7.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2354 QAERIPDHPAVVFEG------QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI-- 2425
Cdd:cd05966    62 HLKERGDKVAIIWEGdepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfa 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2426 --DPEYPEDRIsymlEDSSAQVL--------------------------------LAQRRLQERVSF-AGTVVTVDDEQA 2470
Cdd:cd05966   142 gfSAESLADRI----NDAQCKLVitadggyrggkviplkeivdealekcpsvekvLVVKRTGGEVPMtEGRDLWWHDLMA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2471 YAGDGSNLEsAVGPNDLAYIIYTSGTTGKPKGVMVEHHG-LCSLKQMFANTLQINAQDRVVQFASLSfdascW------E 2543
Cdd:cd05966   218 KQSPECEPE-WMDSEDPLFILYTSGSTGKPKGVVHTTGGyLLYAATTFKYVFDYHPDDIYWCTADIG-----WitghsyI 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2544 VFQTLFFGAT--LYiptkETILDYQWFERYMS---DNGIT---TAtlpPTyAVYLnpdhmpdfkrLIAAGSA-------S 2608
Cdd:cd05966   292 VYGPLANGATtvMF----EGTPTYPDPGRYWDiveKHKVTifyTA---PT-AIRA----------LMKFGDEwvkkhdlS 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2609 SLELL-----------QQWkdkvkYFNAYGPTEDSICTTIWtpSTEDISQLKSvPIGG-----------PIVNHRIYIVD 2666
Cdd:cd05966   354 SLRVLgsvgepinpeaWMW-----YYEVIGKERCPIVDTWW--QTETGGIMIT-PLPGatplkpgsatrPFFGIEPAILD 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2667 AHYQPVPVGVAGELCIAGV--GLARGYLNRPdltaEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYR 2744
Cdd:cd05966   426 EEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHR 501
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2745 IELGEIEEQLLKVASVQEAIVIA-HDDASGQKqLCAYFV-----ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLT 2818
Cdd:cd05966   502 LGTAEVESALVAHPAVAEAAVVGrPHDIKGEA-IYAFVTlkdgeEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKT 580
                         570
                  ....*....|
gi 386647928 2819 PNGKIDRKAL 2828
Cdd:cd05966   581 RSGKIMRRIL 590
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1299-1702 7.45e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 98.08  E-value: 7.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1299 FHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 1378
Cdd:PRK07788   51 FAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1379 PDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAVLCL-----DDEAAYAEDAS--NVANVNEPHDL-------A 1444
Cdd:PRK07788  131 TGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWggnpdDDEPSGSTDETldDLIAGSSTAPLpkppkpgG 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1445 YVIYTSGTTGRPKGVMIEHRSLVNTAAGYrreyrLDQFPVRLLQLASFSFDVF------VGDIARTLynGGTMVIcpkDD 1518
Cdd:PRK07788  211 IVILTSGTTGTPKGAPRPEPSPLAPLAGL-----LSRVPFRAGETTLLPAPMFhatgwaHLTLAMAL--GSTVVL---RR 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1519 RIDPARLHYWISEEKITIFESTPALIIPFMDyVAEHGL---DMSSMELLITSSDSCSVTDYRVLQERFGSqfRIINAYGV 1595
Cdd:PRK07788  281 RFDPEATLEDIAKHKATALVVVPVMLSRILD-LGPEVLakyDTSSLKIIFVSGSALSPELATRALEAFGP--VLYNLYGS 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1596 TEAAIDSSLYDEPLAKLPE-AGNVPIGkaalnAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPelteekfvDSPF 1674
Cdd:PRK07788  358 TEVAFATIATPEDLAEAPGtVGRPPKG-----VTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR--------DKQI 424
                         410       420
                  ....*....|....*....|....*...
gi 386647928 1675 VEGerLYRTGDLARWMPDGNVDFIGRID 1702
Cdd:PRK07788  425 IDG--LLSSGDVGYFDEDGLLFVDGRDD 450
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
255-641 7.63e-20

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 98.41  E-value: 7.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  255 DYPRDTTiHRLfEEQAERRPDAVAVTFED-----RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMG 329
Cdd:PRK08180   36 DYPRRLT-DRL-VHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  330 ILKAGGAYVPIDPEY-----PEERIRYMLE-----------------------DSGTQVLLSQGHLQER--VSFSGtwiR 379
Cdd:PRK08180  114 AMYAGVPYAPVSPAYslvsqDFGKLRHVLElltpglvfaddgaafaralaavvPADVEVVAVRGAVPGRaaTPFAA---L 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  380 LDDEEAYHEDGSNlESVnGPEHLTYVIYTSGTTGKPKGNLTTHRNIirvvkntnyidVTGQDKLLQLS------------ 447
Cdd:PRK08180  191 LATPPTAAVDAAH-AAV-GPDTIAKFLFTSGSTGLPKAVINTHRML-----------CANQQMLAQTFpflaeeppvlvd 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  448 ----SYSFDGSTfdIFG-ALLNGAKLVLvpketvlDVAK-LAGLIEK-----QQISvmfiTTAFFNV------LVD-MNP 509
Cdd:PRK08180  258 wlpwNHTFGGNH--NLGiVLYNGGTLYI-------DDGKpTPGGFDEtlrnlREIS----PTVYFNVpkgwemLVPaLER 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  510 D-CLRHA-----RAILFGG-----------ERVSVSHVrkalGHlgpgKIKHV--YGPTESTVFATSydVHEVEEGAVsi 570
Cdd:PRK08180  325 DaALRRRffsrlKLLFYAGaalsqdvwdrlDRVAEATC----GE----RIRMMtgLGMTETAPSATF--TTGPLSRAG-- 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928  571 PIGGPISNTAIYIVNAQNKLqpigvagELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARW 641
Cdd:PRK08180  393 NIGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
PRK07788 PRK07788
acyl-CoA synthetase; Validated
261-749 9.20e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 97.69  E-value: 9.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPI 340
Cdd:PRK07788   50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  341 DPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSG-------TWIRL-DDEEAYHEDGSNLESVNG----------PEHL 402
Cdd:PRK07788  130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPpdlgrlrAWGGNpDDDEPSGSTDETLDDLIAgsstaplpkpPKPG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  403 TYVIYTSGTTGKPKG-------NLTTHRNIIRVVKntnyidvTGQDKLLQLSSYSFDGSTFDIFG-ALLNGAKLVLVPK- 473
Cdd:PRK07788  210 GIVILTSGTTGTPKGaprpepsPLAPLAGLLSRVP-------FRAGETTLLPAPMFHATGWAHLTlAMALGSTVVLRRRf 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  474 --ETVLDvaklagLIEKQQISVMFITTAFFNVLVDMNPDCLRH-----ARAILFGGERVSVSHVRKALGHLGPgKIKHVY 546
Cdd:PRK07788  283 dpEATLE------DIAKHKATALVVVPVMLSRILDLGPEVLAKydtssLKIIFVSGSALSPELATRALEAFGP-VLYNLY 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  547 GPTESTvFATSYDVHEVEE--GAVsipiGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDltaEKFADN 624
Cdd:PRK07788  356 GSTEVA-FATIATPEDLAEapGTV----GRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD---KQIIDG 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  625 pfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGeKQLCAYYV-- 701
Cdd:PRK07788  428 -------LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgVDDEEFG-QRLRAFVVka 499
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928  702 ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPA 749
Cdd:PRK07788  500 PGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
3879-4309 9.75e-20

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 97.15  E-value: 9.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3879 QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALL-- 3956
Cdd:cd05932     6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvg 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3957 -------TQRHLRERV--------SFAGTFVAVDDEQAYHADgSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCS 4021
Cdd:cd05932    86 klddwkaMAPGVPEGLisislpppSAANCQYQWDDLIAQHPP-LEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAW 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4022 LKLMFANTLQMTEQDRVVQFASLSFDASCWEIF-KALFFGATLYIPTS--TTILDY-----PLFESY-----MNENGITA 4088
Cdd:cd05932   165 AAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEgGSLYGGVLVAFAESldTFVEDVqrarpTLFFSVprlwtKFQQGVQD 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4089 TILPPTYAAYLnpdRMPSLKKLIT----------------GGSAASVEFVQQWKDKV-LYFN-AYGPTEASIVTSIwdea 4150
Cdd:cd05932   245 KIPQQKLNLLL---KIPVVNSLVKrkvlkglgldqcrlagCGSAPVPPALLEWYRSLgLNILeAYGMTENFAYSHL---- 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4151 sDSLGDRKSVPIGRPLANHRIYVVDShnrmlpvgvaGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVR 4230
Cdd:cd05932   318 -NYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF------LRTGDKGE 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4231 WLPDGNLEYLGRIDHQVKI-RGYRIELGEVETQLAKIDAVqEAIVLAREdanGQQQLVAYFVAQRELTA-------AELR 4302
Cdd:cd05932   381 LDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGS---GLPAPLALVVLSEEARLradafarAELE 456

                  ....*..
gi 386647928 4303 ATMSQEL 4309
Cdd:cd05932   457 ASLRAHL 463
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1935-2156 9.81e-20

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 96.55  E-value: 9.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1935 LDRGKLEEAFRQLIARHETLRTGFELVNGEPVQRVYKEV--NFAVEHYRTSEAEAGEVVRGFV----RTFDLAKPPLLRV 2008
Cdd:cd19534    34 LDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVeeLFRLEVVDLSSLAQAAAIEALAaeaqSSLDLEEGPLLAA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2009 GLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYNGESLATLrIQ------YKDYAVWQQSEEQLERVKRQEAYWLD 2082
Cdd:cd19534   114 ALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP-IPlpsktsFQTWAELLAEYAQSPALLEELAYWRE 192
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 2083 MFRGELPvlEMPTDYPrpavRRFEGS-TLSFRLDAGLNEAL-KRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVI 2156
Cdd:cd19534   193 LPAADYW--GLPKDPE----QTYGDArTVSFTLDEEETEALlQEANAAYRTEINDLLLAALALAFQDWTGRAPPAI 262
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1322-1700 1.07e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 96.76  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLtq 1401
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 thlqeraqqwGQTLQavlclDDEAAyaedasnvanvnephdlayVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 1481
Cdd:cd05910    80 ----------GIPKA-----DEPAA-------------------ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 FPVRLLQLASFS-FDVFVgdiartlynGGTMVICPKDD----RIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGL 1556
Cdd:cd05910   126 GEVDLATFPLFAlFGPAL---------GLTSVIPDMDPtrpaRADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGI 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1557 DMSSMELLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEA----AIDSSLYDEPLAKLPEAG-NVPIGKAALNAKFYI 1631
Cdd:cd05910   197 TLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlpvsSIGSRELLATTTAATSGGaGTCVGRPIPGVRVRI 276
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 1632 VDAHLNP---------VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPfveGER-LYRTGDLARWMPDGNVDFIGR 1700
Cdd:cd05910   277 IEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGfWHRMGDLGYLDDEGRLWFCGR 352
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
257-747 1.17e-19

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 97.36  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  257 PRDTTIHRLFEEQAERRPDAVAVT--FEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAG 334
Cdd:PLN02330   25 PDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  335 GAYVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSG---------------TWIRLDDEEAYHEDGSNLESVNGP 399
Cdd:PLN02330  105 GVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGlpvivlgeekiegavNWKELLEAADRAGDTSDNEEILQT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  400 EhLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTNY---IDVTGQDKLLQLSSYsfdgstFDIFG-------ALLNGAKLV 469
Cdd:PLN02330  185 D-LCALPFSSGTTGISKGVMLTHRNLVANLCSSLFsvgPEMIGQVVTLGLIPF------FHIYGitgiccaTLRNKGKVV 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  470 LVPKetvLDVAKLAGLIEKQQISVMFITTAFFNVLVDmNPDCLRharailFGGERVSVSHVRKALGHLGPG--------- 540
Cdd:PLN02330  258 VMSR---FELRTFLNALITQEVSFAPIVPPIILNLVK-NPIVEE------FDLSKLKLQAIMTAAAPLAPElltafeakf 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  541 ---KIKHVYGPTESTVFATSYDVHEVEEG-AVSIPIGGPISNTAIYIVNAQNKLQ-PIGVAGELCVAGDGLARGYLNRPD 615
Cdd:PLN02330  328 pgvQVQEAYGLTEHSCITLTHGDPEKGHGiAKKNSVGFILPNLEVKFIDPDTGRSlPKNTPGELCVRSQCVMQGYYNNKE 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  616 LTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEK-------------- 681
Cdd:PLN02330  408 ETDRTIDEDGW------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDaavvplpdeeagei 481
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  682 --ATVVVRESANGEKQLCAYYVADRSLPANEVRSTlsqelpaymlpsYFVqlEQMPLTTNGKVDRRAL 747
Cdd:PLN02330  482 paACVVINPKAKESEEDILNFVAANVAHYKKVRVV------------QFV--DSIPKSLSGKIMRRLL 535
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
5032-5385 1.19e-19

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 97.59  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5032 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYR---REYRLDQFP-------VRLLQLASFSFDVFVGDIARTLYNGGTM 5101
Cdd:PRK12492  208 DIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRaclSQLGPDGQPlmkegqeVMIAPLPLYHIYAFTANCMCMMVSGNHN 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5102 VIC--PKDDRIDPARLHYWiseeKITIFESTPALIIPFMDYVAEHGLDMSSmvLLITSSDSCSVTdyRVLQERFGSQF-- 5177
Cdd:PRK12492  288 VLItnPRDIPGFIKELGKW----RFSALLGLNTLFVALMDHPGFKDLDFSA--LKLTNSGGTALV--KATAERWEQLTgc 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5178 RIINAYGVTEAAIDSSLydEPLAKLPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEE 5257
Cdd:PRK12492  360 TIVEGYGLTETSPVAST--NPYGELARLGTV--GIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAE 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5258 KfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCA 5336
Cdd:PRK12492  436 A------LDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERsGEAVKLF 509
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 5337 HFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK12492  510 VVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
7471-7869 1.38e-19

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 96.77  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7471 QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLL-- 7548
Cdd:cd05932     6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvg 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7549 ------TQRH-----LQECVSFDGKVIAADDE-QAYGEDGSNLE--PVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSL 7614
Cdd:cd05932    86 klddwkAMAPgvpegLISISLPPPSAANCQYQwDDLIAQHPPLEerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7615 KLMFAETLRITEEDRVVQFASLSFDASCWEIF-KALFFGATLYIP------------AKDTILD-----YPLFesymnEN 7676
Cdd:cd05932   166 AQAGIEHIGTEENDRMLSYLPLAHVTERVFVEgGSLYGGVLVAFAesldtfvedvqrARPTLFFsvprlWTKF-----QQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7677 GITAAILPPTYAIYLSpdrLPSLKKLIT----------------GGSAASVEFVQQWKDKV--RYFNAYGPTEASIVTSV 7738
Cdd:cd05932   241 GVQDKIPQQKLNLLLK---IPVVNSLVKrkvlkglgldqcrlagCGSAPVPPALLEWYRSLglNILEAYGMTENFAYSHL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7739 waASPdgLDLRSVPIGRPIANHQIFIVDSqnhmlpvgvaGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGD 7818
Cdd:cd05932   318 --NYP--GRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFL------RTGD 377
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7819 LARWLPDGNIEYLGRIDHQVKI-RGYRIELGEIEEQLLKIASVQETIVIARG 7869
Cdd:cd05932   378 KGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
1304-1795 1.43e-19

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 97.63  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1304 EKQAERTPEVAAVVYEND------RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAG------ 1371
Cdd:cd05966    60 DRHLKERGDKVAIIWEGDepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGavhsvv 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1372 -GAYvplDPDYPSDRIqfmlEDSAASVLLT---------QTHLQE---RAQQWGQTLQAVL-----------------CL 1421
Cdd:cd05966   140 fAGF---SAESLADRI----NDAQCKLVITadggyrggkVIPLKEivdEALEKCPSVEKVLvvkrtggevpmtegrdlWW 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1422 DDEAAYAEDASNVANVNEPHDLaYVIYTSGTTGRPKGVmiehrslVNTAAGYrreyrldqfpvrLLQLAS---FSFDVFV 1498
Cdd:cd05966   213 HDLMAKQSPECEPEWMDSEDPL-FILYTSGSTGKPKGV-------VHTTGGY------------LLYAATtfkYVFDYHP 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1499 GDI-------------ARTLY----NGGTMVI---CPkdDRIDPARlhYW--ISEEKITIFESTPALIIPFM----DYVA 1552
Cdd:cd05966   273 DDIywctadigwitghSYIVYgplaNGATTVMfegTP--TYPDPGR--YWdiVEKHKVTIFYTAPTAIRALMkfgdEWVK 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1553 EHglDMSSMELLITSSDSCSVTDYRVLQERFG-SQFRIINAYGVTE----------AAIdsslydePL----AKLPEAGN 1617
Cdd:cd05966   349 KH--DLSSLRVLGSVGEPINPEAWMWYYEVIGkERCPIVDTWWQTEtggimitplpGAT-------PLkpgsATRPFFGI 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1618 VPIgkaalnakfyIVDAHLNPVPVGVLGELCIGGI--GVARGYLNRPElteeKFVDSPFVEGERLYRTGDLARWMPDGNV 1695
Cdd:cd05966   420 EPA----------ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYY 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1696 DFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA-KGQkVLCAY------FTAESELKlSELRSSLSQELP 1768
Cdd:cd05966   486 WITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGE-AIYAFvtlkdgEEPSDELR-KELRKHVRKEIG 563
                         570       580
                  ....*....|....*....|....*..
gi 386647928 1769 GYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05966   564 PIATPDKIQFVPGLPKTRSGKIMRRIL 590
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3399-3709 1.56e-19

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 95.63  E-value: 1.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3399 ALTPMQKGMWF----HNTLnrhGG----AYIEqtlFNVRGaLNIELFSRSWNELAARHAVLRTNFHSGWRGEPLQIVYRY 3470
Cdd:cd19535     3 PLTDVQYAYWIgrqdDQEL---GGvgchAYLE---FDGED-LDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3471 kpvEFAYEDLRHLAEAEWSAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFdt 3550
Cdd:cd19535    76 ---GITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELA-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3551 yEAYLRNDLSERPAAPSYSHYIEWLEKQ---DMEAAARYWTGFLAgydsqtTLPQG---KLHNKDGEYTEANILR---SL 3621
Cdd:cd19535   151 -ALYEDPGEPLPPLELSFRDYLLAEQALretAYERARAYWQERLP------TLPPApqlPLAKDPEEIKEPRFTRrehRL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3622 GKSLTERMSRIAKQHQVTVNTLMQAAWGIILQKYNGTDD-----AVFgsvvsGRSAEIAGIEEMIGLFINTIPVRVSCEA 3696
Cdd:cd19535   224 SAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRfllnlTLF-----NRLPLHPDVNDVVGDFTSLLLLEVDGSE 298
                         330
                  ....*....|...
gi 386647928 3697 EQSFADVMKRVQE 3709
Cdd:cd19535   299 GQSFLERARRLQQ 311
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
4163-4337 1.67e-19

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 96.98  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4163 GRPLA-NHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLG 4241
Cdd:PRK10946  356 GRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVG 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4242 RIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTAAELRA-TMSQELPNYMIPSYFVQ 4320
Cdd:PRK10946  430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQLRRfLREQGIAEFKLPDRVEC 509
                         170
                  ....*....|....*..
gi 386647928 4321 LAQMPLTPNGKIDRKAL 4337
Cdd:PRK10946  510 VDSLPLTAVGKVDKKQL 526
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4912-5290 1.68e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 95.99  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLtq 4991
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 thlqeraqqwGQTLQaalclDDEAAyaedasnvanvnephdlayVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQ 5071
Cdd:cd05910    80 ----------GIPKA-----DEPAA-------------------ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5072 FPVRLLQLASFS-FDVFVgdiartlynGGTMVICPKDD----RIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGL 5146
Cdd:cd05910   126 GEVDLATFPLFAlFGPAL---------GLTSVIPDMDPtrpaRADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGI 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5147 DMSSMVLLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEA----AIDSSLYDEPLAKLPEAG-NVPIGKAALNAKFYI 5221
Cdd:cd05910   197 TLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlpvsSIGSRELLATTTAATSGGaGTCVGRPIPGVRVRI 276
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5222 VDAHLNP---------VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPfveGER-LYRTGDLARWMPDGNVDFIGR 5290
Cdd:cd05910   277 IEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGfWHRMGDLGYLDDEGRLWFCGR 352
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
7451-7928 1.70e-19

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 96.98  E-value: 1.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAErmPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGgaYVPIDPEY 7530
Cdd:PRK10946   30 ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALF 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 PEDRI-----------RYMLEDSGAQVL--------LTQRHLQECVS-FDGKVIAADDEQAYGEDGSNLEPVVGP-NHLA 7589
Cdd:PRK10946  106 SHQRSelnayasqiepALLIADRQHALFsdddflntLVAEHSSLRVVlLLNDDGEHSLDDAINHPAEDFTATPSPaDEVA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7590 YVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQF--ASLSFDASCWEIFKALFFGATLYI-PAKDTILDY 7666
Cdd:PRK10946  186 FFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTVVLaPDPSATLCF 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7667 PLFESYmnenGIT-AAILPPTYAIYL-------SPDRLPSLKKLITGGS------AASVEFV-----QQ----WKDKVRY 7723
Cdd:PRK10946  266 PLIEKH----QVNvTALVPPAVSLWLqaiaeggSRAQLASLKLLQVGGArlsetlARRIPAElgcqlQQvfgmAEGLVNY 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7724 FNAYGPTEASIVTSvwaaspdgldlrsvpiGRPIA-NHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKF 7802
Cdd:PRK10946  342 TRLDDSDERIFTTQ----------------GRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7803 VDNPFlagermYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV 7882
Cdd:PRK10946  406 DANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLV 479
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 7883 ADRELTVSELRGTL-SQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK10946  480 VKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
265-747 1.74e-19

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 96.81  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  265 LFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLR-NAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPE 343
Cdd:PRK12492   29 VFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQqHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  344 YPEERIRYMLEDSGTQVLLSQGHLQERVS--FSGTWI------RLDDEE--------------------AYH-------- 387
Cdd:PRK12492  109 YTAREMRHQFKDSGARALVYLNMFGKLVQevLPDTGIeylieaKMGDLLpaakgwlvntvvdkvkkmvpAYHlpqavpfk 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  388 -----EDGSNLESVN-GPEHLTYVIYTSGTTGKPKGNLTTHRNII----RVVKNTNYIDVTGQDKLLQ--------LSSY 449
Cdd:PRK12492  189 qalrqGRGLSLKPVPvGLDDIAVLQYTGGTTGLAKGAMLTHGNLVanmlQVRACLSQLGPDGQPLMKEgqevmiapLPLY 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  450 SFDGSTFDIFGALLNGAKLVLV--PKetvlDVAKLAGLIEKQQISVMFITTAFFNVLVDmNPDclrhARAILFGGERVS- 526
Cdd:PRK12492  269 HIYAFTANCMCMMVSGNHNVLItnPR----DIPGFIKELGKWRFSALLGLNTLFVALMD-HPG----FKDLDFSALKLTn 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  527 ------VSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEE-GAVSIPIGGpisnTAIYIVNAQNKLQPIGVAGEL 599
Cdd:PRK12492  340 sggtalVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPG----TALKVIDDDGNELPLGERGEL 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  600 CVAGDGLARGYLNRPDLTAEKFadnpfaPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAI 679
Cdd:PRK12492  416 CIKGPQVMKGYWQQPEATAEAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928  680 EKATVV-VRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK12492  490 ANCAAIgVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
7454-7928 2.13e-19

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 96.59  E-value: 2.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7454 EQAERMPEKAAVVFENT--QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYP 7531
Cdd:PLN02330   36 QDAELYADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTAL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7532 EDRIRYMLEDSGAQVLLTQR-HLQECVSFDGKVIAADDEQAYGE--------------DGSNLEPVVGPNhLAYVIYTSG 7596
Cdd:PLN02330  116 ESEIKKQAEAAGAKLIVTNDtNYGKVKGLGLPVIVLGEEKIEGAvnwkelleaadragDTSDNEEILQTD-LCALPFSSG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7597 TTGKPKGVMVEHHGLCSlklMFAETLRITEEDRVVQFASLSFdASCWEIFKAL-FFGATLYIPAKDTILDYPLFESYMN- 7674
Cdd:PLN02330  195 TTGISKGVMLTHRNLVA---NLCSSLFSVGPEMIGQVVTLGL-IPFFHIYGITgICCATLRNKGKVVVMSRFELRTFLNa 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7675 ---ENGITAAILPPtyaIYLSPDRLP----------SLKKLITGGSAASVEFVQQWKDK---VRYFNAYGPTEASIVTsV 7738
Cdd:PLN02330  271 litQEVSFAPIVPP---IILNLVKNPiveefdlsklKLQAIMTAAAPLAPELLTAFEAKfpgVQVQEAYGLTEHSCIT-L 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7739 WAASPD---GLDLRSvPIGRPIANHQIFIVDSQNHM-LPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermy 7814
Cdd:PLN02330  347 THGDPEkghGIAKKN-SVGFILPNLEVKFIDPDTGRsLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWL------ 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7815 RTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSE--L 7892
Cdd:PLN02330  420 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEedI 499
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 7893 RGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PLN02330  500 LNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
3876-4337 2.27e-19

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 96.78  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3876 EKSQLTYGELNERANRLARTLRDA-GVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQA 3954
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3955 LLTQRHLRER-------------VSFAGTFVAVDDEQA---------YHA--DGSNLE---PVVGPNHLAYVIYTSGTTG 4007
Cdd:PRK05620  115 IVADPRLAEQlgeilkecpcvraVVFIGPSDADSAAAHmpegikvysYEAllDGRSTVydwPELDETTAAAICYSTGTTG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4008 KPKGVMVEHHGLC--SLKLMFANTLQMTEQDR----VVQFASLSfdascWEI-FKALFFGATLYIPTSTtiLDYPLFESy 4080
Cdd:PRK05620  195 APKGVVYSHRSLYlqSLSLRTTDSLAVTHGESflccVPIYHVLS-----WGVpLAAFMSGTPLVFPGPD--LSAPTLAK- 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4081 mnengITATILP------PT-----YAAYLN--PDRMpSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVTS 4145
Cdd:PRK05620  267 -----IIATAMPrvahgvPTlwiqlMVHYLKnpPERM-SLQEIYVGGSAVPPILIKAWEERygVDVVHVWGMTETSPVGT 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4146 IWDEASDSLGDRKS---VPIGR-PLA-NHRI----YVVDSHNRMlpvgvAGELCISGVGLARGYLNRPELT----AEKFV 4212
Cdd:PRK05620  341 VARPPSGVSGEARWayrVSQGRfPASlEYRIvndgQVMESTDRN-----EGEIQVRGNWVTASYYHSPTEEgggaASTFR 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4213 DNPFEPGERMY------RTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN-GQQQ 4285
Cdd:PRK05620  416 GEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERP 495
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 4286 L----VAYFVAQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK05620  496 LavtvLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
2334-2828 2.41e-19

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 96.38  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2334 FNATAADYEADKtihqlfEEQAERiPDHPA---VVFEGQQL--TYRELNERANRLARTL-QALGVKTDQPVGLMLERSLE 2407
Cdd:cd05928     7 FASDVLDQWADK------EKAGKR-PPNPAlwwVNGKGDEVkwSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2408 MVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQERV-SFAG------TVVTVDDE--------QAYA 2472
Cdd:cd05928    80 WWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVdSVASecpslkTKLLVSEKsrdgwlnfKELL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2473 GDGSNLESAV--GPNDLAYIIYTSGTTGKPKgvMVEH-HGLCSLKqMFANT---LQINAQDRVVQFASLSF-DASCWEVF 2545
Cdd:cd05928   160 NEASTEHHCVetGSQEPMAIYFTSGTTGSPK--MAEHsHSSLGLG-LKVNGrywLDLTASDIMWNTSDTGWiKSAWSSLF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2546 QTLFFGATLYI---PTKETILDYQWFERYmsdnGITTATLPPT-YAVYLNPD----HMPDFKRLIAAGSASSLELLQQWK 2617
Cdd:cd05928   237 EPWIQGACVFVhhlPRFDPLVILKTLSSY----PITTFCGAPTvYRMLVQQDlssyKFPSLQHCVTGGEPLNPEVLEKWK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2618 DK--VKYFNAYGPTEDS-ICTTIWTpstediSQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCI-----AGVGLAR 2689
Cdd:cd05928   313 AQtgLDIYEGYGQTETGlICANFKG------MKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFS 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2690 GYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHD 2769
Cdd:cd05928   387 GYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSP 459
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 2770 DASGQKQLCAYFV-------ADRTMTVGELRGELSGELPGYMIP--AHFVQleRMPLTPNGKIDRKAL 2828
Cdd:cd05928   460 DPIRGEVVKAFVVlapqflsHDPEQLTKELQQHVKSVTAPYKYPrkVEFVQ--ELPKTVTGKIQRNEL 525
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
4901-5387 2.48e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 96.22  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML 4980
Cdd:PRK13383   49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4981 EDSAASVLLTQthlQERAQQWGQTLQAALCLDDEAAYAEDASNVANVNEPHDLayVIYTSGTTGRPKGVmiEHRSLVNTA 5060
Cdd:PRK13383  129 RAHHISTVVAD---NEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRI--VLLTSGTTGKPKGV--PRAPQLRSA 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYrLDQFPVRLLQLASFSFDVF----VGDIARTLYNGGTMVICPKDD---RIDPARLHywiSEEKITIFESTPAL 5133
Cdd:PRK13383  202 VGVWVTI-LDRTRLRTGSRISVAMPMFhglgLGMLMLTIALGGTVLTHRHFDaeaALAQASLH---RADAFTAVPVVLAR 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5134 IIPFMDYVAEHGlDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDSSLYDEPLAKLPEAgnvpIGKA 5213
Cdd:PRK13383  278 ILELPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTYGDI--LYNGYGSTEVGIGALATPADLRDAPET----VGKP 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5214 ALNAKFYIVDAHLNPVPVGVLGELCIGGigvargylnrpELTEEKFVD---SPFVEGerLYRTGDLARWMPDGNVDFIGR 5290
Cdd:PRK13383  351 VAGCPVRILDRNNRPVGPRVTGRIFVGG-----------ELAGTRYTDgggKAVVDG--MTSTGDMGYLDNAGRLFIVGR 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5291 IDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAE--SELKLSELRSSLSQELPGYMIPSYFVQ 5368
Cdd:PRK13383  418 EDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHpgSGVDAAQLRDYLKDRVSRFEQPRDINI 497
                         490
                  ....*....|....*....
gi 386647928 5369 LEQLPLTANGKIDRKALPA 5387
Cdd:PRK13383  498 VSSIPRNPTGKVLRKELPG 516
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
3864-4337 2.77e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 95.91  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKS--QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPED 3941
Cdd:PRK13391    7 AQTTPDKPAVIMASTgeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3942 RIRYMLEDSGAQALLTQRHLRERVSFAGTFV-AVDDEQAYHADGSnLEPVVG-PNHLAYV--------------IYTSGT 4005
Cdd:PRK13391   87 EAAYIVDDSGARALITSAAKLDVARALLKQCpGVRHRLVLDGDGE-LEGFVGyAEAVAGLpatpiadeslgtdmLYSSGT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4006 TGKPKGVMVE--HHGL---CSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATlyiptsTTILDYPLFESY 4080
Cdd:PRK13391  166 TGRPKGIKRPlpEQPPdtpLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGT------VIVMEHFDAEQY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4081 M---NENGITATILPPTYAAylnpdRM-------------PSLKKLITGGSAASVEFVQQ---WKDKVLYfNAYGPTEAS 4141
Cdd:PRK13391  240 LaliEEYGVTHTQLVPTMFS-----RMlklpeevrdkydlSSLEVAIHAAAPCPPQVKEQmidWWGPIIH-EYYAATEGL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4142 IVTSIwdEASDSLGDRKSVpiGRPLANhRIYVVDSHNRMLPVGVAGELCISGvGLARGYLNRPELTAEKfvdnpFEPGER 4221
Cdd:PRK13391  314 GFTAC--DSEEWLAHPGTV--GRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEA-----RHPDGT 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4222 MYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN-GQQ-----QLVAYFVAQRE 4295
Cdd:PRK13391  383 WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDlGEEvkavvQPVDGVDPGPA 462
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928 4296 LtAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK13391  463 L-AAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PLN02246 PLN02246
4-coumarate--CoA ligase
2353-2830 2.86e-19

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 96.20  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2353 EQAERIPDHPAVV--FEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYP 2430
Cdd:PLN02246   31 ERLSEFSDRPCLIdgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2431 EDRISYMLEDSSAQVLLAQRRLQERVS-FAG----TVVTVDD---------EQAYAGDGSNLESAVGPNDLAYIIYTSGT 2496
Cdd:PLN02246  111 PAEIAKQAKASGAKLIITQSCYVDKLKgLAEddgvTVVTIDDppegclhfsELTQADENELPEVEISPDDVVALPYSSGT 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2497 TGKPKGVMVEHHGL-CSLKQMF--AN-TLQINAQDRVV----QFASLSFDAScweVFQTLFFGATLYIPTK-ETILDYQW 2567
Cdd:PLN02246  191 TGLPKGVMLTHKGLvTSVAQQVdgENpNLYFHSDDVILcvlpMFHIYSLNSV---LLCGLRVGAAILIMPKfEIGALLEL 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2568 FERYmsdnGITTATL-PP-TYAVYLNPD-HMPDFK--RLIAAGSASsleLLQQWKDKV--KYFNA-----YGPTED---- 2631
Cdd:PLN02246  268 IQRH----KVTIAPFvPPiVLAIAKSPVvEKYDLSsiRMVLSGAAP---LGKELEDAFraKLPNAvlgqgYGMTEAgpvl 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2632 SICTTIWTPSTEdisqLKSVPIGGPIVNHRIYIVDahyqP-----VPVGVAGELCIAGVGLARGYLNRPDLTAekfvdnp 2706
Cdd:PLN02246  341 AMCLAFAKEPFP----VKSGSCGTVVRNAELKIVD----PetgasLPRNQPGEICIRGPQIMKGYLNDPEATA------- 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2707 fepgermyRTGDLAKWLPDGTIEYL---------GRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAH-DDASGqkQ 2776
Cdd:PLN02246  406 --------NTIDKDGWLHTGDIGYIddddelfivDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMkDEVAG--E 475
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2777 LCAYFVA---DRTMTVGELRGELSGELPGY--MIPAHFVqlERMPLTPNGKIDRKALPA 2830
Cdd:PLN02246  476 VPVAFVVrsnGSEITEDEIKQFVAKQVVFYkrIHKVFFV--DSIPKAPSGKILRKDLRA 532
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2931-3351 2.91e-19

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 94.82  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2931 LTPIQHWFF---EPQFAEPHHFNQSVMLHRRDgFDEAAIRKVLQKLVEHHDALRVVFHksENGYTAWNRAIGEGELYGLE 3007
Cdd:cd19536     4 LSSLQEGMLfhsLLNPGGSVYLHNYTYTVGRR-LNLDLLLEALQVLIDRHDILRTSFI--EDGLGQPVQVVHRQAQVPVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3008 VVDLKGIEESAQAVEA-KANEIQSSIDLEAGPFVKAGLFQCADGDHLLIVI--HHGVVDGVSWRILLEDLAIGYEQAVKG 3084
Cdd:cd19536    81 ELDLTPLEEQLDPLRAyKEETKIRRFDLGRAPLVRAALVRKDERERFLLVIsdHHSILDGWSLYLLVKEILAVYNQLLEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3085 EELRFPAKTDaYRTWSEQLAAYAQSPVIERelaYWKRV---AQTEVQPLPKDEQVDVSlQQDSE---SISIEWTREETEq 3158
Cdd:cd19536   161 KPLSLPPAQP-YRDFVAHERASIQQAASER---YWREYlagATLATLPALSEAVGGGP-EQDSEllvSVPLPVRSRSLA- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3159 llkgvhRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGRESIMTDIDitRTVGWFTSKYPVVLELEQGkDISYLLK 3238
Cdd:cd19536   235 ------KRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRVTLSEE-TVEDLLK 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3239 KTKEDLRGIPNKgigygicRYLSAAknDIAWGAEPEVSFNYLGQF-DQDLQNSDIGVSAHTGGKQSSDRQKRIFVLDING 3317
Cdd:cd19536   306 RAQEQELESLSH-------EQVPLA--DIQRCSEGEPLFDSIVNFrHFDLDFGLPEWGSDEGMRRGLLFSEFKSNYDVNL 376
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 386647928 3318 MIAD--GTLSLELSYNGKEYRRETMERLAASLQESL 3351
Cdd:cd19536   377 SVLPkqDRLELKLAYNSQVLDEEQAQRLAAYYKSAI 412
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2931-3357 3.48e-19

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 94.58  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2931 LTPIQ-----HWFFEPqfAEPHHFNQSVM-LHRRdgFDEAAIRKVLQKLVEHHDALRVVFHKSENGytAWNRAIGEGELY 3004
Cdd:cd19543     4 LSPMQegmlfHSLLDP--GSGAYVEQMVItLEGP--LDPDRFRAAWQAVVDRHPILRTSFVWEGLG--EPLQVVLKDRKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3005 GLEVVDLKGIEESAQAVEA---KANEIQSSIDLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQ 3080
Cdd:cd19543    78 PWRELDLSHLSEAEQEAELealAEEDRERGFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKELFAIYAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3081 AVKGEELRFPA---------------KTDAYRTWSEQLAAYAQSPvierelaywkrvaqtevqPLPKDEQVDVSLQQDSE 3145
Cdd:cd19543   158 LGEGQPPSLPPvrpyrdyiawlqrqdKEAAEAYWREYLAGFEEPT------------------PLPKELPADADGSYEPG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3146 SISIEWTREETEQLLKGVhRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGRESIMTDIDitRTVGWFTSKYPVVL 3225
Cdd:cd19543   220 EVSFELSAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIE--TMVGLFINTLPVRV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3226 ELEQGKDISYLLKKTKEDLrgipNKGIGYGicrYLSAAknDI-AWGAEPEVSF-------NY-------LGQFDQDLQNS 3290
Cdd:cd19543   297 RLDPDQTVLELLKDLQAQQ----LELREHE---YVPLY--EIqAWSEGKQALFdhllvfeNYpvdesleEEQDEDGLRIT 367
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 3291 DIGVSAHTGgkqssdrqkrifvLDINGMIA-DGTLSLELSYNGKEYRRETMERLAASLQESLRVIIAH 3357
Cdd:cd19543   368 DVSAEEQTN-------------YPLTVVAIpGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
PRK09274 PRK09274
peptide synthase; Provisional
4901-5290 3.49e-19

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 96.12  E-value: 3.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4901 PEAAAVV----------YENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPD 4970
Cdd:PRK09274   20 PDQLAVAvpggrgadgkLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4971 YPSDRIQFMLEDSAASVLLTQT--HLQERAQQW------------------GQTLQAALCLDDEAAYAedasnVANVnEP 5030
Cdd:PRK09274  100 MGIKNLKQCLAEAQPDAFIGIPkaHLARRLFGWgkpsvrrlvtvggrllwgGTTLATLLRDGAAAPFP-----MADL-AP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5031 HDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLqlasfSFDVFVgdiartLYN---GGTMVICPKD 5107
Cdd:PRK09274  174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP-----TFPLFA------LFGpalGMTSVIPDMD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5108 DR----IDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLItsSDSCSVTdyRVLQERFGSQF----RI 5179
Cdd:PRK09274  243 PTrpatVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVI--SAGAPVP--IAVIERFRAMLppdaEI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5180 INAYGVTEA----AIDSslyDEPLAKLPEA----GNVPIGKAALNAKFYIVDAHLNP---------VPVGVLGELCIGGI 5242
Cdd:PRK09274  319 LTPYGATEAlpisSIES---REILFATRAAtdngAGICVGRPVDGVEVRIIAISDAPipewddalrLATGEIGEIVVAGP 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 5243 GVARGYLNRPELTEE-KFVDSpfvEGERLYRTGDLARWMPDGNVDFIGR 5290
Cdd:PRK09274  396 MVTRSYYNRPEATRLaKIPDG---QGDVWHRMGDLGYLDAQGRLWFCGR 441
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
270-744 3.64e-19

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 95.64  E-value: 3.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPDAVAVTF-----EDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEY 344
Cdd:cd05970    27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  345 PEERIRYMLEDSGTQ--VLLSQGHLQERVSFS----GTWIRL----DDE----EAYHEDGSNL---------ESVNGPEH 401
Cdd:cd05970   107 TAKDIVYRIESADIKmiVAIAEDNIPEEIEKAapecPSKPKLvwvgDPVpegwIDFRKLIKNAspdferptaNSYPCGED 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  402 LTYVIYTSGTTGKPKgnLTTHRNII---RVVKNTNYIDVTGQDKLLQLSSYSFDGSTF-DIFGALLNGAKlVLVPKETVL 477
Cdd:cd05970   187 ILLVYFSSGTTGMPK--MVEHDFTYplgHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAA-VFVYDYDKF 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  478 DVAKLAGLIEKQQISVMFITTAFFNVLV-----DMNPDCLRHAraiLFGGERVSVSHVRKALGHLGPgKIKHVYGPTEST 552
Cdd:cd05970   264 DPKALLEKLSKYGVTTFCAPPTIYRFLIredlsRYDLSSLRYC---TTAGEALNPEVFNTFKEKTGI-KLMEGFGQTETT 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  553 VFATSYDVHEVEEGAvsipIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGD-----GLARGYLNRPDLTAEKFADNpfa 627
Cdd:cd05970   340 LTIATFPWMEPKPGS----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG--- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  628 pgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEA-IEKATVVVRESANGEK-----QLCAYYV 701
Cdd:cd05970   413 ----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAvLECAVTGVPDPIRGQVvkatiVLAKGYE 488
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 386647928  702 ADRSLpANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDR 744
Cdd:cd05970   489 PSEEL-KKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
1442-1795 4.69e-19

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 92.39  E-value: 4.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFsfdvFVGDIA---RTLYNGGTMVIcpkDD 1518
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLY----HVGGLAilvRSLLAGAELVL---LE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1519 RIDPARlhywiseEKITIFESTPALIIPFM-DYVAEHGLDMSSMELL---------ITSSDSCSVTDYRVlqerfgsqfR 1588
Cdd:cd17630    74 RNQALA-------EDLAPPGVTHVSLVPTQlQRLLDSGQGPAALKSLravllggapIPPELLERAADRGI---------P 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1589 IINAYGVTEAAIDSSLYDEPLAKLPEAGNVPIGkaalnAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPElteek 1668
Cdd:cd17630   138 LYTTYGMTETASQVATKRPDGFGRGGVGVLLPG-----RELRIVED----------GEIWVGGASLAMGYLRGQL----- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1669 fVDSPFVEGerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAY 1747
Cdd:cd17630   198 -VPEFNEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElGQRPVAVI 274
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 1748 fTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd17630   275 -VGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
2342-2772 5.07e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 95.88  E-value: 5.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2342 EADKTIHQLFEEQAERIPDHPAVVFEGQ------QLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAV 2415
Cdd:PRK12582   46 PYPRSIPHLLAKWAAEAPDRPWLAQREPghgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2416 LKAGGAYVPIDPEY---PED--RISYMLEDSSAQVLLAQ------RRLQE-------------------RVSF---AGTV 2462
Cdd:PRK12582  126 MQAGVPAAPVSPAYslmSHDhaKLKHLFDLVKPRVVFAQsgapfaRALAAldlldvtvvhvtgpgegiaSIAFadlAATP 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2463 VTVDDEQAYAgdgsnlesAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQ----------F 2532
Cdd:PRK12582  206 PTAAVAAAIA--------AITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVsldwmpwnhtM 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2533 AS-LSFDASCWEvfqtlffGATLYI----PT----KETILDYqwfeRYMSDngITTATLPPTYAVYLnpDHMPD------ 2597
Cdd:PRK12582  278 GGnANFNGLLWG-------GGTLYIddgkPLpgmfEETIRNL----REISP--TVYGNVPAGYAMLA--EAMEKddalrr 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2598 --FKRL--IAAGSAS-SLELLQQWKD--------KVKYFNAYGPTEDS--ICTTIWTPSTEDIsqlksvpIGGPIVNHRI 2662
Cdd:PRK12582  343 sfFKNLrlMAYGGATlSDDLYERMQAlavrttghRIPFYTGYGATETAptTTGTHWDTERVGL-------IGLPLPGVEL 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2663 YIvdahyqpVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWL----PDGTIEYLGRIDHQV 2738
Cdd:PRK12582  416 KL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGRVAEDF 482
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 2739 KI-RGYRIELGEIEEQLLKVAS--VQEAIVIAHDDAS 2772
Cdd:PRK12582  483 KLsTGTWVSVGTLRPDAVAACSpvIHDAVVAGQDRAF 519
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
7468-7937 5.32e-19

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 95.35  E-value: 5.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7468 ENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVL 7547
Cdd:PRK04319   70 RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7548 LT-----QR-------HLQ------ECVSFDGKVIAADDEQAYGEDGSNLEPvVGPNHLAYVIYTSGTTGKPKGV----- 7604
Cdd:PRK04319  150 ITtpallERkpaddlpSLKhvllvgEDVEEGPGTLDFNALMEQASDEFDIEW-TDREDGAILHYTSGSTGKPKGVlhvhn 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7605 -MVEHH--GLCSLKLmfaetlritEEDRV---------VQFASlsfdascWEIFKALFFGATLYIPAKD-------TILD 7665
Cdd:PRK04319  229 aMLQHYqtGKYVLDL---------HEDDVywctadpgwVTGTS-------YGIFAPWLNGATNVIDGGRfsperwyRILE 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7666 yplfesymnENGITAAILPPTyAIYL----SPD-----RLPSLKKLITGGSAASVEFVqQWKDKV---RYFNAYGPTE-A 7732
Cdd:PRK04319  293 ---------DYKVTVWYTAPT-AIRMlmgaGDDlvkkyDLSSLRHILSVGEPLNPEVV-RWGMKVfglPIHDNWWMTEtG 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7733 SIVTSVWAAspdgLDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISgAG---LARGYLNRPELTAEKFVDNpfla 7809
Cdd:PRK04319  362 GIMIANYPA----MDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNPEKYESYFAGD---- 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7810 gerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAyFVA------ 7883
Cdd:PRK04319  433 ---WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKA-FVAlrpgye 508
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7884 -DRELTvSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPA-----PEGSMQT 7937
Cdd:PRK04319  509 pSEELK-EEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwelglPEGDLST 567
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
2486-2823 5.45e-19

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 92.56  E-value: 5.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2486 DLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDR--VVQ--FASLSFDASCWEVFQTlffGATLYiptKET 2561
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRylIINpfFHTFGYKAGIVACLLT---GATVV---PVA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2562 ILDYQWFERYMSDNGITTATLPPTyaVYLNPDHMPDFK-------RLIAAGSAS-SLELLQQWKDKVKYFN---AYGPTE 2630
Cdd:cd17638    75 VFDVDAILEAIERERITVLPGPPT--LFQSLLDHPGRKkfdlsslRAAVTGAATvPVELVRRMRSELGFETvltAYGLTE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2631 dSICTTIWTPstEDISQLKSVPIGGPIVNHRIYIVDahyqpvpvgvAGELCIAGVGLARGYLNRPDLTAEKfVDnpfepG 2710
Cdd:cd17638   153 -AGVATMCRP--GDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEA-ID-----A 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2711 ERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTVG 2790
Cdd:cd17638   214 DGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLT 293
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 386647928 2791 E--LRGELSGELPGYMIPAHFVQLERMPLTPNGKI 2823
Cdd:cd17638   294 EedVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
5945-6422 5.74e-19

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 95.06  E-value: 5.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK13383   45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDGAYHEDGSNLEPVNGPEHlTYVIYTSGTTGRPKGV--MVEHRNVVR 6102
Cdd:PRK13383  125 AAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG-RIVLLTSGTTGKPKGVprAPQLRSAVG 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6103 LvkntnYVELNEQTHiLQTGAVVFDAS-TFEIWG------ALLNGGRLYVVRN---ETILDAVSLKNAIQQYGINTMW-- 6170
Cdd:PRK13383  204 V-----WVTILDRTR-LRTGSRISVAMpMFHGLGlgmlmlTIALGGTVLTHRHfdaEAALAQASLHRADAFTAVPVVLar 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6171 -LTAP----LYNQLSQqdsgmfagLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTEnttfstthtiVGEQKEAVP- 6244
Cdd:PRK13383  278 iLELPprvrARNPLPQ--------LRVVMSSGDRLD-PTLGQRFMDTYGDILYNGYGSTE----------VGIGALATPa 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6245 --------IGKPINNSTAYIVDSKLSllPVG--VWGELIVGGDGVARGYLNrpelTAEKFVESSFLpgercyRTGDLARW 6314
Cdd:PRK13383  339 dlrdapetVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGGELAGTRYTD----GGGKAVVDGMT------STGDMGYL 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6315 LPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAALSQEL 6392
Cdd:PRK13383  407 DNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHpgSGVDAAQLRDYLKDRV 486
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 6393 PNYMIPSHFVPLERMPLTPNGKIDRRALPA 6422
Cdd:PRK13383  487 SRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
5032-5385 5.76e-19

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 92.39  E-value: 5.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5032 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFsfdvFVGDIA---RTLYNGGTMVIcpkDD 5108
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLY----HVGGLAilvRSLLAGAELVL---LE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5109 RIDPARlhywiseEKITIFESTPALIIPFM-DYVAEHGLDMSSM-----VLLITSSDScsvtdyRVLQERFGSQ-FRIIN 5181
Cdd:cd17630    74 RNQALA-------EDLAPPGVTHVSLVPTQlQRLLDSGQGPAALkslraVLLGGAPIP------PELLERAADRgIPLYT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5182 AYGVTEAAIDSSLYDEPLAKLPEAGNVPIGkaalnAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPElteekfVD 5261
Cdd:cd17630   141 TYGMTETASQVATKRPDGFGRGGVGVLLPG-----RELRIVED----------GEIWVGGASLAMGYLRGQL------VP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5262 SPFVEGerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLcAHFTA 5340
Cdd:cd17630   200 EFNEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElGQRPV-AVIVG 276
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 5341 ESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd17630   277 RGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
405-744 5.83e-19

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 92.33  E-value: 5.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 VIYTSGTTGKPKGNLTTHRNIIRVVKNTNY-IDVTGQD---KLLQLSSYSFDGSTFDIFGAllnGAKLVLVPKetvLDVA 480
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHaMGLTEADvylNMLPLFHIAGLNLALATFHA---GGANVVMEK---FDPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  481 KLAGLIEKQQISVMF----ITTAFFNVLVDMNPDcLRHARAILfgGerVSVSHVRKALGHLGPGKIKHVYGPTESTVFAT 556
Cdd:cd17637    79 EALELIEEEKVTLMGsfppILSNLLDAAEKSGVD-LSSLRHVL--G--LDAPETIQRFEETTGATFWSLYGQTETSGLVT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  557 SYDVHEvEEGAVsipiGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTG 636
Cdd:cd17637   154 LSPYRE-RPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHTG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  637 DLARWLPDGTIEYVGRI--DDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGE--KQLCAYYvADRSLPANEV 711
Cdd:cd17637   222 DLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIgVPDPKWGEgiKAVCVLK-PGATLTADEL 300
                         330       340       350
                  ....*....|....*....|....*....|...
gi 386647928  712 RSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDR 744
Cdd:cd17637   301 IEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK09274 PRK09274
peptide synthase; Provisional
258-658 6.44e-19

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 94.97  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  258 RDTTIHRLFEEQAERRPDAVAVTFED----------RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGI 327
Cdd:PRK09274    4 SMANIARHLPRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  328 MGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQ--GHL------------QERVSFSGTWI----RLDDEEAyHED 389
Cdd:PRK09274   84 FALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIpkAHLarrlfgwgkpsvRRLVTVGGRLLwggtTLATLLR-DGA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  390 GSNLESVN-GPEHLTYVIYTSGTTGKPKGNLTTHRNI---IRVVKNTnYIDVTGqdkllqlssySFDGSTFDIFgALLN- 464
Cdd:PRK09274  163 AAPFPMADlAPDDMAAILFTSGSTGTPKGVVYTHGMFeaqIEALRED-YGIEPG----------EIDLPTFPLF-ALFGp 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  465 --GAKLVlVP-----KETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDmnpDCLRHA------RAILFGGERV---SVS 528
Cdd:PRK09274  231 alGMTSV-IPdmdptRPATVDPAKLFAAIERYGVTNLFGSPALLERLGR---YGEANGiklpslRRVISAGAPVpiaVIE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  529 HVRKALGHlgPGKIKHVYGPTES---------TVFATSYDVHEVEEGA-VSIPIGG------PISNTAIYIVNAQNKLqP 592
Cdd:PRK09274  307 RFRAMLPP--DAEILTPYGATEAlpissiesrEILFATRAATDNGAGIcVGRPVDGvevriiAISDAPIPEWDDALRL-A 383
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  593 IGVAGELCVAGDGLARGYLNRPDLTAE-KFADnpfAPGERMYRTGDLARWLPDGTIEYVGRIDDQVK 658
Cdd:PRK09274  384 TGEIGEIVVAGPMVTRSYYNRPEATRLaKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
2359-2855 7.24e-19

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 95.46  E-value: 7.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEG------QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAG-------GAYVP- 2424
Cdd:cd05967    65 GDQIALIYDSpvtgteRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAAk 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2425 -----ID---PEY---------PEDRISYM------LEDSSAQ---VLLAQRRLQERVSFA-GTVVTVDDEQAYAG--DG 2475
Cdd:cd05967   145 elasrIDdakPKLivtascgiePGKVVPYKplldkaLELSGHKphhVLVLNRPQVPADLTKpGRDLDWSELLAKAEpvDC 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2476 SNLESavgpNDLAYIIYTSGTTGKPKGVMVEHHGLC-SLKQMFANTLQINAQDrvVQFAslsfdAS--CWEV------FQ 2546
Cdd:cd05967   225 VPVAA----TDPLYILYTSGTTGKPKGVVRDNGGHAvALNWSMRNIYGIKPGD--VWWA-----ASdvGWVVghsyivYG 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2547 TLFFGATlyiptkeTILdY-----------QWFeRYMSDNGITTATLPPT----------YAVYLNPDHMPDFKRLIAAG 2605
Cdd:cd05967   294 PLLHGAT-------TVL-YegkpvgtpdpgAFW-RVIEKYQVNALFTAPTairairkedpDGKYIKKYDLSSLRTLFLAG 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2606 S---ASSLELLQQwKDKVKYFNAYGPTEdsictTIWtPSTEDISQLKSVPI-----GGPIVNHRIYIVDAHYQPVPVGVA 2677
Cdd:cd05967   365 ErldPPTLEWAEN-TLGVPVIDHWWQTE-----TGW-PITANPVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNEL 437
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2678 GELCIAGvGLARGYLNRPDLTAEKFVDNPFE--PGerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLL 2755
Cdd:cd05967   438 GNIVIKL-PLPPGCLLTLWKNDERFKKLYLSkfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2756 KVASVQEAIVIA-HDDASGQKQLCAY-FVADRTMTVGELRGELSGELPGYMIP------AHFVQleRMPLTPNGKIDRKA 2827
Cdd:cd05967   515 SHPAVAECAVVGvRDELKGQVPLGLVvLKEGVKITAEELEKELVALVREQIGPvaafrlVIFVK--RLPKTRSGKILRRT 592
                         570       580
                  ....*....|....*....|....*....
gi 386647928 2828 LPApqgnASAGADYVAPRS-EEEKVLADV 2855
Cdd:cd05967   593 LRK----IADGEDYTIPSTiEDPSVLDEI 617
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
2371-2728 7.42e-19

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 94.97  E-value: 7.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKT--DQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLA 2448
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2449 QRRLqervsfagTVVTVDD-EQAYAGDGSNLESAVgPNDLAYIIYTSGTTGKPKGVMVEHHGLCS----LKQMFANTLQI 2523
Cdd:cd05927    86 DAGV--------KVYSLEEfEKLGKKNKVPPPPPK-PEDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEILNKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2524 NAQDRVVQFASLS--FDASCWEVFqtLFFGA---------------------TLYI---------------------PTK 2559
Cdd:cd05927   157 NPTDVYISYLPLAhiFERVVEALF--LYHGAkigfysgdirlllddikalkpTVFPgvprvlnriydkifnkvqakgPLK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2560 ETILD--YQWFERYMSDNGITTatlpptyavylnpDHMPD---FK----------RLIAAGSA----SSLELLQQWKDkV 2620
Cdd:cd05927   235 RKLFNfaLNYKLAELRSGVVRA-------------SPFWDklvFNkikqalggnvRLMLTGSAplspEVLEFLRVALG-C 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2621 KYFNAYGPTEDSICTTIWTPSTEDISQlksvpIGGPIVNHRIYIVDA------HYQPVPvgvAGELCIAGVGLARGYLNR 2694
Cdd:cd05927   301 PVLEGYGQTECTAGATLTLPGDTSVGH-----VGGPLPCAEVKLVDVpemnydAKDPNP---RGEVCIRGPNVFSGYYKD 372
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 2695 PDLTAEKFVDNPFepgermYRTGDLAKWLPDGTI 2728
Cdd:cd05927   373 PEKTAEALDEDGW------LHTGDIGEWLPNGTL 400
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
1291-1813 7.43e-19

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 95.46  E-value: 7.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1291 PDAPENEVFHALfEKQAER-TPEVAAVVYEN------DRLTYRELNERANRLARMLRAQGVKPNQLVGI----------- 1352
Cdd:cd05967    45 VGGRLNTCYNAL-DRHVEAgRGDQIALIYDSpvtgteRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympmipeaaia 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1353 ----------------------LADRSAD----LLVGAlAVWKAGGAYVPLDPdypsdriqfmLEDSAASVLLTQTH--- 1403
Cdd:cd05967   124 mlacarigaihsvvfggfaakeLASRIDDakpkLIVTA-SCGIEPGKVVPYKP----------LLDKALELSGHKPHhvl 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1404 LQERAQQWGQTLQAVLCLD--DEAAYAEDAsNVANVNEPHDLaYVIYTSGTTGRPKGVmiehrslVNTAAGYrreyrldq 1481
Cdd:cd05967   193 VLNRPQVPADLTKPGRDLDwsELLAKAEPV-DCVPVAATDPL-YILYTSGTTGKPKGV-------VRDNGGH-------- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 fPVRLLQLASFSFDVFVGDIART-----------------LYNGGTMVICP-KDDRI-DPARlhYW--ISEEKITIFEST 1540
Cdd:cd05967   256 -AVALNWSMRNIYGIKPGDVWWAasdvgwvvghsyivygpLLHGATTVLYEgKPVGTpDPGA--FWrvIEKYQVNALFTA 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1541 PALI--IPFMDYVAEHG--LDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTE-----AAIDSSLYDEPlak 1611
Cdd:cd05967   333 PTAIraIRKEDPDGKYIkkYDLSSLRTLFLAGERLDPPTLEWAENTLGVP--VIDHWWQTEtgwpiTANPVGLEPLP--- 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1612 lPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGiGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMP 1691
Cdd:cd05967   408 -IKAGSP--GKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDE 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1692 DGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA-KGQKVLCAYF-------TAESELKlsELRSSL 1763
Cdd:cd05967   484 DGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDElKGQVPLGLVVlkegvkiTAEELEK--ELVALV 561
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 1764 SQELPGYMIPSYFVQLEQLPLTANGKIDRKALpapdASMQTGMEYVAPRT 1813
Cdd:cd05967   562 REQIGPVAAFRLVIFVKRLPKTRSGKILRRTL----RKIADGEDYTIPST 607
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
4881-5403 7.56e-19

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 95.07  E-value: 7.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4881 PDAPENEAFHALFEKQAECTPEAAAVVYEN------DRLTYRELNERANRLARTLRAQGVKPNQLVGI------------ 4942
Cdd:cd05967    45 VGGRLNTCYNALDRHVEAGRGDQIALIYDSpvtgteRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympmipeaaiam 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4943 ---------------------LADRSAD----LLVGAlAVWKAGGAYVPLDPdypsdriqfmLEDSAASVLLTQTH---L 4994
Cdd:cd05967   125 lacarigaihsvvfggfaakeLASRIDDakpkLIVTA-SCGIEPGKVVPYKP----------LLDKALELSGHKPHhvlV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4995 QERAQQWGQTLQAALCLD--DEAAYAEDAsNVANVNEPHDLaYVIYTSGTTGRPKGVmiehrslVNTAAGYrreyrldqf 5072
Cdd:cd05967   194 LNRPQVPADLTKPGRDLDwsELLAKAEPV-DCVPVAATDPL-YILYTSGTTGKPKGV-------VRDNGGH--------- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5073 PVRLLQLASFSFDVFVGDIART-----------------LYNGGTMVICP-KDDRI-DPARlhYW--ISEEKITIFESTP 5131
Cdd:cd05967   256 AVALNWSMRNIYGIKPGDVWWAasdvgwvvghsyivygpLLHGATTVLYEgKPVGTpDPGA--FWrvIEKYQVNALFTAP 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 ALI--IPFMDYVAEHG--LDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTE-----AAIDSSLYDEPlakl 5202
Cdd:cd05967   334 TAIraIRKEDPDGKYIkkYDLSSLRTLFLAGERLDPPTLEWAENTLGVP--VIDHWWQTEtgwpiTANPVGLEPLP---- 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5203 PEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGiGVARGYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPD 5282
Cdd:cd05967   408 IKAGSP--GKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDED 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5283 GNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA-KGQKVLC-----AHFTAESELKLSELRSSLSQE 5356
Cdd:cd05967   485 GYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDElKGQVPLGlvvlkEGVKITAEELEKELVALVREQ 564
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 5357 LPGYMIPSYFVQLEQLPLTANGKIDRKALpapdASMQTGMEYVAPRT 5403
Cdd:cd05967   565 IGPVAAFRLVIFVKRLPKTRSGKILRRTL----RKIADGEDYTIPST 607
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
7455-7938 7.93e-19

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 95.32  E-value: 7.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7455 QAERMPEKAAVVFE------NTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDP 7528
Cdd:cd05966    62 HLKERGDKVAIIWEgdepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7529 EYPEDRIRYMLEDSGAQVLLT-----------------QRHLQECVSFDgKVIAA-----------------DDEQAYGE 7574
Cdd:cd05966   142 GFSAESLADRINDAQCKLVITadggyrggkviplkeivDEALEKCPSVE-KVLVVkrtggevpmtegrdlwwHDLMAKQS 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7575 DGSNLEPVvGPNHLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMFAETLRITEEDRV--------------VQFASLSFD 7639
Cdd:cd05966   221 PECEPEWM-DSEDPLFILYTSGSTGKPKGVVHTTGGyLLYAATTFKYVFDYHPDDIYwctadigwitghsyIVYGPLANG 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7640 ASCweifkALFFGATLYiPakdtilDYPLFESYMNENGITAAILPPTyAIYL-------SPDR--LPSLKKLITGGSAAS 7710
Cdd:cd05966   300 ATT-----VMFEGTPTY-P------DPGRYWDIVEKHKVTIFYTAPT-AIRAlmkfgdeWVKKhdLSSLRVLGSVGEPIN 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7711 VEfVQQWkdkvrYFNAYGPTEASIVTSVWAASPDGLDLRSVPI---------GRPIANHQIFIVDSQNHMLPVGVAGELC 7781
Cdd:cd05966   367 PE-AWMW-----YYEVIGKERCPIVDTWWQTETGGIMITPLPGatplkpgsaTRPFFGIEPAILDEEGNEVEGEVEGYLV 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7782 ISGA--GLARGYLNRPEltaeKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIAS 7859
Cdd:cd05966   441 IKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPA 516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7860 VQETIVIARGDANGQQQLCAYFV------ADRELtVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPA-PE 7932
Cdd:cd05966   517 VAEAAVVGRPHDIKGEAIYAFVTlkdgeePSDEL-RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKiAA 595

                  ....*.
gi 386647928 7933 GSMQTG 7938
Cdd:cd05966   596 GEEELG 601
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
7471-7914 1.03e-18

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 93.57  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7471 QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDpeypedrirYMLEdsgAQVLltq 7550
Cdd:cd05940     3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN---------YNLR---GESL--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7551 RHLQECVSfdGKVIAADdeqaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRV 7630
Cdd:cd05940    68 AHCLNVSS--AKHLVVD--------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7631 VQFASLSFDAS---CWEifKALFFGATLYIPAKDTILDyplFESYMNENGITAAILPPTYAIYL--SP----DRLPSLKK 7701
Cdd:cd05940   126 YTCLPLYHSTAlivGWS--ACLASGATLVIRKKFSASN---FWDDIRKYQATIFQYIGELCRYLlnQPpkptERKHKVRM 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7702 LITGGSAASV--EFVQQWKD-KVRYFnaYGPTEASIvTSVWAASPDGLDLRSVPIGRPIANHQIFIVDSQNHML------ 7772
Cdd:cd05940   201 IFGNGLRPDIweEFKERFGVpRIAEF--YAATEGNS-GFINFFGKPGAIGRNPSLLRKVAPLALVKYDLESGEPirdaeg 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7773 -----PVGVAGELC--ISGAGLARGYLNrPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRI 7845
Cdd:cd05940   278 rcikvPRGEPGLLIsrINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENV 356
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7846 ELGEIEEQLLKIASVQETIV--IARGDANGQQQLCAYFV-ADRELTVSELRGTLSQELPGYMIPsYFVQLEQ 7914
Cdd:cd05940   357 STTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLqPNEEFDLSALAAHLEKNLPGYARP-LFLRLQP 427
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
2367-2828 1.03e-18

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 94.46  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2367 EGQQLTYRELNERANRLARTLQ-ALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQV 2445
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2446 LLAQRRLQERV------------------SFAGTVVTVDDEQAYAGDGSNL---ESAVGP------NDLAYIIYTSGTTG 2498
Cdd:PRK05620  115 IVADPRLAEQLgeilkecpcvravvfigpSDADSAAAHMPEGIKVYSYEALldgRSTVYDwpeldeTTAAAICYSTGTTG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2499 KPKGVMVEHhglcslKQMFANTLQINAQDRVVQFASLSFdASCWEVFQTLFF---------GATLYIPTKEtiLDYQWFE 2569
Cdd:PRK05620  195 APKGVVYSH------RSLYLQSLSLRTTDSLAVTHGESF-LCCVPIYHVLSWgvplaafmsGTPLVFPGPD--LSAPTLA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2570 RYMSDNGITTATLPPTYAVYL------NPDHMPDFKRLIAAGSASSLELLQQWKDK--VKYFNAYGPTEDSICTTIWTP- 2640
Cdd:PRK05620  266 KIIATAMPRVAHGVPTLWIQLmvhylkNPPERMSLQEIYVGGSAVPPILIKAWEERygVDVVHVWGMTETSPVGTVARPp 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2641 -----STED---ISQLKsVPIGgpiVNHRIyIVDAHYQPVPVGVAGELCIAGVGLARGYLNRP----DLTAEKFVDNPFE 2708
Cdd:PRK05620  346 sgvsgEARWayrVSQGR-FPAS---LEYRI-VNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegGGAASTFRGEDVE 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2709 PGERMY------RTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAH-DDASGQKQLCAYF 2781
Cdd:PRK05620  421 DANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYpDDKWGERPLAVTV 500
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928 2782 VADRT----MTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK05620  501 LAPGIeptrETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PLN02246 PLN02246
4-coumarate--CoA ligase
5948-6422 1.07e-18

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 94.28  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5948 IPDHLAVT---FED----------------KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKA 6008
Cdd:PLN02246   19 IPNHLPLHdycFERlsefsdrpclidgatgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6009 GGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQghlldrASFADKLVNLND-------------DGAYH------EDGSNLE 6069
Cdd:PLN02246   99 GAVTTTANPFYTPAEIAKQAKASGAKLIITQ------SCYVDKLKGLAEddgvtvvtiddppEGCLHfseltqADENELP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6070 PVN-GPEHLTYVIYTSGTTGRPKGVMVEHRNVVRLV------KNTN-YVELNEQT-------HI----------LQTGAV 6124
Cdd:PLN02246  173 EVEiSPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVaqqvdgENPNlYFHSDDVIlcvlpmfHIyslnsvllcgLRVGAA 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6125 VFDASTFEIwGALLnggrlyvvrnetildavslkNAIQQYGINTMWLTAPLynqlsqqdsgMFAGLKTLIVGGDVLSvpH 6204
Cdd:PLN02246  253 ILIMPKFEI-GALL--------------------ELIQRHKVTIAPFVPPI----------VLAIAKSPVVEKYDLS--S 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6205 INRVLREHAGLS---------------IVNGYGPTE-------NTTFStthtivgeqKEAVPI-----GKPINNSTAYIV 6257
Cdd:PLN02246  300 IRMVLSGAAPLGkeledafraklpnavLGQGYGMTEagpvlamCLAFA---------KEPFPVksgscGTVVRNAELKIV 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6258 DSKLSL-LPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYR 6336
Cdd:PLN02246  371 DPETGAsLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWL------HTGDIGYIDDDDELFIVDRLKELIKYKGFQ 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6337 IELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFV--AERELTIGELRAALSQELPNY-MIPS-HFVplERMPLTPN 6412
Cdd:PLN02246  445 VAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVrsNGSEITEDEIKQFVAKQVVFYkRIHKvFFV--DSIPKAPS 522
                         570
                  ....*....|
gi 386647928 6413 GKIDRRALPA 6422
Cdd:PLN02246  523 GKILRKDLRA 532
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
283-741 1.15e-18

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 93.19  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  283 DRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLL 362
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  363 SqghlqervsfsgtwirldDEEAYhedgsnlesvngpehltyvIYTSGTTGKPKGNLTTHRNIIRVVKNTNYIDVT-GQD 441
Cdd:cd05940    81 V------------------DAALY-------------------IYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAlPSD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  442 KL-LQLSSYSFDGSTFDIFGALLNGAKLVLVPKetvldvaklagliekqqisvmFITTAFFnvlvdmnPDClRHARAILF 520
Cdd:cd05940   124 VLyTCLPLYHSTALIVGWSACLASGATLVIRKK---------------------FSASNFW-------DDI-RKYQATIF 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  521 G--GERVSV-----------SH-VRKALGH-------------LGPGKIKHVYGPTESTVFATSYDvheVEEGAV--SIP 571
Cdd:cd05940   175 QyiGELCRYllnqppkpterKHkVRMIFGNglrpdiweefkerFGVPRIAEFYAATEGNSGFINFF---GKPGAIgrNPS 251
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  572 IGGPISNTAIYIVNAQNKlQPI------------GVAGELCVAGDGLAR--GYLNrPDLTAEKFADNPFAPGERMYRTGD 637
Cdd:cd05940   252 LLRKVAPLALVKYDLESG-EPIrdaegrcikvprGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVFKKGDAWFNTGD 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  638 LARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATV--VVRESANGEKQLCAYYVADrslPANEVRSTL 715
Cdd:cd05940   330 LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLQP---NEEFDLSAL 406
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928  716 S----QELPAYMLPsYFVQL-EQMPLTTNGK 741
Cdd:cd05940   407 AahleKNLPGYARP-LFLRLqPEMEITGTFK 436
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
5932-6332 1.17e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 94.73  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5932 PSDKTIHQLFEEQAERIPDHLAV---TFEDKQ---LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAI 6005
Cdd:PRK12582   46 PYPRSIPHLLAKWAAEAPDRPWLaqrEPGHGQwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6006 LKAGGAYVPIDPDY---PED--RIRYMLEDSGAKLLLVQghllDRASFADKLVNLNDDGA--YHEDGSN----------- 6067
Cdd:PRK12582  126 MQAGVPAAPVSPAYslmSHDhaKLKHLFDLVKPRVVFAQ----SGAPFARALAALDLLDVtvVHVTGPGegiasiafadl 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6068 -LEPVN----------GPEHLTYVIYTSGTTGRPKGVMVEHR----------NVVRLVKNTN---YVELNEQTHILqTGA 6123
Cdd:PRK12582  202 aATPPTaavaaaiaaiTPDTVAKYLFTSGSTGMPKAVINTQRmmcaniamqeQLRPREPDPPppvSLDWMPWNHTM-GGN 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6124 VVFDastfeiwGALLNGGRLYV-------------VRNetiLDAVSlknaiqqygiNTMWLTAPL-YNQLS---QQDSGM 6186
Cdd:PRK12582  281 ANFN-------GLLWGGGTLYIddgkplpgmfeetIRN---LREIS----------PTVYGNVPAgYAMLAeamEKDDAL 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6187 ----FAGLKTLIVGGDVLSVPHINRvLREHA----GLSIV--NGYGPTENT-TFSTTHTI---VGEqkeavpIGKPINNS 6252
Cdd:PRK12582  341 rrsfFKNLRLMAYGGATLSDDLYER-MQALAvrttGHRIPfyTGYGATETApTTTGTHWDterVGL------IGLPLPGV 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6253 TayivdskLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGDLARWL----PDGTLEYKGRIDE 6328
Cdd:PRK12582  414 E-------LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGRVAE 480

                  ....
gi 386647928 6329 QVKI 6332
Cdd:PRK12582  481 DFKL 484
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
7456-7928 1.21e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 93.99  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENT--QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPED 7533
Cdd:PRK13391    7 AQTTPDKPAVIMASTgeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7534 RIRYMLEDSGAQVLLTQR--------------HLQECVSFDGkviaaDDE----QAYGEDGSNLEPVVGPNHL--AYVIY 7593
Cdd:PRK13391   87 EAAYIVDDSGARALITSAakldvarallkqcpGVRHRLVLDG-----DGElegfVGYAEAVAGLPATPIADESlgTDMLY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7594 TSGTTGKPKGVMVE--HHGL---CSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAKdtiLDYPL 7668
Cdd:PRK13391  162 SSGTTGRPKGIKRPlpEQPPdtpLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEH---FDAEQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7669 FESYMNENGITAAILPPTY---------AIYLSPDrLPSLKKLITGGSAASVEFVQQ----WKDKVRYFnaYGPTEASIV 7735
Cdd:PRK13391  239 YLALIEEYGVTHTQLVPTMfsrmlklpeEVRDKYD-LSSLEVAIHAAAPCPPQVKEQmidwWGPIIHEY--YAATEGLGF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7736 TSVwaASPDGLDLRSVpIGRPIANhQIFIVDSQNHMLPVGVAGELCISGaGLARGYLNRPELTAEKFVDNPflageRMYR 7815
Cdd:PRK13391  316 TAC--DSEEWLAHPGT-VGRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----TWST 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7816 TGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDAN-GQQ-----QLCAYFVADRELTv 7889
Cdd:PRK13391  386 VGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDlGEEvkavvQPVDGVDPGPALA- 464
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 386647928 7890 SELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK13391  465 AELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1901-2253 1.34e-18

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 92.76  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1901 YPVSSAQKRLYILHQLEGAEQSYNMTGELVLEGILDRGKLEEAFRQLIARHETLRTGFELVN-GEPVQRVYKEVN--FAV 1977
Cdd:cd19547     2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAppWAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1978 EHYRTSE----AEAGEVVRGFVRT--FDLAKPPLLRVGLVELAEDLHILLLDMHHIVSDGMSTDVLTEEFGRLYngESLA 2051
Cdd:cd19547    82 LDWSGEDpdrrAELLERLLADDRAagLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVY--EELA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2052 TLR-------IQYKDYAVWQQSeeQLERVKRQEAYWLDMFRgEL---PVLEMPTDyprpavRRFEGSTLSFRLDAGLNEA 2121
Cdd:cd19547   160 HGRepqlspcRPYRDYVRWIRA--RTAQSEESERFWREYLR-DLtpsPFSTAPAD------REGEFDTVVHEFPEQLTRL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2122 LKRVAAESGATLYMVLLAAYNVMLQKYTGQEDIVIGTPIAGRTH--GDLQPLIGMFVNTLAIRNYPAGGKTFRSFLEEVK 2199
Cdd:cd19547   231 VNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIH 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2200 ETTLGAYEHQTYPFEELVEKLQVPRdLSRNPIFDAMFVLQNTENEELQLDGLKL 2253
Cdd:cd19547   311 RDLATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSI 363
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
3880-4281 1.40e-18

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 93.82  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGgayIPIDPEYP---EDRIRYMLEDSGAQALL 3956
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3957 TqrhlrervsfagtfvavddeqayhaDGSnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCS--LKLMFANTLQMTE 4034
Cdd:cd17639    83 T-------------------------DGK-------PDDLACIMYTSGSTGNPKGVMLTHGNLVAgiAGLGDRVPELLGP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4035 QDRVVQFASLSfdascwEIFK------ALFFGATLYIPTSTTILDyplfESYMNENGiTATILPPTY------------- 4095
Cdd:cd17639   131 DDRYLAYLPLA------HIFElaaenvCLYRGGTIGYGSPRTLTD----KSKRGCKG-DLTEFKPTLmvgvpaiwdtirk 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4096 --AAYLNPdrMPSLKKLI--------------------------------TGG------------SAASVEFVQQWKDKV 4129
Cdd:cd17639   200 gvLAKLNP--MGGLKRTLfwtayqsklkalkegpgtplldelvfkkvraaLGGrlrymlsggaplSADTQEFLNIVLCPV 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4130 LyfNAYGPTE---ASIVTSIWDEASDSlgdrksvpIGRPLANHRIYVVD----------SHNRmlpvgvaGELCISGVGL 4196
Cdd:cd17639   278 I--QGYGLTEtcaGGTVQDPGDLETGR--------VGPPLPCCEIKLVDweeggystdkPPPR-------GEILIRGPNV 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4197 ARGYLNRPELTAEKFVdnpfepGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIR-GYRIELGEVETQLAKIDAVQEAIVL 4275
Cdd:cd17639   341 FKGYYKNPEKTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVY 414

                  ....*.
gi 386647928 4276 AREDAN 4281
Cdd:cd17639   415 ADPDKS 420
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1634-1883 1.44e-18

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 90.58  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1634 AHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFV------EGERLYRTGDLARWMPDGNVDFIGRIDNQAKI 1707
Cdd:COG3433    30 LLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPvpypaqPGRQADDLRLLLRRGLGPGGGLERLVQQVVIR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1708 RGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTAN 1787
Cdd:COG3433   110 AERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLAL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1788 GKIDRKALPAPDASMQTGMEYVAPRTPQ---EAKLASIWQEVLGL--EKVGVKDNFFELGGHSLRATLLVGKVhKEMNVE 1862
Cdd:COG3433   190 KVVARAAPALAAAEALLAAASPAPALETaltEEELRADVAELLGVdpEEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLD 268
                         250       260
                  ....*....|....*....|.
gi 386647928 1863 LPLRDVFRCSTVEEMAQAIAR 1883
Cdd:COG3433   269 VSFADLAEHPTLAAWWALLAA 289
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
286-679 1.62e-18

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 93.82  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGV--QADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLS 363
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  364 QGHLqERVSFsgtwirlddEEAYHEDGSNLESVN--GPEHLTYVIYTSGTTGKPKGNLTTHRNII-------RVVKNTNY 434
Cdd:cd05927    86 DAGV-KVYSL---------EEFEKLGKKNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVsnvagvfKILEILNK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  435 IDVTGQ-----------DKLLQLSSYSFdGSTFDIFGA----LLNGAK------LVLVP--------------------K 473
Cdd:cd05927   156 INPTDVyisylplahifERVVEALFLYH-GAKIGFYSGdirlLLDDIKalkptvFPGVPrvlnriydkifnkvqakgplK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  474 ETVLDVA---KLAGLiekqQISVMFITTaFFNVLVDmnpdclrHARAILFGGE-RVSVS-------HV----RKALG-HL 537
Cdd:cd05927   235 RKLFNFAlnyKLAEL----RSGVVRASP-FWDKLVF-------NKIKQALGGNvRLMLTgsaplspEVleflRVALGcPV 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  538 GPGkikhvYGPTESTVFATSYDVHEVEEGAVsipiGGPISNTAI---------YIVNAQNKlqpigvAGELCVAGDGLAR 608
Cdd:cd05927   303 LEG-----YGQTECTAGATLTLPGDTSVGHV----GGPLPCAEVklvdvpemnYDAKDPNP------RGEVCIRGPNVFS 367
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  609 GYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIeyvgRIDDQVK-IrgFRIELGEIEAhLLKLEAI 679
Cdd:cd05927   368 GYYKDPEKTAEALDEDGW------LHTGDIGEWLPNGTL----KIIDRKKnI--FKLSQGEYVA-PEKIENI 426
PRK07788 PRK07788
acyl-CoA synthetase; Validated
4889-5292 1.66e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 93.84  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4889 FHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLD 4968
Cdd:PRK07788   51 FAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4969 PDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAALCL-----DDEAAYAEDAS--NVANVNEPHDL-------A 5034
Cdd:PRK07788  131 TGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWggnpdDDEPSGSTDETldDLIAGSSTAPLpkppkpgG 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5035 YVIYTSGTTGRPKGVMIEHRSLVNTAAGYrreyrLDQFPVRLLQLASFSFDVF------VGDIARTLynGGTMVIcpkDD 5108
Cdd:PRK07788  211 IVILTSGTTGTPKGAPRPEPSPLAPLAGL-----LSRVPFRAGETTLLPAPMFhatgwaHLTLAMAL--GSTVVL---RR 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5109 RIDPARLHYWISEEKITIFESTPALIIPFMDyVAEHGL---DMSSMVLLITSSDSCSVTDYRVLQERFGSqfRIINAYGV 5185
Cdd:PRK07788  281 RFDPEATLEDIAKHKATALVVVPVMLSRILD-LGPEVLakyDTSSLKIIFVSGSALSPELATRALEAFGP--VLYNLYGS 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5186 TEAAIDSSLYDEPLAKLPE-AGNVPIGkaalnAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPelteekfvDSPF 5264
Cdd:PRK07788  358 TEVAFATIATPEDLAEAPGtVGRPPKG-----VTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR--------DKQI 424
                         410       420
                  ....*....|....*....|....*...
gi 386647928 5265 VEGerLYRTGDLARWMPDGNVDFIGRID 5292
Cdd:PRK07788  425 IDG--LLSSGDVGYFDEDGLLFVDGRDD 450
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
6080-6417 1.66e-18

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 91.18  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6080 VIYTSGTTGRPKGVMVEHRNVVrlvknTNYVELNEQTHILQTGAVVFDASTFEIWG-----ALLNGGRLYVVRNEtiLDA 6154
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLI-----AANLQLIHAMGLTEADVYLNMLPLFHIAGlnlalATFHAGGANVVMEK--FDP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6155 VSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTL-IVGGdvLSVPHINRVLREHAGLSIVNGYGPTENTTFSTTH 6233
Cdd:cd17637    78 AEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLrHVLG--LDAPETIQRFEETTGATFWSLYGQTETSGLVTLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6234 TIVGEQKEAvpiGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESsflpgerCYRTGDLAR 6313
Cdd:cd17637   156 PYRERPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHTGDLGR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6314 WLPDGTLEYKGRIDEQ--VKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQ--KQLCAyFVAERELTIGELRAAL 6388
Cdd:cd17637   226 FDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIgVPDPKWGEgiKAVCV-LKPGATLTADELIEFV 304
                         330       340
                  ....*....|....*....|....*....
gi 386647928 6389 SQELPNYMIPSHFVPLERMPLTPNGKIDR 6417
Cdd:cd17637   305 GSRIARYKKPRYVVFVEALPKTADGSIDR 333
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
6074-6420 1.75e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 91.39  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6074 PEHLTYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVELNEQTHILQTGAVVF--DASTFEIWGALLNGGRLYVV----- 6146
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFhvNGSVVTLLTPLASGAHVVLAgpagy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6147 RNETILDavSLKNAIQQYGINTMWLTAPLYNQLSQQ-DSGMFAGLKTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTE 6225
Cdd:cd05944    81 RNPGLFD--NFWKLVERYRITSLSTVPTVYAALLQVpVNADISSLRFAMSGAAPLPVELRAR-FEDATGLPVVEGYGLTE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6226 NTTFSTTHTIVGEQKEAvPIGKPINNSTAYIVDSKLS---LLPVGV--WGELIVGGDGVARGYLNRpELTAEKFVESSFL 6300
Cdd:cd05944   158 ATCLVAVNPPDGPKRPG-SVGLRLPYARVRIKVLDGVgrlLRDCAPdeVGEICVAGPGVFGGYLYT-EGNKNAFVADGWL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6301 pgercyRTGDLARWLPDGTLEYKGRIDEQVkIR-GYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAY--FVAER 6377
Cdd:cd05944   236 ------NTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYvqLKPGA 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 386647928 6378 ELTIGELRAALSQELPNY-MIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05944   309 VVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK07867 PRK07867
acyl-CoA synthetase; Validated
7464-7930 2.01e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 93.21  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7464 AVVFENTQLTYRELNERANRLARTLRAEgVQADQP--VGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLED 7541
Cdd:PRK07867   21 GLYFEDSFTSWREHIRGSAARAAALRAR-LDPTRPphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAH 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7542 SGAQVLLT---QRHLQECVSFDGKVIAADDEQAYGEDGSNLEP-----VVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCS 7613
Cdd:PRK07867  100 ADCQLVLTesaHAELLDGLDPGVRVINVDSPAWADELAAHRDAeppfrVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7614 LKLMFAETLRITEEDrvVQFASLSFDAS-----CWEIfkALFFGATLYIPAK-------DTILDYPLfeSYMNENG---- 7677
Cdd:PRK07867  180 AGVMLAQRFGLGPDD--VCYVSMPLFHSnavmaGWAV--ALAAGASIALRRKfsasgflPDVRRYGA--TYANYVGkpls 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7678 -ITAAilPPtyaiylSPDRLPSLKKLITGGSAASV---EFVQQWKdkVRYFNAYGPTEASIVTSVWAASPDGldlrsvPI 7753
Cdd:PRK07867  254 yVLAT--PE------RPDDADNPLRIVYGNEGAPGdiaRFARRFG--CVVVDGFGSTEGGVAITRTPDTPPG------AL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7754 GRPIANHQIFIVDSQNHmLPVGVA------------GELC-ISGAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLA 7820
Cdd:PRK07867  318 GPLPPGVAIVDPDTGTE-CPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7821 RWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVA--DRELTVSELRGTLSQ 7898
Cdd:PRK07867  390 YRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLapGAKFDPDAFAEFLAA 469
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 7899 --ELPGYMIPSYFVQLEQMPLTPNGKIDRNALPA 7930
Cdd:PRK07867  470 qpDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
3863-4337 2.04e-18

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 93.78  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3863 QALRNPDAVAVVFE------KSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDP 3936
Cdd:cd05966    62 HLKERGDKVAIIWEgdepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3937 EYPEDRIRYMLEDSGAQALLTQ--------------------------------RHLRERVSF-AGTFVAVDDEQAYHAD 3983
Cdd:cd05966   142 GFSAESLADRINDAQCKLVITAdggyrggkviplkeivdealekcpsvekvlvvKRTGGEVPMtEGRDLWWHDLMAKQSP 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3984 GSNLEPVvGPNHLAYVIYTSGTTGKPKGVMvehHGLCSLKLMFANTLQMTeqdrvvqfaslsFDASCWEIFkalFFGATL 4063
Cdd:cd05966   222 ECEPEWM-DSEDPLFILYTSGSTGKPKGVV---HTTGGYLLYAATTFKYV------------FDYHPDDIY---WCTADI 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4064 -YIPTSTTILDYPLFesymneNGITATILP--PTYAaylNPDRMpslkklitggsaasVEFVQQWKDKVLY--------F 4132
Cdd:cd05966   283 gWITGHSYIVYGPLA------NGATTVMFEgtPTYP---DPGRY--------------WDIVEKHKVTIFYtaptairaL 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4133 NAYG--PTEASIVTSI--------------WDEASDSLGDRKsVPI----------------------------GRPLAN 4168
Cdd:cd05966   340 MKFGdeWVKKHDLSSLrvlgsvgepinpeaWMWYYEVIGKER-CPIvdtwwqtetggimitplpgatplkpgsaTRPFFG 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4169 HRIYVVDSHNRMLPVGVAGELCISGV--GLARGYLNRPEltaeKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQ 4246
Cdd:cd05966   419 IEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDV 494
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4247 VKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV------AQRELtAAELRATMSQELPNYMIPSYFVQ 4320
Cdd:cd05966   495 INVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdgeePSDEL-RKELRKHVRKEIGPIATPDKIQF 573
                         570
                  ....*....|....*..
gi 386647928 4321 LAQMPLTPNGKIDRKAL 4337
Cdd:cd05966   574 VPGLPKTRSGKIMRRIL 590
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
2326-2828 2.09e-18

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 93.51  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2326 EQTQLHHVFNA--TAADYEADKTIHQLFEEQAERIPDHPAVV--FEGQQLTYRELNERANRLARTLQALGVKTDQPVGLM 2401
Cdd:PLN02330    7 KQEDNEHIFRSryPSVPVPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2402 LERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAY---------- 2471
Cdd:PLN02330   87 LPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEEKIegavnwkell 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2472 -----AGDGSNLESaVGPNDLAYIIYTSGTTGKPKGVMVEHH----GLCSlkQMFANTLQINAQdrVVQFASLSFdascW 2542
Cdd:PLN02330  167 eaadrAGDTSDNEE-ILQTDLCALPFSSGTTGISKGVMLTHRnlvaNLCS--SLFSVGPEMIGQ--VVTLGLIPF----F 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2543 EVFQ-TLFFGATLYIPTKETIL---DYQWFERYMSDNGITTATLPPTYAVYLNPDHMPD--------FKRLIAAGSASSL 2610
Cdd:PLN02330  238 HIYGiTGICCATLRNKGKVVVMsrfELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEefdlsklkLQAIMTAAAPLAP 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2611 ELLQQWKDK---VKYFNAYGPTEDS-ICTTIWTPST-EDISQLKSVpiGGPIVNHRIYIVDAHY-QPVPVGVAGELCIAG 2684
Cdd:PLN02330  318 ELLTAFEAKfpgVQVQEAYGLTEHScITLTHGDPEKgHGIAKKNSV--GFILPNLEVKFIDPDTgRSLPKNTPGELCVRS 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2685 VGLARGYLNRPDLTAeKFVDNpfepgERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAI 2764
Cdd:PLN02330  396 QCVMQGYYNNKEETD-RTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAA 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 2765 VIAHDDASGQKQLCAYFVADRTMTVGE--LRGELSGELPGY--MIPAHFVqlERMPLTPNGKIDRKAL 2828
Cdd:PLN02330  470 VVPLPDEEAGEIPAACVVINPKAKESEedILNFVAANVAHYkkVRVVQFV--DSIPKSLSGKIMRRLL 535
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
3860-4332 2.41e-18

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 93.87  E-value: 2.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3860 FEEQALR---NPDAVAVVF----EKSQLTYGELNERANRLARTLRDAGVRP-DQLVGLMvERSLEMVVGIMAIMKAGGAY 3931
Cdd:cd05943    72 YAENLLRhadADDPAAIYAaedgERTEVTWAELRRRVARLAAALRALGVKPgDRVAGYL-PNIPEAVVAMLATASIGAIW 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3932 IPIDPEYPE----DRI-----RYMLEDSGAQ-------ALLTQRHLRERVSFAGTFVAVDDEQAYH-------------- 3981
Cdd:cd05943   151 SSCSPDFGVpgvlDRFgqiepKVLFAVDAYTyngkrhdVREKVAELVKGLPSLLAVVVVPYTVAAGqpdlskiakaltle 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3982 ---ADGSNLEPV---VGPNHLAYVIYTSGTTGKPK-------GVMVEH---HGLCSlklmfantlQMTEQDRVVQFASLS 4045
Cdd:cd05943   231 dflATGAAGELEfepLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHlkeHILHC---------DLRPGDRLFYYTTCG 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4046 FDASCWEIfKALFFGAT--LY-----IPTSTTILDYplfesyMNENGIT-----ATILPPTYAAYLNPDRMPSLKKLITG 4113
Cdd:cd05943   302 WMMWNWLV-SGLAVGATivLYdgspfYPDTNALWDL------ADEEGITvfgtsAKYLDALEKAGLKPAETHDLSSLRTI 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4114 GSAAS------VEFV-QQWKDKVLYFNAYGPTeasivtsiwDEASDSLGDRKSVPIGR-----PLANHRIYVVDSHNRML 4181
Cdd:cd05943   375 LSTGSplkpesFDYVyDHIKPDVLLASISGGT---------DIISCFVGGNPLLPVYRgeiqcRGLGMAVEAFDEEGKPV 445
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4182 pVGVAGEL-CISGV-GLARGYLNRPEltAEKFVDNPFE--PGerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELG 4257
Cdd:cd05943   446 -WGEKGELvCTKPFpSMPVGFWNDPD--GSRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTA 520
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4258 EVETQLAKIDAVQEAIVLAREDANGQQQLVaYFVAQR---ELT---AAELRATMSQELPNYMIPSYFVQLAQMPLTPNGK 4331
Cdd:cd05943   521 EIYRVVEKIPEVEDSLVVGQEWKDGDERVI-LFVKLRegvELDdelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599

                  .
gi 386647928 4332 I 4332
Cdd:cd05943   600 K 600
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
7585-7928 2.57e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 91.00  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7585 PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDrvVQFASLSF---DASCWEIFKALFFGATLYIPAKD 7661
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDD--VLLCGLPLfhvNGSVVTLLTPLASGAHVVLAGPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7662 TILDYPLFESY---MNENGITAAILPPT-YAIYLS-PDR--LPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEA 7732
Cdd:cd05944    79 GYRNPGLFDNFwklVERYRITSLSTVPTvYAALLQvPVNadISSLRFAMSGAAPLPVELRARFEDAtgLPVVEGYGLTEA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7733 SIVTSVwaASPDG-LDLRSVPIGRPIANHQIFIVDSQNHML---PVGVAGELCISGAGLARGYLNRpELTAEKFVDNPFL 7808
Cdd:cd05944   159 TCLVAV--NPPDGpKRPGSVGLRLPYARVRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7809 agermyRTGDLARWLPDGNIEYLGRIDHQVkIR-GYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAY--FVADR 7885
Cdd:cd05944   236 ------NTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYvqLKPGA 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 386647928 7886 ELTVSELRGTLSQELPGY-MIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05944   309 VVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
286-707 2.57e-18

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 93.05  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGgayVPIDPEYP---EERIRYMLEDSGTQVLL 362
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  363 SqghlqervsfsgtwirlddeeayhedgsnlesVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVK--NTNYIDVTG- 439
Cdd:cd17639    83 T--------------------------------DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAglGDRVPELLGp 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  440 QDKLL------------------------------QLSSYSFDGSTFDIfgALLNGAKLVLVP------KETVLdvAKLA 483
Cdd:cd17639   131 DDRYLaylplahifelaaenvclyrggtigygsprTLTDKSKRGCKGDL--TEFKPTLMVGVPaiwdtiRKGVL--AKLN 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  484 --GLIEKQqisvMF--------------ITTAFFNVLVDMNPdclRHA-----RAILFGGERVSVSHVR---KALGHLGP 539
Cdd:cd17639   207 pmGGLKRT----LFwtayqsklkalkegPGTPLLDELVFKKV---RAAlggrlRYMLSGGAPLSADTQEflnIVLCPVIQ 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  540 GkikhvYGPTESTVFATSYDVHEVEEGAVSIPIGgpisntAIYIvnaqnKLQPIGVA----------GELCVAGDGLARG 609
Cdd:cd17639   280 G-----YGLTETCAGGTVQDPGDLETGRVGPPLP------CCEI-----KLVDWEEGgystdkppprGEILIRGPNVFKG 343
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  610 YLNRPDLTAEKFAdnpfapGERMYRTGDLARWLPDGTIEYVGRIDDQVKirgfrIELGEIEAhLLKLEAIEKATVVVres 689
Cdd:cd17639   344 YYKNPEKTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVK-----LQNGEYIA-LEKLESIYRSNPLV--- 408
                         490
                  ....*....|....*...
gi 386647928  690 angeKQLCAYYVADRSLP 707
Cdd:cd17639   409 ----NNICVYADPDKSYP 422
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
404-745 2.86e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 90.90  E-value: 2.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  404 YVIYTSGTTGKPKGNLTTHRNIIRVVKNTNYID--VTGQDKLLQLSSYSFDGSTFDI-------------FGALLNGAKL 468
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGtgEFTPSEDAHKAAAAAAGTVMFPapplmhgtgswtaFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  469 VLVPKEtvLDVAKLAGLIEKQQISVMFIT-TAFFNVLVD----MNPDCLRHARAILFGGERVSVSHVRKALGHLGPGKIK 543
Cdd:cd05924    87 VLPDDR--FDPEEVWRTIEKHKVTSMTIVgDAMARPLIDalrdAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  544 HVYGPTESTVFATSYDVHEVEEGAVSIPIGGpisnTAIYIVNAQNKLQPiGVAGELCVAGDGL-ARGYLNRPDLTAEKFa 622
Cdd:cd05924   165 DAFGSSETGFTGSGHSAGSGPETGPFTRANP----DTVVLDDDGRVVPP-GSGGVGWIARRGHiPLGYYGDEAKTAETF- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  623 dnPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVA 702
Cdd:cd05924   239 --PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 386647928  703 DR--SLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRR 745
Cdd:cd05924   317 REgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
7472-7834 2.87e-18

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 93.40  E-value: 2.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY---PED--RIRYMLE------ 7540
Cdd:PRK08180   70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYslvSQDfgKLRHVLElltpgl 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7541 ---DSGAqvlLTQRHLQECVSFDGKVIAADD--------------EQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKG 7603
Cdd:PRK08180  150 vfaDDGA---AFARALAAVVPADVEVVAVRGavpgraatpfaallATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKA 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7604 VMVEHHGLCSLKLMFAETLRITEEDRVVQFASL----SFDAScwEIFK-ALFFGATLYI------PAkdtildypLFESy 7672
Cdd:PRK08180  227 VINTHRMLCANQQMLAQTFPFLAEEPPVLVDWLpwnhTFGGN--HNLGiVLYNGGTLYIddgkptPG--------GFDE- 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 mnengiTAAIL---PPTyaIYLSPDR-----LPSLK-------------KLITGGSAASVEFVqqWKD-----------K 7720
Cdd:PRK08180  296 ------TLRNLreiSPT--VYFNVPKgwemlVPALErdaalrrrffsrlKLLFYAGAALSQDV--WDRldrvaeatcgeR 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7721 VRYFNAYGPTEAS-IVTSV-WAASpdgldlRSVPIGRPIANHQIFIVdsqnhmlPVGVAGELCISGAGLARGYLNRPELT 7798
Cdd:PRK08180  366 IRMMTGLGMTETApSATFTtGPLS------RAGNIGLPAPGCEVKLV-------PVGGKLEVRVKGPNVTPGYWRAPELT 432
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 386647928 7799 AEKFVDNPFlagermYRTGDLARWL----PDGNIEYLGRI 7834
Cdd:PRK08180  433 AEAFDEEGY------YRSGDAVRFVdpadPERGLMFDGRI 466
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
6080-6420 3.18e-18

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 90.49  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6080 VIYTSGTTGRPKGVMVEHRNVV--------RLVKNTNYVELNEQTHI--LQ---------TGAVVFDAST-FEIwGAL-- 6137
Cdd:PRK07824   40 VVATSGTTGTPKGAMLTAAALTasadathdRLGGPGQWLLALPAHHIagLQvlvrsviagSEPVELDVSAgFDP-TALpr 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6138 ----LNGGRLYvvrneTILDAVSLKNAIQqygintmwltaplynqlSQQDSGMFAGLKTLIVGGDVLSVPhinrVLR--E 6211
Cdd:PRK07824  119 avaeLGGGRRY-----TSLVPMQLAKALD-----------------DPAATAALAELDAVLVGGGPAPAP----VLDaaA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6212 HAGLSIVNGYGPTEnttfstthTIVGeqkeAVPIGKPINNSTAYIVDSKLSLlpvgvwgelivGGDGVARGYLNRPELTA 6291
Cdd:PRK07824  173 AAGINVVRTYGMSE--------TSGG----CVYDGVPLDGVRVRVEDGRIAL-----------GGPTLAKGYRNPVDPDP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6292 ekFVESSFlpgercYRTGDLARwLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDES-GQKQLC 6370
Cdd:PRK07824  230 --FAEPGW------FRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVA 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928 6371 AYFVAEREL-TIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK07824  301 AVVGDGGPApTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
5224-5473 3.22e-18

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 89.42  E-value: 3.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5224 AHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFV------EGERLYRTGDLARWMPDGNVDFIGRIDNQAKI 5297
Cdd:COG3433    30 LLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPvpypaqPGRQADDLRLLLRRGLGPGGGLERLVQQVVIR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5298 RGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTAN 5377
Cdd:COG3433   110 AERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLAL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5378 GKIDRKALPAPDASMQTGMEYVAPRTPQ---EAKLVSIWQEVLGL--EKVGVKDNFFELGGHSLRATLLVGKVhKEMNVE 5452
Cdd:COG3433   190 KVVARAAPALAAAEALLAAASPAPALETaltEEELRADVAELLGVdpEEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLD 268
                         250       260
                  ....*....|....*....|.
gi 386647928 5453 LPLRDVFRCSTVEEMAQAIAR 5473
Cdd:COG3433   269 VSFADLAEHPTLAAWWALLAA 289
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
4897-5382 4.00e-18

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 92.55  E-value: 4.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4897 AECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDpdYpsdri 4976
Cdd:PLN02860   17 ATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN--Y----- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4977 QFMLEDSAASVLLTQTHL---QERAQQWGQTLQAALC--------LDDEAA-YAEDASNVANVNE--------------- 5029
Cdd:PLN02860   90 RWSFEEAKSAMLLVRPVMlvtDETCSSWYEELQNDRLpslmwqvfLESPSSsVFIFLNSFLTTEMlkqralgtteldyaw 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 -PHDLAYVIYTSGTTGRPKGVMIEHRSLVN------TAAGYRREyrlDQFpvrlLQLASFsfdVFVGDIARTLYN---GG 5099
Cdd:PLN02860  170 aPDDAVLICFTSGTTGRPKGVTISHSALIVqslakiAIVGYGED---DVY----LHTAPL---CHIGGLSSALAMlmvGA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5100 TMVICPKddrIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMS--SMVLLITSSDSCSVtdyRVLQE--RFGS 5175
Cdd:PLN02860  240 CHVLLPK---FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVfpSVRKILNGGGSLSS---RLLPDakKLFP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5176 QFRIINAYGVTEAAidSSL----YDEPLAKLPeagnvpigKAALNAKFYIVDAHLNPvPVGV-LG------ELCIGGIGV 5244
Cdd:PLN02860  314 NAKLFSAYGMTEAC--SSLtfmtLHDPTLESP--------KQTLQTVNQTKSSSVHQ-PQGVcVGkpaphvELKIGLDES 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5245 AR--GYLNRPELTEEKFVDSPFVEGERLYR-----TGDLArWMPD-GNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEG 5316
Cdd:PLN02860  383 SRvgRILTRGPHVMLGYWGQNSETASVLSNdgwldTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPG 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5317 VREAVVVVREDAK-GQKVL-CA------------HFTAESELKLSE--LRSSLS-QELPGYMIPSYFVQLE-QLPLTANG 5378
Cdd:PLN02860  462 VASVVVVGVPDSRlTEMVVaCVrlrdgwiwsdneKENAKKNLTLSSetLRHHCReKNLSRFKIPKLFVQWRkPFPLTTTG 541

                  ....
gi 386647928 5379 KIDR 5382
Cdd:PLN02860  542 KIRR 545
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
6522-6837 4.32e-18

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 91.28  E-value: 4.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6522 GLTPIQR--WFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGYAAWnraIGEGELYSLE 6599
Cdd:cd19533     3 PLTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQW---IDPYTPVPIR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6600 VADFRDVKSAEQAVEA-KANEIQSSIDLEVGPLFKAGLFQCADGDHLLLV-IHHGVVDGVSWRILLEDVALGYEQAAKGE 6677
Cdd:cd19533    80 HIDLSGDPDPEGAAQQwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFALFGQRVAEIYTALLKGR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6678 EVRlPAKTDSFRTWSEQLAAYAQSPAMENERAYW-EQIAQTAVAPLPKDKQSDRSLqqDSESITIQWSRKETEQLLK--K 6754
Cdd:cd19533   160 PAP-PAPFGSFLDLVEEEQAYRQSERFERDRAFWtEQFEDLPEPVSLARRAPGRSL--AFLRRTAELPPELTRTLLEaaE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6755 VHRAYNTEMndiLLTALGMAVQKWSGLDRLLVNLEGHGResimTDIDITRTVGWFTSKYPVLLQMEPGRSLSTRIKKVKE 6834
Cdd:cd19533   237 AHGASWPSF---FIALVAAYLHRLTGANDVVLGVPVMGR----LGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309

                  ...
gi 386647928 6835 DLR 6837
Cdd:cd19533   310 ELR 312
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
4886-5385 4.55e-18

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 92.62  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4886 NEAFHALfEKQAECTPEAAAVVYEND------RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWK 4959
Cdd:cd05966    53 NISYNCL-DRHLKERGDKVAIIWEGDepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACAR 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4960 AG-------GAYvplDPDYPSDRIqfmlEDSAASVLLT---------QTHLQERAQQwgqTLQAA--------------- 5008
Cdd:cd05966   132 IGavhsvvfAGF---SAESLADRI----NDAQCKLVITadggyrggkVIPLKEIVDE---ALEKCpsvekvlvvkrtgge 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5009 --------LCLDDEAAYAEDASNVANVNEPHDLaYVIYTSGTTGRPKGVmiehrslVNTAAGYrreyrldqfpvrLLQLA 5080
Cdd:cd05966   202 vpmtegrdLWWHDLMAKQSPECEPEWMDSEDPL-FILYTSGSTGKPKGV-------VHTTGGY------------LLYAA 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5081 S---FSFDVFVGDI-------------ARTLY----NGGTMVI---CPkdDRIDPARlhYW--ISEEKITIFESTPALII 5135
Cdd:cd05966   262 TtfkYVFDYHPDDIywctadigwitghSYIVYgplaNGATTVMfegTP--TYPDPGR--YWdiVEKHKVTIFYTAPTAIR 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5136 PFM----DYVAEHglDMSSMVLLITSSDSCSVTDYRVLQERFG-SQFRIINAYGVTE----------AAIdsslydePL- 5199
Cdd:cd05966   338 ALMkfgdEWVKKH--DLSSLRVLGSVGEPINPEAWMWYYEVIGkERCPIVDTWWQTEtggimitplpGAT-------PLk 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5200 ---AKLPEAGNVPIgkaalnakfyIVDAHLNPVPVGVLGELCIGGI--GVARGYLNRPElteeKFVDSPFVEGERLYRTG 5274
Cdd:cd05966   409 pgsATRPFFGIEPA----------ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTG 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5275 DLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA-KGQK-----VLCAHFTAESELKlSE 5348
Cdd:cd05966   475 DGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGEAiyafvTLKDGEEPSDELR-KE 553
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 386647928 5349 LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05966   554 LRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
7473-7928 5.09e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 92.08  E-value: 5.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7473 TYRELNERANRLARTLRAEGVQADQPVGLMI---ERSLEMIvgaFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVL-- 7547
Cdd:PRK07008   41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAY---YGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVlf 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7548 ------LTQRHLQECVSFDGKVIAADDE---------QAY-----GEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVE 7607
Cdd:PRK07008  118 dltflpLVDALAPQCPNVKGWVAMTDAAhlpagstplLCYetlvgAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7608 HHG--LCSLKLMFAETLRITEEDRVVQFASLsFDASCWEI-FKALFFGATLYIPAKDtiLD----YPLFESymneNGITA 7680
Cdd:PRK07008  198 HRStvLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLpYSAPLTGAKLVLPGPD--LDgkslYELIEA----ERVTF 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7681 AILPPTYAI----YLSPD--RLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTEAS----IVTSVWAASPDGLDL 7748
Cdd:PRK07008  271 SAGVPTVWLgllnHMREAglRFSTLRRTVIGGSACPPAMIRTFEDEygVEVIHAWGMTEMSplgtLCKLKWKHSQLPLDE 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7749 RSVPI---GRPIANHQIFIVDSQNHMLPV-GVA-GELCISGAGLARGYLNRPeltaekfvDNPFLAGerMYRTGDLARWL 7823
Cdd:PRK07008  351 QRKLLekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRGD--------ASPLVDG--WFPTGDVATID 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7824 PDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIArgdangqqqlCAY---------FVADR---ELTVSE 7891
Cdd:PRK07008  421 ADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA----------CAHpkwderpllVVVKRpgaEVTREE 490
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 7892 LRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK07008  491 LLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
PRK05857 PRK05857
fatty acid--CoA ligase;
3862-4339 5.44e-18

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 91.99  E-value: 5.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3862 EQALRNPDAVAVVFE--KSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYP 3939
Cdd:PRK05857   22 EQARQQPEAIALRRCdgTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3940 EDRIRYMLEDSGAQALLTQR-----------------HLRERVSFAGTFVAVDDEQAYHADgsnlEPVVGPNHLAYVIYT 4002
Cdd:PRK05857  102 IAAIERFCQITDPAAALVAPgskmassavpealhsipVIAVDIAAVTRESEHSLDAASLAG----NADQGSEDPLAMIFT 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4003 SGTTGKPKGVMVEHHGLCSL-KLMFANTLQ-MTEQDRVVQFASLSFD--ASCWEIFKALFFGATLYIPTSTTIldyPLFE 4078
Cdd:PRK05857  178 SGTTGEPKAVLLANRTFFAVpDILQKEGLNwVTWVVGETTYSPLPAThiGGLWWILTCLMHGGLCVTGGENTT---SLLE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4079 sYMNENGITATILPPT------YAAYLNPDRMPSLKKLITGGS---AASVEFVQQWKDKVLYFnaYGPTEASIVTSIWDE 4149
Cdd:PRK05857  255 -ILTTNAVATTCLVPTllsklvSELKSANATVPSLRLVGYGGSraiAADVRFIEATGVRTAQV--YGLSETGCTALCLPT 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4150 ASDSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGE------LCISGVGLARGYLNRPELTAEKFVDNpfepgerMY 4223
Cdd:PRK05857  332 DDGSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPsasfgtLWIKSPANMLGYWNNPERTAEVLIDG-------WV 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4224 RTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQREL---TAAE 4300
Cdd:PRK05857  405 NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELdesAARA 484
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 386647928 4301 LRATMS----QELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:PRK05857  485 LKHTIAarfrRESEPMARPSTIVIVTDIPRTQSGKVMRASLAA 527
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
5961-6364 7.60e-18

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 91.51  E-value: 7.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGgayVPIDPDYP---EDRIRYMLEDSGAklll 6037
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETEC---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6038 vqghlldRASFADklvnlnddgayhedgsnlepvNGPEHLTYVIYTSGTTGRPKGVMVEHRNVV--------RLVKNTN- 6108
Cdd:cd17639    79 -------SAIFTD---------------------GKPDDLACIMYTSGSTGNPKGVMLTHGNLVagiaglgdRVPELLGp 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6109 ---YVELNEQTHILQTGAVvfdaSTFEIWGALLNGGR-----LYVVRN--------------------ETILDAVSLK-- 6158
Cdd:cd17639   131 ddrYLAYLPLAHIFELAAE----NVCLYRGGTIGYGSprtltDKSKRGckgdltefkptlmvgvpaiwDTIRKGVLAKln 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6159 --NAIQQyginTMWLTApLYNQLSQQDSGM---------FAGLKTL--------IVGGDVLSVP---HINRVLREhagls 6216
Cdd:cd17639   207 pmGGLKR----TLFWTA-YQSKLKALKEGPgtplldelvFKKVRAAlggrlrymLSGGAPLSADtqeFLNIVLCP----- 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6217 IVNGYGPTEnTTFSTTHTIVGEQKEAVpIGKPINNSTAYIVDsklsllpvgvW-------------GELIVGGDGVARGY 6283
Cdd:cd17639   277 VIQGYGLTE-TCAGGTVQDPGDLETGR-VGPPLPCCEIKLVD----------WeeggystdkppprGEILIRGPNVFKGY 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6284 LNRPELTAEKFVessflpGERCYRTGDLARWLPDGTLEYKGRIDEQVKIR-GYRIELGEIEEQLLKVASVKEATVIVRED 6362
Cdd:cd17639   345 YKNPEKTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPD 418

                  ..
gi 386647928 6363 ES 6364
Cdd:cd17639   419 KS 420
PLN02246 PLN02246
4-coumarate--CoA ligase
3880-4339 7.72e-18

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 91.58  E-value: 7.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQR 3959
Cdd:PLN02246   51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQS 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3960 HLRERVS-FAG----TFVAVDD--EQAYH------ADGSNLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCS---L 4022
Cdd:PLN02246  131 CYVDKLKgLAEddgvTVVTIDDppEGCLHfseltqADENELPEVeISPDDVVALPYSSGTTGLPKGVMLTHKGLVTsvaQ 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4023 KLMFAN-TLQMTEQDRVV----QFASLSFDAScweIFKALFFGATLYIPTS---TTILDypLFESYmnenGIT-ATILPP 4093
Cdd:PLN02246  211 QVDGENpNLYFHSDDVILcvlpMFHIYSLNSV---LLCGLRVGAAILIMPKfeiGALLE--LIQRH----KVTiAPFVPP 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4094 TYAAYL-NPD----RMPSLKKLITGGSAASVEFVQQWKDKVLyfNA-----YGPTEASIVTSIwdeasdSLG------DR 4157
Cdd:PLN02246  282 IVLAIAkSPVvekyDLSSIRMVLSGAAPLGKELEDAFRAKLP--NAvlgqgYGMTEAGPVLAM------CLAfakepfPV 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4158 KSVPIGRPLANHRIYVVDSHNRM-LPVGVAGELCISGVGLARGYLNRPELTAekfvdnpfepgermyRTGDLVRWLPDGN 4236
Cdd:PLN02246  354 KSGSCGTVVRNAELKIVDPETGAsLPRNQPGEICIRGPQIMKGYLNDPEATA---------------NTIDKDGWLHTGD 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4237 LEYL---------GRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQR--ELTAAELRATM 4305
Cdd:PLN02246  419 IGYIddddelfivDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNgsEITEDEIKQFV 498
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 4306 SQELPNY-MIPS-YFVQlaQMPLTPNGKIDRKALPA 4339
Cdd:PLN02246  499 AKQVVFYkRIHKvFFVD--SIPKAPSGKILRKDLRA 532
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2484-2828 8.64e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 89.46  E-value: 8.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2484 PNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDrvVQFASLSF---DASCWEVFQTLFFGATLYIPT-- 2558
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDD--VLLCGLPLfhvNGSVVTLLTPLASGAHVVLAGpa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2559 ---KETILDYQW--FERYMSDngiTTATLPPTYAVYLNPDHMPDFKRL-IAAGSASSL--ELLQQWKDK--VKYFNAYGP 2628
Cdd:cd05944    79 gyrNPGLFDNFWklVERYRIT---SLSTVPTVYAALLQVPVNADISSLrFAMSGAAPLpvELRARFEDAtgLPVVEGYGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2629 TEDSICTTIWTPSTEdiSQLKSVPIGGPIVNHRIYIVDA--HYQ-PVPVGVAGELCIAGVGLARGYLNRpDLTAEKFVDn 2705
Cdd:cd05944   156 TEATCLVAVNPPDGP--KRPGSVGLRLPYARVRIKVLDGvgRLLrDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVA- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2706 pfepgERMYRTGDLAKWLPDGTIEYLGRIDHQVkIR-GYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAY--FV 2782
Cdd:cd05944   232 -----DGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYvqLK 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 2783 ADRTMTVGELRGELSGELPGY-MIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05944   306 PGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1304-1667 8.85e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 91.29  E-value: 8.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1304 EKQAERTPEVAAVVYENDR--LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 1381
Cdd:PRK13391    4 GIHAQTTPDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1382 PSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAV-LCLD-------------DEAAYAEDASNVANVNEPHDLayvI 1447
Cdd:PRK13391   84 TPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVrHRLVldgdgelegfvgyAEAVAGLPATPIADESLGTDM---L 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1448 YTSGTTGRPKGVMIEHRS-----------LVNTAAGYRREYRLDQfPVRLLQLASFSfdvFVGDIARTlynGGTMVICpk 1516
Cdd:PRK13391  161 YSSGTTGRPKGIKRPLPEqppdtplpltaFLQRLWGFRSDMVYLS-PAPLYHSAPQR---AVMLVIRL---GGTVIVM-- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1517 dDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAE--HGLDMSSMELLITSSDSCSVTDYRVLQERFGSqfrIINA-Y 1593
Cdd:PRK13391  232 -EHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEvrDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGP---IIHEyY 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 1594 GVTEA----AIDSslyDEPLAKLPEAGNVPIGkaalnaKFYIVDAHLNPVPVGVLGELCIGGiGVARGYLNRPELTEE 1667
Cdd:PRK13391  308 AATEGlgftACDS---EEWLAHPGTVGRAMFG------DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAE 375
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
4868-5312 8.99e-18

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 91.58  E-value: 8.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4868 EKAQIVHVFN---PAAPdAPENEAFHALFEKQAECTPEAAAVV--YENDRLTYRELNERANRLARTLRAQGVKPNQLVGI 4942
Cdd:PLN02330    7 KQEDNEHIFRsryPSVP-VPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4943 LADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ-THLQ-----------------ERAQQWGQT 5004
Cdd:PLN02330   86 VLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNdTNYGkvkglglpvivlgeekiEGAVNWKEL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5005 LQAALCLDDEAAYAEDASNvanvnephDLAYVIYTSGTTGRPKGVMIEHRSLV----NTAAGYRREYrLDQfpVRLLQLA 5080
Cdd:PLN02330  166 LEAADRAGDTSDNEEILQT--------DLCALPFSSGTTGISKGVMLTHRNLVanlcSSLFSVGPEM-IGQ--VVTLGLI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5081 SFsFDVF--VGDIARTLYNGGTMVICPKDD-RIdpaRLHYWISEEkITIFESTPALIIPFMDYVAEHGLDMSSMVL--LI 5155
Cdd:PLN02330  235 PF-FHIYgiTGICCATLRNKGKVVVMSRFElRT---FLNALITQE-VSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIM 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5156 TSSDSCSVTDYRVLQERF-GSQFRiiNAYGVTEAAIDSSLYDEP-----LAKLPEAGNVpigKAALNAKFYIVDAHLNpV 5229
Cdd:PLN02330  310 TAAAPLAPELLTAFEAKFpGVQVQ--EAYGLTEHSCITLTHGDPekghgIAKKNSVGFI---LPNLEVKFIDPDTGRS-L 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5230 PVGVLGELCIGGIGVARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIET 5309
Cdd:PLN02330  384 PKNTPGELCVRSQCVMQGYYNNKEETDRT------IDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEA 457

                  ...
gi 386647928 5310 QLL 5312
Cdd:PLN02330  458 ILL 460
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
5944-6420 9.25e-18

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 91.85  E-value: 9.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5944 QAERIPDHLAVTFE------DKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDP 6017
Cdd:cd05966    62 HLKERGDKVAIIWEgdepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6018 DYPEDRIRYMLEDSGAKLL--------------------------------LVQGHLLDRASFADKL-VNLNDDGAYHED 6064
Cdd:cd05966   142 GFSAESLADRINDAQCKLVitadggyrggkviplkeivdealekcpsvekvLVVKRTGGEVPMTEGRdLWWHDLMAKQSP 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6065 GSNLEPVNgPEHLTYVIYTSGTTGRPKGVMveHRNVVRLVkntnyvelneqtHILQTGAVVFDAS--------------- 6129
Cdd:cd05966   222 ECEPEWMD-SEDPLFILYTSGSTGKPKGVV--HTTGGYLL------------YAATTFKYVFDYHpddiywctadigwit 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6130 --TFEIWGALLNG---------------GRLYVVrnetildavslknaIQQYGInTMWLTAP----LYnqlsqqdsgMFA 6188
Cdd:cd05966   287 ghSYIVYGPLANGattvmfegtptypdpGRYWDI--------------VEKHKV-TIFYTAPtairAL---------MKF 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6189 G--------LKTLIVGGdvlSV--PhIN----RVLREHAG---LSIVNGYGPTENTTFSTTHtIVGeqkeAVPIgKPINN 6251
Cdd:cd05966   343 GdewvkkhdLSSLRVLG---SVgeP-INpeawMWYYEVIGkerCPIVDTWWQTETGGIMITP-LPG----ATPL-KPGSA 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6252 ST------AYIVDSKLSLLPVGVWGELIVGGD--GVARGYLNRPEltaeKFVESSFLPGERCYRTGDLARWLPDGTLEYK 6323
Cdd:cd05966   413 TRpffgiePAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWIT 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6324 GRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDE-SGQKqLCAYFV------AERELtIGELRAALSQELPNYM 6396
Cdd:cd05966   489 GRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGEA-IYAFVTlkdgeePSDEL-RKELRKHVRKEIGPIA 566
                         570       580
                  ....*....|....*....|....*.
gi 386647928 6397 IPS--HFVPleRMPLTPNGKIDRRAL 6420
Cdd:cd05966   567 TPDkiQFVP--GLPKTRSGKIMRRIL 590
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
7591-7925 9.40e-18

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 88.87  E-value: 9.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7591 VIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLsFDAScweifkALFFG-ATLYIPAKDTILDYplF 7669
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPL-FHIA------GLNLAlATFHAGGANVVMEK--F 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7670 ESYM-----NENGITA-AILPPTYAIYL-----SPDRLPSLKkLITGGSAAsvEFVQQWKDKV--RYFNAYGPTEASIVT 7736
Cdd:cd17637    76 DPAEaleliEEEKVTLmGSFPPILSNLLdaaekSGVDLSSLR-HVLGLDAP--ETIQRFEETTgaTFWSLYGQTETSGLV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7737 SVwAASPDgldlRSVPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNpflagerMYRT 7816
Cdd:cd17637   153 TL-SPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHT 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7817 GDLARWLPDGNIEYLGRIDHQ--VKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSEL 7892
Cdd:cd17637   221 GDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVlkPGATLTADEL 300
                         330       340       350
                  ....*....|....*....|....*....|...
gi 386647928 7893 RGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd17637   301 IEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
3399-3711 9.84e-18

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 89.94  E-value: 9.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3399 ALTPMQKGMWFHNTLNRhggayiEQTLFNV------RGALNIELFSRSWNELAARHAVLRTNFHSGwRGEPLQIVYRYKP 3472
Cdd:cd19537     3 ALSPIEREWWHKYQLST------GTSSFNVsfacrlSGDVDRDRLASAWNTVLARHRILRSRYVPR-DGGLRRSYSSSPP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3473 VefayedlrhlaeAEWSAYLDqlVNDDKTRGFDLEQDALMRVKVVRTqeesfHVLWSFHHILMDGWCLPLIAKELFDTYe 3552
Cdd:cd19537    76 R------------VQRVDTLD--VWKEINRPFDLEREDPIRVFISPD-----TLLVVMSHIICDLTTLQLLLREVSAAY- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3553 aylrNDLSERPAAPSYSHYIEWLEKQDMEAAArYWTGFLAGYDSQTTLPQGKLHNKDGEyteaNILRSLGKSLTERMSRI 3632
Cdd:cd19537   136 ----NGKLLPPVRREYLDSTAWSRPASPEDLD-FWSEYLSGLPLLNLPRRTSSKSYRGT----SRVFQLPGSLYRSLLQF 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3633 AKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSGRSAEiaGIEEMIGLFINTIPVRV--SCEAEQSFADVMKRVQEA 3710
Cdd:cd19537   207 STSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSE--EDMETVGLFLEPLPIRIrfPSSSDASAADFLRAVRRS 284

                  .
gi 386647928 3711 A 3711
Cdd:cd19537   285 S 285
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
1274-1701 1.12e-17

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 91.48  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1274 LTVEEKAQLVHVFNPAAPDAPENEVFHALFEKQAERTPEVAAVVYEND-----RLTYRELNERANRLARMLRAQGVKPNQ 1348
Cdd:PRK08180   16 VEVERRADGTIYLRSAEPLGDYPRRLTDRLVHWAQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGLSAER 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1349 LVGILADRSADLLVGALAVWKAGGAYVPLDPDY---PSD--RIQFMLEdsaasvLLTQTHL-QERAQQWGQTLQAVLCLD 1422
Cdd:PRK08180   96 PLMILSGNSIEHALLALAAMYAGVPYAPVSPAYslvSQDfgKLRHVLE------LLTPGLVfADDGAAFARALAAVVPAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1423 DEAAYAEDASN---------------VANVNE------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYR-LD 1480
Cdd:PRK08180  170 VEVVAVRGAVPgraatpfaallatppTAAVDAahaavgPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfLA 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1481 QFPVRLLQLASFSfDVFVG--DIARTLYNGGTMVICpkDDRIDPARLhywisEEKI--------TIFESTPA---LIIPF 1547
Cdd:PRK08180  250 EEPPVLVDWLPWN-HTFGGnhNLGIVLYNGGTLYID--DGKPTPGGF-----DETLrnlreispTVYFNVPKgweMLVPA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1548 M---DYVAEHGLdmSSMELLITS--SDSCSVTD--YRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKlpeAGNVPI 1620
Cdd:PRK08180  322 LerdAALRRRFF--SRLKLLFYAgaALSQDVWDrlDRVAEATCGERIRMMTGLGMTETAPSATFTTGPLSR---AGNIGL 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1621 GKAALNAKFyivdahlnpVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvEGerLYRTGDLARWM----PDGNVD 1696
Cdd:PRK08180  397 PAPGCEVKL---------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDE----EG--YYRSGDAVRFVdpadPERGLM 461

                  ....*
gi 386647928 1697 FIGRI 1701
Cdd:PRK08180  462 FDGRI 466
PLN02246 PLN02246
4-coumarate--CoA ligase
284-749 1.17e-17

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 91.20  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  284 RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLS 363
Cdd:PLN02246   49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  364 QGHLQERVSFSG-----TWIRLDDE--------EAYHEDGSNLESVN-GPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVV 429
Cdd:PLN02246  129 QSCYVDKLKGLAeddgvTVVTIDDPpegclhfsELTQADENELPEVEiSPDDVVALPYSSGTTGLPKGVMLTHKGLVTSV 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  430 ------KNTNyIDVTGQDKLL----QLSSYSFDGStfdIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQISVMFITTA 499
Cdd:PLN02246  209 aqqvdgENPN-LYFHSDDVILcvlpMFHIYSLNSV---LLCGLRVGAAILIMPK---FEIGALLELIQRHKVTIAPFVPP 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  500 FFnVLVDMNPDCLRH----ARAILFGG-------ERVSVSHVRKALghLGPGkikhvYGPTE-----STVFATSYDVHEV 563
Cdd:PLN02246  282 IV-LAIAKSPVVEKYdlssIRMVLSGAaplgkelEDAFRAKLPNAV--LGQG-----YGMTEagpvlAMCLAFAKEPFPV 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  564 EEGAVsipiGGPISNTAIYIVNAQNKLQ-PIGVAGELCVAGDGLARGYLNRPDLTAekfadnpfapgermyRTGDLARWL 642
Cdd:PLN02246  354 KSGSC----GTVVRNAELKIVDPETGASlPRNQPGEICIRGPQIMKGYLNDPEATA---------------NTIDKDGWL 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  643 PDGTIEY---------VGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVR-ESANGEKQLcAYYV--ADRSLPANE 710
Cdd:PLN02246  415 HTGDIGYiddddelfiVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMkDEVAGEVPV-AFVVrsNGSEITEDE 493
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928  711 VRSTLSQELPAY--MLPSYFVqlEQMPLTTNGKVDRRALPA 749
Cdd:PLN02246  494 IKQFVAKQVVFYkrIHKVFFV--DSIPKAPSGKILRKDLRA 532
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1274-1722 1.21e-17

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 91.19  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1274 LTVEEKAQLVHVFN---PAAPdAPENEVFHALFEKQAERTPEVAAVV--YENDRLTYRELNERANRLARMLRAQGVKPNQ 1348
Cdd:PLN02330    3 MEIQKQEDNEHIFRsryPSVP-VPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1349 LVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ-THLQ-----------------ERAQQ 1410
Cdd:PLN02330   82 VVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNdTNYGkvkglglpvivlgeekiEGAVN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1411 WGQTLQAvlclddeaayAEDASNVANVNEPH--DLAYVIYTSGTTGRPKGVMIEHRSLV----NTAAGYRREYrLDQfpV 1484
Cdd:PLN02330  162 WKELLEA----------ADRAGDTSDNEEILqtDLCALPFSSGTTGISKGVMLTHRNLVanlcSSLFSVGPEM-IGQ--V 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1485 RLLQLASFsFDVF--VGDIARTLYNGGTMVICPKDD-RIdpaRLHYWISEEkITIFESTPALIIPFMDYVAEHGLDMSSM 1561
Cdd:PLN02330  229 VTLGLIPF-FHIYgiTGICCATLRNKGKVVVMSRFElRT---FLNALITQE-VSFAPIVPPIILNLVKNPIVEEFDLSKL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1562 EL--LITSSDSCSVTDYRVLQERF-GSQFRiiNAYGVTEAAIDSSLYDEP-----LAKLPEAGNVpigKAALNAKFYIVD 1633
Cdd:PLN02330  304 KLqaIMTAAAPLAPELLTAFEAKFpGVQVQ--EAYGLTEHSCITLTHGDPekghgIAKKNSVGFI---LPNLEVKFIDPD 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1634 AHLNpVPVGVLGELCIGGIGVARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIE 1713
Cdd:PLN02330  379 TGRS-LPKNTPGELCVRSQCVMQGYYNNKEETDRT------IDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVA 451

                  ....*....
gi 386647928 1714 TGEIETQLL 1722
Cdd:PLN02330  452 PAELEAILL 460
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
1442-1792 1.22e-17

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 88.47  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1442 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpKDDRID 1521
Cdd:cd17635     2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT--GGENTT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1522 PARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLqERFGSQfRIINAYGVTEAAID 1601
Cdd:cd17635    80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFI-EATGLT-NTAQVYGLSETGTA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1602 SSL-YDEplaKLPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerl 1680
Cdd:cd17635   158 LCLpTDD---DSIEINAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV------ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1681 yRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESEL---KLS 1757
Cdd:cd17635   227 -NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELdenAIR 305
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 386647928 1758 ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 1792
Cdd:cd17635   306 ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PLN02574 PLN02574
4-coumarate--CoA ligase-like
7472-7928 1.32e-17

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 91.06  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQ 7550
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7551 RH--------------LQECVSFDGKVI--AADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSL 7614
Cdd:PLN02574  147 PEnveklsplgvpvigVPENYDFDSKRIefPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAM 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7615 KLMFaetlriteedrvVQF-ASLSFDASCWEIFKALF-----FGATLY----IPAKDTILDYPLFES-----YMNENGIT 7679
Cdd:PLN02574  227 VELF------------VRFeASQYEYPGSDNVYLAALpmfhiYGLSLFvvglLSLGSTIVVMRRFDAsdmvkVIDRFKVT 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7680 A-AILPPTYAIYLSPDR------LPSLKKLITGGSAASVEFVQQWKD---KVRYFNAYGPTEASIVTSVWAASPDGLDLR 7749
Cdd:PLN02574  295 HfPVVPPILMALTKKAKgvcgevLKSLKQVSCGAAPLSGKFIQDFVQtlpHVDFIQGYGMTESTAVGTRGFNTEKLSKYS 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7750 SVPIGRPiaNHQIFIVD-SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNI 7828
Cdd:PLN02574  375 SVGLLAP--NMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYFDEDGYL 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7829 EYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELTVSE--LRGTLSQELPGYMIP 7906
Cdd:PLN02574  447 YIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQeaVINYVAKQVAPYKKV 526
                         490       500
                  ....*....|....*....|..
gi 386647928 7907 SYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PLN02574  527 RKVVFVQSIPKSPAGKILRREL 548
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
2486-2825 1.51e-17

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 87.85  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2486 DLAYIIYTSGTTGKPKGVMVEHHGLcsLKQMFANT--LQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTKETIL 2563
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSW--IESFVCNEdlFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2564 DY-QWFERYMSDNGITTATLPPTYAVYLNPDHmpDFKRLIAAG---SASSLELLQQWKDKVKYFNAYGPTEDSICTTIwt 2639
Cdd:cd17633    79 SWiRKINQYNATVIYLVPTMLQALARTLEPES--KIKSIFSSGqklFESTKKKLKNIFPKANLIEFYGTSELSFITYN-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2640 pSTEDISQLKSVpiGGPIVNHRIYIVDAHYqpvpvGVAGELCIAGVGLARGYLNRPDLTAEKFvdnpfepgermYRTGDL 2719
Cdd:cd17633   155 -FNQESRPPNSV--GRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDI 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2720 AKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADrTMTVGELRGELSGE 2799
Cdd:cd17633   216 GYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYKQLKRFLKQK 294
                         330       340
                  ....*....|....*....|....*.
gi 386647928 2800 LPGYMIPAHFVQLERMPLTPNGKIDR 2825
Cdd:cd17633   295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
7460-7928 1.61e-17

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 90.84  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVFE----NTQ--LTYRELNERANRLARTLRAEGVQADQPVGL---MI-ERSLEM------------IVGAFA-- 7515
Cdd:cd05967    65 GDQIALIYDspvtGTErtYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympMIpEAAIAMlacarigaihsvVFGGFAak 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7516 -------------IMKA-----GGAYVPIDPEYPEdriryMLEDSGAQ---VLLTQRHLQECVSFDGkviAAD-DEQAYG 7573
Cdd:cd05967   145 elasriddakpklIVTAscgiePGKVVPYKPLLDK-----ALELSGHKphhVLVLNRPQVPADLTKP---GRDlDWSELL 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7574 EDGSNLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCslkLMFAETLRITEEdrvVQFASLSFDAS--CWEI----- 7645
Cdd:cd05967   217 AKAEPVDCVpVAATDPLYILYTSGTTGKPKGVVRDNGGHA---VALNWSMRNIYG---IKPGDVWWAASdvGWVVghsyi 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7646 -FKALFFGAT--LYIPAKDTILDYPLFESYMNENGITAAILPPTyAI-----------YLSPDRLPSLKKLITGGS---A 7708
Cdd:cd05967   291 vYGPLLHGATtvLYEGKPVGTPDPGAFWRVIEKYQVNALFTAPT-AIrairkedpdgkYIKKYDLSSLRTLFLAGErldP 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7709 ASVEFVQQwKDKVRYFNAYGPTEasivtSVWA--ASPDGLDLRSVPIG---RPIANHQIFIVDSQNHMLPVGVAGELCIS 7783
Cdd:cd05967   370 PTLEWAEN-TLGVPVIDHWWQTE-----TGWPitANPVGLEPLPIKAGspgKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7784 GAgLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQET 7863
Cdd:cd05967   444 LP-LPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEC 522
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 7864 IVIARGDANGQQQLCAYFVA------DRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05967   523 AVVGVRDELKGQVPLGLVVLkegvkiTAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
276-747 1.62e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 90.35  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  276 AVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLED 355
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  356 SGTQVL---------------LSQGHLQERVSFSGTwirLDDEEAYHEDGSNLESVNGPEHL--TYVIYTSGTTGKPKGn 418
Cdd:PRK08276   82 SGAKVLivsaaladtaaelaaELPAGVPLLLVVAGP---VPGFRSYEEALAAQPDTPIADETagADMLYSSGTTGRPKG- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  419 ltthrniIRVVKNTNYIDVTgQDKLLQLSSYSFDGSTFDI--------------FG--ALLNGAKLVLVPK---ETVLDv 479
Cdd:PRK08276  158 -------IKRPLPGLDPDEA-PGMMLALLGFGMYGGPDSVylspaplyhtaplrFGmsALALGGTVVVMEKfdaEEALA- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  480 aklagLIEKQQISVM-FITTAFFNVLvdMNPDCLRharailfggERVSVSHVRKALgHLG---PGKIK------------ 543
Cdd:PRK08276  229 -----LIERYRVTHSqLVPTMFVRML--KLPEEVR---------ARYDVSSLRVAI-HAAapcPVEVKramidwwgpiih 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  544 HVYGPTES--TVFATSYDVHEvEEGAVSIPIGGpisntAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEkf 621
Cdd:PRK08276  292 EYYASSEGggVTVITSEDWLA-HPGSVGKAVLG-----EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA-- 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  622 ADNPfapgERMYRTGDLArWL-PDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEK----- 694
Cdd:PRK08276  364 ARNP----HGWVTVGDVG-YLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgVPDEEMGERvkavv 438
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928  695 QLCAYYVADRSLpANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK08276  439 QPADGADAGDAL-AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
2360-2836 1.77e-17

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 90.72  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2360 DHPAVVFEG----QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRIS 2435
Cdd:PRK04319   59 DKVALRYLDasrkEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2436 YMLEDSSAQVLLAQRRLQERVSFAG-----TVVTVDDEQ-------------AYAGDGSNLEsAVGPNDLAYIIYTSGTT 2497
Cdd:PRK04319  139 DRLEDSEAKVLITTPALLERKPADDlpslkHVLLVGEDVeegpgtldfnalmEQASDEFDIE-WTDREDGAILHYTSGST 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2498 GKPKGV------MVEHHglcslkqmfantlqinAQDRVVQfaSLSFDASCW-------------EVFQTLFFGATLYIPT 2558
Cdd:PRK04319  218 GKPKGVlhvhnaMLQHY----------------QTGKYVL--DLHEDDVYWctadpgwvtgtsyGIFAPWLNGATNVIDG 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2559 KETILDyQWFeRYMSDNGIT---TAtlpPTyavylnpdhmpDFKRLIAAGSasslELLQQ-------------------- 2615
Cdd:PRK04319  280 GRFSPE-RWY-RILEDYKVTvwyTA---PT-----------AIRMLMGAGD----DLVKKydlsslrhilsvgeplnpev 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2616 --WKDKVkyfnaYG-PTEDsictTIWTpsTED----ISQLKSVPI-----GGPIVNHRIYIVDAHYQPVPVGVAGELCI- 2682
Cdd:PRK04319  340 vrWGMKV-----FGlPIHD----NWWM--TETggimIANYPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIk 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2683 AG-VGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQ 2761
Cdd:PRK04319  409 KGwPSMMRGIWNNPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVA 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2762 EAIVIAHDDASGQKQLCAyFVADRTmtvG-----ELRGELSG----ELPGYMIPAHFVQLERMPLTPNGKIDRKALPA-- 2830
Cdd:PRK04319  482 EAGVIGKPDPVRGEIIKA-FVALRP---GyepseELKEEIRGfvkkGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwe 557

                  ....*....
gi 386647928 2831 ---PQGNAS 2836
Cdd:PRK04319  558 lglPEGDLS 566
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
1307-1792 1.91e-17

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 90.63  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDpdYpsdri 1386
Cdd:PLN02860   17 ATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN--Y----- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QFMLEDSAASVLLTQTHL---QERAQQWGQTLQA---------VLCLDDEAAYAEDASNVANVNE--------------- 1439
Cdd:PLN02860   90 RWSFEEAKSAMLLVRPVMlvtDETCSSWYEELQNdrlpslmwqVFLESPSSSVFIFLNSFLTTEMlkqralgtteldyaw 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1440 -PHDLAYVIYTSGTTGRPKGVMIEHRSLVN------TAAGYRREyrlDQFpvrlLQLASFsfdVFVGDIARTLYN---GG 1509
Cdd:PLN02860  170 aPDDAVLICFTSGTTGRPKGVTISHSALIVqslakiAIVGYGED---DVY----LHTAPL---CHIGGLSSALAMlmvGA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1510 TMVICPKddrIDPARLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMS--SMELLITSSDSCSVtdyRVLQE--RFGS 1585
Cdd:PLN02860  240 CHVLLPK---FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVfpSVRKILNGGGSLSS---RLLPDakKLFP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1586 QFRIINAYGVTEAAidSSL----YDEPLAKLPeagnvpigKAALNAKFYIVDAHLNPvPVGV-LG------ELCIGGIGV 1654
Cdd:PLN02860  314 NAKLFSAYGMTEAC--SSLtfmtLHDPTLESP--------KQTLQTVNQTKSSSVHQ-PQGVcVGkpaphvELKIGLDES 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1655 AR--GYLNRPELTEEKFVDSPFVEGERLYR-----TGDLArWMPD-GNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEG 1726
Cdd:PLN02860  383 SRvgRILTRGPHVMLGYWGQNSETASVLSNdgwldTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPG 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1727 VREAVVVVREDAK-GQKVL-CA------------YFTAESELKLSE--LRSSLS-QELPGYMIPSYFVQLE-QLPLTANG 1788
Cdd:PLN02860  462 VASVVVVGVPDSRlTEMVVaCVrlrdgwiwsdneKENAKKNLTLSSetLRHHCReKNLSRFKIPKLFVQWRkPFPLTTTG 541

                  ....
gi 386647928 1789 KIDR 1792
Cdd:PLN02860  542 KIRR 545
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
3999-4333 2.05e-17

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 87.74  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3999 VIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLsFDASCWEIFKALFF--GATLYIP--TSTTILDy 4074
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTLMFTLATFHagGTNVFVRrvDAEEVLE- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4075 pLFESymnENGITATILPPTYA--AYLNPDRMPSLKKLITGGSAASvefvqqWKDKVL--------YFNAYGPTEAS-IV 4143
Cdd:cd17636    83 -LIEA---ERCTHAFLLPPTIDqiVELNADGLYDLSSLRSSPAAPE------WNDMATvdtspwgrKPGGYGQTEVMgLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4144 TSIWdeasdsLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDnpfepgeRMY 4223
Cdd:cd17636   153 TFAA------LGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GWH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4224 RTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV--AQRELTAAEL 4301
Cdd:cd17636   220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkPGASVTEAEL 299
                         330       340       350
                  ....*....|....*....|....*....|..
gi 386647928 4302 RATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:cd17636   300 IEHCRARIASYKKPKSVEFADALPRTAGGADD 331
PLN02479 PLN02479
acetate-CoA ligase
4882-5387 2.26e-17

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 90.29  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4882 DAPENEA-FHAL-----FEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGAL 4955
Cdd:PLN02479    9 DLPKNAAnYTALtplwfLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4956 AVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVL--------LTQTHLQERAQQWGQTLQAALCL---DD-------EAAY 5017
Cdd:PLN02479   89 GVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVmvdqefftLAEEALKILAEKKKSSFKPPLLIvigDPtcdpkslQYAL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5018 AEDASNVANVNEPHDLAYVI-------------YTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSF 5084
Cdd:PLN02479  169 GKGAIEYEKFLETGDPEFAWkppadewqsialgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHC 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5085 DVFVGDIARTLYNGGTmvICPKddRIDPARLHYWISEEKITIFESTPALIIPFMDY-VAEHGLDMSSMVLLITSSDSCSV 5163
Cdd:PLN02479  249 NGWCFTWTLAALCGTN--ICLR--QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNApKSETILPLPRVVHVMTAGAAPPP 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5164 TDYRVLQERfgsQFRIINAYGVTEAAIDSSLydepLAKLPEAGNVP-IGKAALNAK----------FYIVDAH-LNPVPV 5231
Cdd:PLN02479  325 SVLFAMSEK---GFRVTHTYGLSETYGPSTV----CAWKPEWDSLPpEEQARLNARqgvryiglegLDVVDTKtMKPVPA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5232 --GVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIET 5309
Cdd:PLN02479  398 dgKTMGEIVMRGNMVMKGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVEN 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5310 QLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSELRSSLS-------QELPGYMIPSYFVqLEQLPLTANGKIDR 5382
Cdd:PLN02479  471 VVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEdimkfcrERLPAYWVPKSVV-FGPLPKTATGKIQK 549

                  ....*
gi 386647928 5383 KALPA 5387
Cdd:PLN02479  550 HVLRA 554
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
1321-1718 2.43e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 90.06  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1321 DRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPL-DPDYPSD---------RIQFML 1390
Cdd:PRK07768   28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLhQPTPRTDlavwaedtlRVIGMI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1391 EDSAasVLLTqthlqERAQQWGQTLQA----VLCLDDeaAYAEDASNVANVNEpHDLAYVIYTSGTTGRPKGVMIEHRSL 1466
Cdd:PRK07768  108 GAKA--VVVG-----EPFLAAAPVLEEkgirVLTVAD--LLAADPIDPVETGE-DDLALMQLTSGSTGSPKAVQITHGNL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1467 VNTAAGYRREYRLDQFPVRLLQLASFSFDV-FVGDIARTLYNGGTMV-ICPKDDRIDP---ARLhywISEEKITIfESTP 1541
Cdd:PRK07768  178 YANAEAMFVAAEFDVETDVMVSWLPLFHDMgMVGFLTVPMYFGAELVkVTPMDFLRDPllwAEL---ISKYRGTM-TAAP 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 ----ALIIPFMDYVAEHG-LDMSSMELLITSSDSCSVTDYRVLQE---RFGsqFR---IINAYGVTEAAIDSSL------ 1604
Cdd:PRK07768  254 nfayALLARRLRRQAKPGaFDLSSLRFALNGAEPIDPADVEDLLDagaRFG--LRpeaILPAYGMAEATLAVSFspcgag 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1605 --YDEPLAKLPEAGN--VPIGKAALNA-----------KFYIVDAHLNPVPVGVLGELCIGGIGVARGYlnrpeLTEEKF 1669
Cdd:PRK07768  332 lvVDEVDADLLAALRraVPATKGNTRRlatlgpplpglEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGF 406
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 1670 VdsPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIE 1718
Cdd:PRK07768  407 I--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1416-1795 2.45e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 90.21  E-value: 2.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1416 QAVLCLDDEAAYAEDASNVANVNePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR--EYRLDQ------FPVRLL 1487
Cdd:PRK05677  183 QAVKFNDALAKGAGQPVTEANPQ-ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRAlmGSNLNEgceiliAPLPLY 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1488 QLASFSFDVFVgdiarTLYNGGTMVICPkDDRIDPARLHYwISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITS 1567
Cdd:PRK05677  262 HIYAFTFHCMA-----MMLIGNHNILIS-NPRDLPAMVKE-LGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSG 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1568 SDSCSVTDYRVLQERFGSQfrIINAYGVTEAAidsslydePLAKLPEAGNVPIGKAAL---NAKFYIVDAHLNPVPVGVL 1644
Cdd:PRK05677  335 GMALQLATAERWKEVTGCA--ICEGYGMTETS--------PVVSVNPSQAIQVGTIGIpvpSTLCKVIDDDGNELPLGEV 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1645 GELCIGGIGVARGYLNRPELTEEKFVDSPFVegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKA 1724
Cdd:PRK05677  405 GELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 1725 EGVREAVVVVREDAKGQKVLCAYFTAESELKLSE--LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK05677  479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKeqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
3875-4337 2.67e-17

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 89.41  E-value: 2.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3875 FEKSQLTYGELNERANRLARTLRDA-GVRPDQLVGLMVERSLEMVVGIMAIMKAGGAyipidPEYpedrIRYMLEDSGAQ 3953
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF----INYNLSGDPLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3954 ALLtqrhlreRVSFAgTFVAVDDEQayhadgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMT 4033
Cdd:cd05937    72 HCL-------KLSGS-RFVIVDPDD-----------------PAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLK 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4034 EQDRV-----VQFASLSFDASCWEI-----------FKALFFGATLYIPTSTTILdyplfesYMNENGITATILPPTyaa 4097
Cdd:cd05937   127 NGDRTytcmpLYHGTAAFLGACNCLmsggtlalsrkFSASQFWKDVRDSGATIIQ-------YVGELCRYLLSTPPS--- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4098 ylnP-DRMPSLKklITGGSAASVEFVQQWKDKvlyFNA------YGPTEAsiVTSIWDEASDSLGD---RKSVPIGRPLA 4167
Cdd:cd05937   197 ---PyDRDHKVR--VAWGNGLRPDIWERFRER---FNVpeigefYAATEG--VFALTNHNVGDFGAgaiGHHGLIRRWKF 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4168 NHRIYVV--DSHNRM------------LPVGVAGELCI----SGVGLARGYLNRPELTAEKFVDNPFEPGERMYRTGDLV 4229
Cdd:cd05937   267 ENQVVLVkmDPETDDpirdpktgfcvrAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLL 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4230 RWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN--GQQQLVAYFVAQR-----ELTAAELR 4302
Cdd:cd05937   347 RQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGhdGRAGCAAITLEESsavptEFTKSLLA 426
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 4303 ATMSQELPNYMIPsYFVQLA-QMPLTPNGKIDRKAL 4337
Cdd:cd05937   427 SLARKNLPSYAVP-LFLRLTeEVATTDNHKQQKGVL 461
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
5941-6398 3.14e-17

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 89.93  E-value: 3.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5941 FEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYP 6020
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6021 EDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVN-------LNDDGAYHEDG-SNLE------PVNGPEH--------LT 6078
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEELVEAFEEARADLArpprlwvAGGDTLDDPEGyEDLAaaaagaPTTNPASrsgvtakdTA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6079 YVIYTSGTTGRPKGVMVEHRNVVR-------LV----KNTNYVEL----NeqthilqTGAVVfdastfeIWGALLNGGRL 6143
Cdd:PRK08279  203 FYIYTSGTTGLPKAAVMSHMRWLKamggfggLLrltpDDVLYCCLplyhN-------TGGTV-------AWSSVLAAGAT 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6144 YVVRnetilDAVSLKN---AIQQYGInTMW-----LTAPLYNQ-LSQQDSG-----MF-AGLKtlivgGDVLS------- 6201
Cdd:PRK08279  269 LALR-----RKFSASRfwdDVRRYRA-TAFqyigeLCRYLLNQpPKPTDRDhrlrlMIgNGLR-----PDIWDefqqrfg 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6202 VPHinrvlrehaglsIVNGYGPTE-NTTFS-----------------TTHTIVGEQKEAvpiGKPINNStayivDSKLSL 6263
Cdd:PRK08279  338 IPR------------ILEFYAASEgNVGFInvfnfdgtvgrvplwlaHPYAIVKYDVDT---GEPVRDA-----DGRCIK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6264 LPVGVWGELI--VGGDGVARGYlNRPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGE 6341
Cdd:PRK08279  398 VKPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTE 476
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVI-VR-EDESGQKQLCAYFVAE-RELTIGELRAALSQELPNYMIP 6398
Cdd:PRK08279  477 VENALSGFPGVEEAVVYgVEvPGTDGRAGMAAIVLADgAEFDLAALAAHLYERLPAYAVP 536
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
7472-7854 3.19e-17

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 89.58  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGgayVPIDPEYP---EDRIRYMLEDSGAQVLL 7548
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7549 TqrhlqecvsfDGKviaaddeqaygedgsnlepvvgPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETL--RITE 7626
Cdd:cd17639    83 T----------DGK----------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVpeLLGP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7627 EDRVVQFASLSfdascwEIFK------ALFFGATL-YIPAKdTILDyplfESYMNENG-ITAaiLPPTY-----AIYLS- 7692
Cdd:cd17639   131 DDRYLAYLPLA------HIFElaaenvCLYRGGTIgYGSPR-TLTD----KSKRGCKGdLTE--FKPTLmvgvpAIWDTi 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7693 ----PDRLPSL----KKLITGGSAASVEFVQQWKD------------------KVRYF---------------------- 7724
Cdd:cd17639   198 rkgvLAKLNPMgglkRTLFWTAYQSKLKALKEGPGtplldelvfkkvraalggRLRYMlsggaplsadtqeflnivlcpv 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7725 -NAYGPTE---ASIVTSVWaaspdglDLRSVPIGRPIANHQIFIVD-------SQNHMlPvgvAGELCISGAGLARGYLN 7793
Cdd:cd17639   278 iQGYGLTEtcaGGTVQDPG-------DLETGRVGPPLPCCEIKLVDweeggysTDKPP-P---RGEILIRGPNVFKGYYK 346
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7794 RPELTAEKFvdnpflAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIR-GYRIELGEIEEQL 7854
Cdd:cd17639   347 NPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIY 402
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
4913-5311 3.20e-17

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 89.45  E-value: 3.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 4992
Cdd:cd05932     7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 HLQERAQQWG---QTLQAALCLDDEAAYAEDASNVAN---------VNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 5060
Cdd:cd05932    87 LDDWKAMAPGvpeGLISISLPPPSAANCQYQWDDLIAqhppleerpTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYR-------LDQFPVR------LLQLASF----------SFDVFVGDIAR---TLYNGgtmviCPKDDRIDPAR 5114
Cdd:cd05932   167 QAGIEHIGteendrmLSYLPLAhvtervFVEGGSLyggvlvafaeSLDTFVEDVQRarpTLFFS-----VPRLWTKFQQG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5115 LHYWISEEKITIFestpaLIIPFMDYVAEH------GLDMSSMVLLITSSDSCSVTD-YRVLqerfgsQFRIINAYGVTE 5187
Cdd:cd05932   242 VQDKIPQQKLNLL-----LKIPVVNSLVKRkvlkglGLDQCRLAGCGSAPVPPALLEwYRSL------GLNILEAYGMTE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5188 AAIDSSLydeplaklpeagNVP-------IGKAALNAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPELTEEKFV 5260
Cdd:cd05932   311 NFAYSHL------------NYPgrdkigtVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFT 368
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 5261 DSPFVegerlyRTGDLARWMPDGNVDFIGRI-DNQAKIRGYRIETGEIETQL 5311
Cdd:cd05932   369 ADGFL------RTGDKGELDADGNLTITGRVkDIFKTSKGKYVAPAPIENKL 414
PRK08162 PRK08162
acyl-CoA synthetase; Validated
5941-6420 3.23e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 89.62  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5941 FEEQAERI-PDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDY 6019
Cdd:PRK08162   23 FLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6020 PEDRIRYMLEDSGAKLLLVqghllDRAsFAD------------KLVNLNDDGAYHEDGSNLEPVN-------GPEHLTYV 6080
Cdd:PRK08162  103 DAASIAFMLRHGEAKVLIV-----DTE-FAEvarealallpgpKPLVIDVDDPEYPGGRFIGALDyeaflasGDPDFAWT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6081 I-----------YTSGTTGRPKGVMVEHRNVvrlvkntnYveLNEQTHILQTG----AV------VFDAS--TFEiWGAL 6137
Cdd:PRK08162  177 LpadewdaialnYTSGTTGNPKGVVYHHRGA--------Y--LNALSNILAWGmpkhPVylwtlpMFHCNgwCFP-WTVA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6138 LNGGR---LYVVRNETILDAvslknaIQQYGInTMWLTAPL-YNQLSQQDSGMFAGLkTLIVGGDVLSVPHINRVLR--E 6211
Cdd:PRK08162  246 ARAGTnvcLRKVDPKLIFDL------IREHGV-THYCGAPIvLSALINAPAEWRAGI-DHPVHAMVAGAAPPAAVIAkmE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6212 HAGLSIVNGYGPTEntTFSTThTIVGEQKE--AVPIG----KPINNSTAYIVDSKLSLL------PVG----VWGELIVG 6275
Cdd:PRK08162  318 EIGFDLTHVYGLTE--TYGPA-TVCAWQPEwdALPLDeraqLKARQGVRYPLQEGVTVLdpdtmqPVPadgeTIGEIMFR 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6276 GDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEA 6355
Cdd:PRK08162  395 GNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVA 467
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 6356 TVIVREDESGQKQLCAyFVAERE---LTIGELRAALSQELPNYMIPSHFVpLERMPLTPNGKIDRRAL 6420
Cdd:PRK08162  468 AVVAKPDPKWGEVPCA-FVELKDgasATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
2346-2722 3.24e-17

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 89.94  E-value: 3.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVFEG-----QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGG 2420
Cdd:PRK08180   40 RLTDRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2421 AYVPIDPEY---PED--RISYMLE-----------------------DSSAQVLLAQRRLQER--VSFA---GTVVTVDD 2467
Cdd:PRK08180  120 PYAPVSPAYslvSQDfgKLRHVLElltpglvfaddgaafaralaavvPADVEVVAVRGAVPGRaaTPFAallATPPTAAV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2468 EQAYAgdgsnlesAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASL----SFDAScWE 2543
Cdd:PRK08180  200 DAAHA--------AVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDWLpwnhTFGGN-HN 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2544 VFQTLFFGATLYIptketildyqwferymsDNGITTA-----TL------PPTyaVYLN-P-------DHMPD------- 2597
Cdd:PRK08180  271 LGIVLYNGGTLYI-----------------DDGKPTPggfdeTLrnlreiSPT--VYFNvPkgwemlvPALERdaalrrr 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2598 -FKRLI------AAGSASSLELLQQW-----KDKVKYFNAYGPTEDSICTTIWTPSTEdisqlKSVPIGGPIvnhriyiv 2665
Cdd:PRK08180  332 fFSRLKllfyagAALSQDVWDRLDRVaeatcGERIRMMTGLGMTETAPSATFTTGPLS-----RAGNIGLPA-------- 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2666 dahyqP------VPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKW 2722
Cdd:PRK08180  399 -----PgcevklVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
2368-2831 3.25e-17

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 89.37  E-value: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2368 GQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLL 2447
Cdd:PRK12406    9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2448 AQ----RRLQERVSFAGTVVTV----DDEQAYAGDGSNLESAVGPNDL------------------AYIIYTSGTTGKPK 2501
Cdd:PRK12406   89 AHadllHGLASALPAGVTVLSVptppEIAAAYRISPALLTPPAGAIDWegwlaqqepydgppvpqpQSMIYTSGTTGHPK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2502 GV-----MVEHhgLCSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTK---ETILdyQWFERYMs 2573
Cdd:PRK12406  169 GVrraapTPEQ--AAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRfdpEELL--QLIERHR- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2574 dngITTATLPPTYAVYLN--PDH------MPDFKRLIAAGSASSLELLQQ---WKDKVKYfNAYGPTEDSICTtiWTPST 2642
Cdd:PRK12406  244 ---ITHMHMVPTMFIRLLklPEEvrakydVSSLRHVIHAAAPCPADVKRAmieWWGPVIY-EYYGSTESGAVT--FATSE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2643 EDISQLKSVpiGGPIVNHRIYIVDAHYQPVPVGVAGELC--IAGVGLARgYLNRPDLTAEKFVDNPFEPGERMYRTGDLA 2720
Cdd:PRK12406  318 DALSHPGTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYsrIAGNPDFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2721 KWLPDgtieylgRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYF--VADRTMTVGELRGELSG 2798
Cdd:PRK12406  395 LFLCD-------RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVepQPGATLDEADIRAQLKA 467
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 2799 ELPGYMIPAHFVQLERMPLTPNGKIDRKALPAP 2831
Cdd:PRK12406  468 RLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1318-1797 3.63e-17

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 90.09  E-value: 3.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1318 YENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASV 1397
Cdd:PRK06060   26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1398 LLTQTHLQERAQQwgqtlQAVLcldDEAAYAEDASNVanvnEPHDL--------AYVIYTSGTTGRPKGVMIEHRSLVN- 1468
Cdd:PRK06060  106 VVTSDALRDRFQP-----SRVA---EAAELMSEAARV----APGGYepmggdalAYATYTSGTTGPPKAAIHRHADPLTf 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1469 TAAGYRREYRLDQFPVRLLQlASFSFDVFVGD-IARTLYNGGTMVICPKDDRIDPARLhywISeekiTIFESTPALIIP- 1546
Cdd:PRK06060  174 VDAMCRKALRLTPEDTGLCS-ARMYFAYGLGNsVWFPLATGGSAVINSAPVTPEAAAI---LS----ARFGPSVLYGVPn 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1547 -FMDYVAEHGLD-MSSMELLITSSDSCSVTDYRVLQERFGSqFRIINAYGVTEAA---IDSSLYDEPLAKLpeagnvpiG 1621
Cdd:PRK06060  246 fFARVIDSCSPDsFRSLRCVVSAGEALELGLAERLMEFFGG-IPILDGIGSTEVGqtfVSNRVDEWRLGTL--------G 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1622 KAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPElteekfvdsPFVEGERLYRTGDLARWMPDGNVDFIGRI 1701
Cdd:PRK06060  317 RVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRA 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1702 DNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAES-----ELKLSELRSSLSQELPGYMIPSYF 1776
Cdd:PRK06060  388 DDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgatidGSVMRDLHRGLLNRLSAFKVPHRF 467
                         490       500
                  ....*....|....*....|.
gi 386647928 1777 VQLEQLPLTANGKIDRKALPA 1797
Cdd:PRK06060  468 AVVDRLPRTPNGKLVRGALRK 488
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
4886-5387 5.02e-17

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 89.71  E-value: 5.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4886 NEAFHALFEKQA-ECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAY 4964
Cdd:PRK06060    3 NGNLAGLLAEQAsEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4965 VPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQwgQTLQAALCLDDEAAYAEDASNvanvnEP---HDLAYVIYTSG 5041
Cdd:PRK06060   83 FLANPELHRDDHALAARNTEPALVVTSDALRDRFQP--SRVAEAAELMSEAARVAPGGY-----EPmggDALAYATYTSG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5042 TTGRPKGVMIEHRSLVN-TAAGYRREYRLDQFPVRLLQlASFSFDVFVGD-IARTLYNGGTMVICPKDDRIDPARLhywI 5119
Cdd:PRK06060  156 TTGPPKAAIHRHADPLTfVDAMCRKALRLTPEDTGLCS-ARMYFAYGLGNsVWFPLATGGSAVINSAPVTPEAAAI---L 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5120 SeekiTIFESTPALIIP--FMDYVAEHGLD-MSSMVLLITSSDSCSVTDYRVLQERFGSqFRIINAYGVTEAA---IDSS 5193
Cdd:PRK06060  232 S----ARFGPSVLYGVPnfFARVIDSCSPDsFRSLRCVVSAGEALELGLAERLMEFFGG-IPILDGIGSTEVGqtfVSNR 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5194 LYDEPLAKLpeagnvpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPElteekfvdsPFVEGERLYRT 5273
Cdd:PRK06060  307 VDEWRLGTL--------GRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDT 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5274 GDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAES-----ELKLSE 5348
Cdd:PRK06060  370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgatidGSVMRD 449
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 386647928 5349 LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 5387
Cdd:PRK06060  450 LHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
2355-2828 5.17e-17

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 88.98  E-value: 5.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVF--EGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPED 2432
Cdd:PRK13391    7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2433 RISYMLEDSSAQVLLAQRRLQERVSFAGT---------VVTVDDE----QAYAGDGSNLESAVGPNDL--AYIIYTSGTT 2497
Cdd:PRK13391   87 EAAYIVDDSGARALITSAAKLDVARALLKqcpgvrhrlVLDGDGElegfVGYAEAVAGLPATPIADESlgTDMLYSSGTT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2498 GKPKGVMVE--HHGL---CSLKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTK---ETILdyQWFE 2569
Cdd:PRK13391  167 GRPKGIKRPlpEQPPdtpLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHfdaEQYL--ALIE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2570 RYmsdnGITTATLPPTY---------AVYLNPDHmPDFKRLIAAGSASSLELLQQ---WKDKVKYfNAYGPTEDSICTTI 2637
Cdd:PRK13391  245 EY----GVTHTQLVPTMfsrmlklpeEVRDKYDL-SSLEVAIHAAAPCPPQVKEQmidWWGPIIH-EYYAATEGLGFTAC 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2638 wtPSTEDISQLKSVpiGGPIVNhRIYIVDAHYQPVPVGVAGELCIAGvGLARGYLNRPDLTAEKfvdnpFEPGERMYRTG 2717
Cdd:PRK13391  319 --DSEEWLAHPGTV--GRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEA-----RHPDGTWSTVG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2718 DLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA-HDDASGQK-----QLCAYFVADRTMTvGE 2791
Cdd:PRK13391  388 DIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGvPNEDLGEEvkavvQPVDGVDPGPALA-AE 466
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 2792 LRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK13391  467 LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1323-1721 6.14e-17

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 88.68  E-value: 6.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT 1402
Cdd:cd05932     7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 HLQERAQQWGQTLQAVLCL---DDEAAYAEDASNVAN---------VNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTA 1470
Cdd:cd05932    87 LDDWKAMAPGVPEGLISISlppPSAANCQYQWDDLIAqhppleerpTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGYRREYR-------LDQFPVR------LLQLASF----------SFDVFVGDIAR---TLYNGgtmviCPKDDRIDPAR 1524
Cdd:cd05932   167 QAGIEHIGteendrmLSYLPLAhvtervFVEGGSLyggvlvafaeSLDTFVEDVQRarpTLFFS-----VPRLWTKFQQG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1525 LHYWISEEKITIFestpaLIIPFMDYVAEH----GLDMSSMELLITSSD--SCSVTD-YRVLqerfgsQFRIINAYGVTE 1597
Cdd:cd05932   242 VQDKIPQQKLNLL-----LKIPVVNSLVKRkvlkGLGLDQCRLAGCGSApvPPALLEwYRSL------GLNILEAYGMTE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1598 AAIDSSLydeplaklpeagNVP-------IGKAALNAKFYIVDAhlnpvpvgvlGELCIGGIGVARGYLNRPELTEEKFV 1670
Cdd:cd05932   311 NFAYSHL------------NYPgrdkigtVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFT 368
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 1671 DSPFVegerlyRTGDLARWMPDGNVDFIGRI-DNQAKIRGYRIETGEIETQL 1721
Cdd:cd05932   369 ADGFL------RTGDKGELDADGNLTITGRVkDIFKTSKGKYVAPAPIENKL 414
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
5935-6420 6.18e-17

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 88.59  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5935 KTIHQLFEEQAERIPDHLAVTFED-----KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAG 6009
Cdd:PRK08008    7 QHLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6010 GAYVPIDPDYPEDRIRYMLEDSGAKLLLVQGHLLD--RASFADKLVNLN-----DDGAYHEDGS-------NLEPVNGPE 6075
Cdd:PRK08008   87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPmyRQIQQEDATPLRhicltRVALPADDGVssftqlkAQQPATLCY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTY-------VIYTSGTTGRPKGVMVEHRNV----------VRLVKNTNYVELNEQTHI-LQTGAVVfdastfeiwGAL 6137
Cdd:PRK08008  167 APPLstddtaeILFTSGTTSRPKGVVITHYNLrfagyysawqCALRDDDVYLTVMPAFHIdCQCTAAM---------AAF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6138 LNGGRLYVVrnetildavslknaiQQYGINTMWLTAPLYNQLSQQDSGMFagLKTLIVGG-----------DVLSVPHIN 6206
Cdd:PRK08008  238 SAGATFVLL---------------EKYSARAFWGQVCKYRATITECIPMM--IRTLMVQPpsandrqhclrEVMFYLNLS 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6207 ----RVLREHAGLSIVNGYGPTEnttfstthTIVG-------EQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELI-- 6273
Cdd:PRK08008  301 dqekDAFEERFGVRLLTSYGMTE--------TIVGiigdrpgDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICik 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6274 -VGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASV 6352
Cdd:PRK08008  373 gVPGKTIFKEYYLDPKATAKVLEADGWL------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKI 446
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6353 KEATVIVREDESGQKQLCAY--FVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK08008  447 QDIVVVGIKDSIRDEAIKAFvvLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
3880-4237 6.22e-17

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 88.81  E-value: 6.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVR--PDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLT 3957
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3958 QRHLrERVSFagtfvavddEQAYHADGSNLEPVV--GPNHLAYVIYTSGTTGKPKGVMVEHHGLCS----LKLMFANTLQ 4031
Cdd:cd05927    86 DAGV-KVYSL---------EEFEKLGKKNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEILNK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4032 MTEQDRVVQFASLS--FDASCWEIFkaLFFGATLYI----------------PTS----------------TTILDYP-- 4075
Cdd:cd05927   156 INPTDVYISYLPLAhiFERVVEALF--LYHGAKIGFysgdirlllddikalkPTVfpgvprvlnriydkifNKVQAKGpl 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4076 ---LF-------ESYMNENGITATilppTYAAYLNPDRMPSL-----KKLITGGSAASV---EFVQQWKDkVLYFNAYGP 4137
Cdd:cd05927   234 krkLFnfalnykLAELRSGVVRAS----PFWDKLVFNKIKQAlggnvRLMLTGSAPLSPevlEFLRVALG-CPVLEGYGQ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4138 TEASIVTSIWDEasdslGDRKSVPIGRPLANHRIYVVD------SHNRMLPvgvAGELCISGVGLARGYLNRPELTAEKF 4211
Cdd:cd05927   309 TECTAGATLTLP-----GDTSVGHVGGPLPCAEVKLVDvpemnyDAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEAL 380
                         410       420
                  ....*....|....*....|....*.
gi 386647928 4212 VDNPFepgermYRTGDLVRWLPDGNL 4237
Cdd:cd05927   381 DEDGW------LHTGDIGEWLPNGTL 400
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
5949-6420 6.45e-17

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 89.23  E-value: 6.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  5949 PDHLAVTFE------DKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPI----DPD 6018
Cdd:TIGR02188   71 PDKVAIIWEgdepgeVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVfggfSAE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6019 YPEDRIrymlEDSGAKLLLVQghllDRASFADKLVNLND---------------------------------DGAYHE-- 6063
Cdd:TIGR02188  151 ALADRI----NDAGAKLVITA----DEGLRGGKVIPLKAivdealekcpvsvehvlvvrrtgnpvvpwvegrDVWWHDlm 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6064 ----DGSNLEPVNgPEHLTYVIYTSGTTGRPKGVMveHRNVVRLVkntnyvelneqtHILQTGAVVFD------------ 6127
Cdd:TIGR02188  223 akasAYCEPEPMD-SEDPLFILYTSGSTGKPKGVL--HTTGGYLL------------YAAMTMKYVFDikdgdifwctad 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6128 -----ASTFEIWGALLNG---------------GRLYVVrnetildavslknaIQQYGINTmWLTAPlynqlsqqdsgmf 6187
Cdd:TIGR02188  288 vgwitGHSYIVYGPLANGattvmfegvptypdpGRFWEI--------------IEKHKVTI-FYTAP------------- 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6188 AGLKTLIVGGD------------VL-SV--PhIN----RVLREHAGLS---IVNGYGPTENTTFSTTHtIVGeqkeAVPI 6245
Cdd:TIGR02188  340 TAIRALMRLGDewvkkhdlsslrLLgSVgeP-INpeawMWYYKVVGKErcpIVDTWWQTETGGIMITP-LPG----ATPT 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6246 -----GKPINNSTAYIVDSKLSLLP-VGVWGELIVGGD--GVARGYLNRPeltaEKFVESSFLPGERCYRTGDLARWLPD 6317
Cdd:TIGR02188  414 kpgsaTLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFPGYYFTGDGARRDKD 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  6318 GTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTIG-----ELRAALSQEL 6392
Cdd:TIGR02188  490 GYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDdelrkELRKHVRKEI 569
                          570       580
                   ....*....|....*....|....*...
gi 386647928  6393 PNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:TIGR02188  570 GPIAKPDKIRFVPGLPKTRSGKIMRRLL 597
PRK05857 PRK05857
fatty acid--CoA ligase;
7454-7938 6.83e-17

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 88.53  E-value: 6.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7454 EQAERMPEKAAVVFEN--TQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYP 7531
Cdd:PRK05857   22 EQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7532 EDRIRYMLEDS-------------GAQVLLTQRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTT 7598
Cdd:PRK05857  102 IAAIERFCQITdpaaalvapgskmASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTT 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7599 GKPKGVMVEHHGLCSL-KLMFAETLR-ITEEDRVVQFASLSFD--ASCWEIFKALFFGATLYIPAKDTIldyPLFEsYMN 7674
Cdd:PRK05857  182 GEPKAVLLANRTFFAVpDILQKEGLNwVTWVVGETTYSPLPAThiGGLWWILTCLMHGGLCVTGGENTT---SLLE-ILT 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7675 ENGITAAILPPT------YAIYLSPDRLPSLKKLITGGS---AASVEFVQqwKDKVRYFNAYGPTEASiVTSVWAASPDG 7745
Cdd:PRK05857  258 TNAVATTCLVPTllsklvSELKSANATVPSLRLVGYGGSraiAADVRFIE--ATGVRTAQVYGLSETG-CTALCLPTDDG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7746 --LDLRSVPIGRPIANHQIFIVDSQNHMLPVGVAGE------LCISGAGLARGYLNRPELTAEKFVDNpflagerMYRTG 7817
Cdd:PRK05857  335 siVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPsasfgtLWIKSPANMLGYWNNPERTAEVLIDG-------WVNTG 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7818 DLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADREL---TVSELRG 7894
Cdd:PRK05857  408 DLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELdesAARALKH 487
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 7895 TLS----QELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAPEGSMQTG 7938
Cdd:PRK05857  488 TIAarfrRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKAR 535
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
7470-7928 6.92e-17

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 88.66  E-value: 6.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7470 TQLTYRELNERANRLARTLRAEGVQADQPVGLM---IERSLEMIVGafaIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQV 7546
Cdd:PRK06018   38 VRTTYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYG---IMGIGAICHTVNPRLFPEQIAWIINHAEDRV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7547 LLT-------------------------------QRHLQECVSFDGKVIAADDEQAYGEdgsnlepvVGPNHLAYVIYTS 7595
Cdd:PRK06018  115 VITdltfvpilekiadklpsveryvvltdaahmpQTTLKNAVAYEEWIAEADGDFAWKT--------FDENTAAGMCYTS 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7596 GTTGKPKGVMVEHHG--LCSLKLMFAETLRITEEDRVVQFASLsFDASCWEI-FKALFFGATLYIP-AK-DTILDYPLFE 7670
Cdd:PRK06018  187 GTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVMPgAKlDGASVYELLD 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7671 SymNENGITAAIlpPTYAI----YLSPDR--LPSLKKLITGGSAASVEFVQQWKD-KVRYFNAYGPTEASIVTSVWAASP 7743
Cdd:PRK06018  266 T--EKVTFTAGV--PTVWLmllqYMEKEGlkLPHLKMVVCGGSAMPRSMIKAFEDmGVEVRHAWGMTEMSPLGTLAALKP 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7744 DGLDL-------RSVPIGRPIANHQIFIVDSQNHMLPV-GVA-GELCISGAGLARGYLNrpeltaekfVDNPFLAGERMY 7814
Cdd:PRK06018  342 PFSKLpgdarldVLQKQGYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYYR---------VDGEILDDDGFF 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7815 RTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQ--LCAYFVADRELTVSEL 7892
Cdd:PRK06018  413 DTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERplLIVQLKPGETATREEI 492
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 7893 RGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PRK06018  493 LKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
PRK09192 PRK09192
fatty acyl-AMP ligase;
1323-1475 7.11e-17

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 88.91  E-value: 7.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP-------SDRIQFMLEDSAA 1395
Cdd:PRK09192   50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQP 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1396 SVLLTQTHLQERAQQWGQTLQAVLCLDDEAAYAEDASNVA-NVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYR 1474
Cdd:PRK09192  130 AAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVAlPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIS 209

                  .
gi 386647928 1475 R 1475
Cdd:PRK09192  210 H 210
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
6992-7301 8.31e-17

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 87.16  E-value: 8.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKGMWFHTALDKEAG-----AYFEqmrFTVQGsLDAEQFARSWNDLVARHAILRTNFFSGPRGEPLQIVYRDkriG 7066
Cdd:cd19535     4 LTDVQYAYWIGRQDDQELGgvgchAYLE---FDGED-LDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWY---G 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7067 FVYEDLSHLPADERQASVERLEQEDIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDGWCLPLVVKELFetyEAY 7146
Cdd:cd19535    77 ITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELA---ALY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7147 VQGDRPEQKAAPAYSQYIEWLENQDSAA---ASAYWSNYLAGYEGQTALPQEKAQKRsegyVAEHVVC----ELDKELSE 7219
Cdd:cd19535   154 EDPGEPLPPLELSFRDYLLAEQALRETAyerARAYWQERLPTLPPAPQLPLAKDPEE----IKEPRFTrrehRLSAEQWQ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7220 RMNRAAKQCRVTVNTLMQAVWGVILQKYNATDDVVYGSVVSGRPAEIPGIEEMIGLFINTIPVRVACQPEESFADVMGRM 7299
Cdd:cd19535   230 RLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRL 309

                  ..
gi 386647928 7300 QE 7301
Cdd:cd19535   310 QQ 311
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
2355-2828 8.60e-17

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 87.62  E-value: 8.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRI 2434
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 SYMLEDSSAQVLLAqrrLQERVSFAGtvVTVDDEQAYAGDGSnleSAVGPNDLAYIIYTSGTTGKPKGVM--VEHH---- 2508
Cdd:PRK09029   93 EELLPSLTLDFALV---LEGENTFSA--LTSLHLQLVEGAHA---VAWQPQRLATMTLTSGSTGLPKAAVhtAQAHlasa 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2509 -GLCSLkqmfantLQINAQDRVVqfasLS---FDASC------WevfqtLFFGATLYIPTKETIldyqwferYMSDNGIT 2578
Cdd:PRK09029  165 eGVLSL-------MPFTAQDSWL----LSlplFHVSGqgivwrW-----LYAGATLVVRDKQPL--------EQALAGCT 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2579 TATLPPTYAV-YLNPDHMP-DFKRLIAAGSASSLELLQQWKDK-VKYFNAYGPTEdsicttiwTPSTEDISQLKSVP-IG 2654
Cdd:PRK09029  221 HASLVPTQLWrLLDNRSEPlSLKAVLLGGAAIPVELTEQAEQQgIRCWCGYGLTE--------MASTVCAKRADGLAgVG 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2655 GPIVNHRIYIVDahyqpvpvgvaGELCIAGVGLARGYLNRPDLTaekfvdnPFEPGERMYRTGDLAKWLpDGTIEYLGRI 2734
Cdd:PRK09029  293 SPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTILGRL 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2735 DHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDAS-GQKQLcAYFVADRTMTVGELRGELSGELPGYMIPahfVQLE 2813
Cdd:PRK09029  354 DNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEfGQRPV-AVVESDSEAAVVNLAEWLQDKLARFQQP---VAYY 429
                         490
                  ....*....|....*...
gi 386647928 2814 RMPLT-PNG--KIDRKAL 2828
Cdd:PRK09029  430 LLPPElKNGgiKISRQAL 447
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
247-710 1.06e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 88.25  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  247 DAFNKTGT-DYPRDTTIHRLFEEQAERRPDAVAVTFED---------RQLTYGELNERANRLARTLRNAGVQADQlVGLM 316
Cdd:PRK07769    7 NPFDVNGKiRFPPNTNLVRHVERWAKVRGDKLAYRFLDfsterdgvaRDLTWSQFGARNRAVGARLQQVTKPGDR-VAIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  317 VERSLEMIVGIMGILKAGGAYVPI-DPEYP--EERIRYMLEDSGTQVLLSQGHLQERV---------------------- 371
Cdd:PRK07769   86 APQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVrkffrarpakerprviavdavp 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  372 -SFSGTWIRLDdeeAYHEDgsnlesvngpehLTYVIYTSGTTGKPKGNLTTHRNI-IRVVKNTNYIDVTGQDKLLQ-LSS 448
Cdd:PRK07769  166 dEVGATWVPPE---ANEDT------------IAYLQYTSGSTRIPAGVQITHLNLpTNVLQVIDALEGQEGDRGVSwLPF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  449 YSFDGSTFDIFGALLNG-------AKLVLVPKETVLDVAKLAGLIEKQqISVM----FITTAFFNVLVDMNPDC-LRHAR 516
Cdd:PRK07769  231 FHDMGLITVLLPALLGHyitfmspAAFVRRPGRWIRELARKPGGTGGT-FSAApnfaFEHAAARGLPKDGEPPLdLSNVK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  517 AILFGGERVSVSHVRK---ALGHLG--PGKIKHVYGPTESTVFATS-----------YDVHEVEEG-AVSIPIGGP---- 575
Cdd:PRK07769  310 GLLNGSEPVSPASMRKfneAFAPYGlpPTAIKPSYGMAEATLFVSTtpmdeeptviyVDRDELNAGrFVEVPADAPnava 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  576 --------ISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFAD---NPFAP--------GERMYRTG 636
Cdd:PRK07769  390 qvsagkvgVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNilkSRLSEshaegapdDALWVRTG 469
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928  637 DLARWLpDGTIEYVGRIDDQVKIRGFRIELGEIEAhllkleAIEKATVVVRESangekqlcayYVADRSLPANE 710
Cdd:PRK07769  470 DYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEY------TAQEATKALRTG----------YVAAFSVPANQ 526
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
7585-7925 1.07e-16

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 87.54  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7585 PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFD---ASCWeiFKALFFGATLYI-PAK 7660
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDmglIAFH--LAPLIAGMNQYLmPTR 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7661 DTILDYPLFESYMNENGITAaILPPTYAIYLSPDR----------LPSLKKLITGGSAASVEFVQQWKDKVRYFN----- 7725
Cdd:cd05908   183 LFIRRPILWLKKASEHKATI-VSSPNFGYKYFLKTlkpekandwdLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrna 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7726 ---AYGPTEASI-VTSVWAASP--------DGLD---------------LRSVPIGRPIANHQIFIVDSQNHMLPVGVAG 7778
Cdd:cd05908   262 ilpVYGLAEASVgASLPKAQSPfktitlgrRHVThgepepevdkkdsecLTFVEVGKPIDETDIRICDEDNKILPDGYIG 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7779 ELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLArWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIA 7858
Cdd:cd05908   342 HIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELE 414
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 7859 SVQETIVIARG--DANGQQQLCAYFV-----ADRELTVSELRGTLSQELPGYMIpSYFVQLEQMPLTPNGKIDR 7925
Cdd:cd05908   415 GVELGRVVACGvnNSNTRNEEIFCFIehrksEDDFYPLGKKIKKHLNKRGGWQI-NEVLPIRRIPKTTSGKVKR 487
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3993-4337 1.08e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 86.00  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3993 PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDrvVQFASLSF---DASCWEIFKALFFGATLYIPTST 4069
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDD--VLLCGLPLfhvNGSVVTLLTPLASGAHVVLAGPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4070 TILDYPLFESY---MNENGITATILPPT-YAAYL----NPDrMPSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTE 4139
Cdd:cd05944    79 GYRNPGLFDNFwklVERYRITSLSTVPTvYAALLqvpvNAD-ISSLRFAMSGAAPLPVELRARFEDAtgLPVVEGYGLTE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4140 ASIVTSI-WDEASDSLGdrkSVPIGRPLANHRIYVVDSHNRML---PVGVAGELCISGVGLARGYLNRpELTAEKFVDnp 4215
Cdd:cd05944   158 ATCLVAVnPPDGPKRPG---SVGLRLPYARVRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVA-- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4216 fepgERMYRTGDLVRWLPDGNLEYLGRIDHQVkIR-GYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAY--FVA 4292
Cdd:cd05944   232 ----DGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYvqLKP 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 386647928 4293 QRELTAAELRATMSQELPNY-MIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05944   307 GAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
5032-5382 1.14e-16

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 85.78  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5032 DLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpKDDRID 5111
Cdd:cd17635     2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT--GGENTT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5112 PARLHYWISEEKITIFESTPALiipfmdyvaehgldMSSMVLLITSSDScSVTDYRVLQerFGSQF-------------- 5177
Cdd:cd17635    80 YKSLFKILTTNAVTTTCLVPTL--------------LSKLVSELKSANA-TVPSLRLIG--YGGSRaiaadvrfieatgl 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5178 -RIINAYGVTEAAIDSSL-YDEplaKLPEAGNVpiGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELT 5255
Cdd:cd17635   143 tNTAQVYGLSETGTALCLpTDD---DSIEINAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERT 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5256 EEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLC 5335
Cdd:cd17635   218 AEVLIDGWV-------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVG 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 5336 AHFTAESEL---KLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDR 5382
Cdd:cd17635   291 LAVVASAELdenAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2937-3244 1.21e-16

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 87.05  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2937 WFFEpQFAEPHHFNQSVMLHR-RDGFDEAAIRKVLQKLVEHHDALRVVFHKSENG-YTAWnraIGEGELYGLEVVDLK-G 3013
Cdd:cd19539    12 WFID-QGEDGGPAYNIPGAWRlTGPLDVEALREALRDVVARHEALRTLLVRDDGGvPRQE---ILPPGPAPLEVRDLSdP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3014 IEESAQAVEAKANEIQSSI-DLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFPA 3091
Cdd:cd19539    88 DSDRERRLEELLRERESRGfDLDEEPPIRAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3092 KTDAYRTWSEQLAAYAQSPVIERELAYW-KRVAQTEVQPLPKDEQVDVSLQQDSESISIEWTREETEQlLKGVHRAYNTE 3170
Cdd:cd19539   168 LRQQYKEYAAWQREALAAPRAAELLDFWrRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAA-LRELAKRARSS 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 3171 MNDILLAALGMAVQKWSGLDRVLVNLEGHGResimTDIDITRTVGWFTSKYPVVLELEQGKDISYLLKKTKEDL 3244
Cdd:cd19539   247 LFMVLLAAYCVLLRRYTGQTDIVVGTPVAGR----NHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL 316
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
2368-2814 1.29e-16

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 87.02  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2368 GQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLL 2447
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2448 AqrrlqervsfagtvvtvddeqayagdgsnlesavgpnDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQD 2527
Cdd:cd05940    81 V-------------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2528 RVVQFASLSFDAS---CWEvfQTLFFGATLYIPTKETILDYqWFE----------------RYMsdngittATLPPtyaV 2588
Cdd:cd05940   124 VLYTCLPLYHSTAlivGWS--ACLASGATLVIRKKFSASNF-WDDirkyqatifqyigelcRYL-------LNQPP---K 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2589 YLNPDHmpDFKRLIAAGSASSLellqqWKDKVKYFNA------YGPTEDSIctTIWTPSTEDISQLKSVPIGGPIVNHRI 2662
Cdd:cd05940   191 PTERKH--KVRMIFGNGLRPDI-----WEEFKERFGVpriaefYAATEGNS--GFINFFGKPGAIGRNPSLLRKVAPLAL 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2663 YIVDAHYQ-----------PVPVGVAGELC--IAGVGLARGYLNrPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIE 2729
Cdd:cd05940   262 VKYDLESGepirdaegrciKVPRGEPGLLIsrINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWY 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2730 YLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIV--IAHDDASGQKQLCAYFVADRTMTVGE-LRGELSGELPGYMIP 2806
Cdd:cd05940   341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLQPNEEFDLSaLAAHLEKNLPGYARP 420

                  ....*...
gi 386647928 2807 AhFVQLER 2814
Cdd:cd05940   421 L-FLRLQP 427
PLN03102 PLN03102
acyl-activating enzyme; Provisional
4893-5385 1.31e-16

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 87.77  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4893 FEKQA-ECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 4971
Cdd:PLN03102   19 FLKRAsECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4972 PSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQA-------ALCLDDEAAYAEDAS---------------------N 5023
Cdd:PLN03102   99 DATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSedsnlnlPVIFIHEIDFPKRPSseeldyecliqrgeptpslvaR 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5024 VANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFV---GDIARtlynGGT 5100
Cdd:PLN03102  179 MFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTftwGTAAR----GGT 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5101 MViCPKddRIDPARLHYWISEEKITIFESTPALiipFMDYVAEHGLDMS---SMVLLITSSDSCSVTDYRVLQeRFGsqF 5177
Cdd:PLN03102  255 SV-CMR--HVTAPEIYKNIEMHNVTHMCCVPTV---FNILLKGNSLDLSprsGPVHVLTGGSPPPAALVKKVQ-RLG--F 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5178 RIINAYGVTEAA--IDSSLYDEPLAKLPEAGNVPIG--KAALNAKFYIVDAH----LNPVPVG--VLGELCIGGIGVARG 5247
Cdd:PLN03102  326 QVMHAYGLTEATgpVLFCEWQDEWNRLPENQQMELKarQGVSILGLADVDVKnketQESVPRDgkTMGEIVIKGSSIMKG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5248 YLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED 5327
Cdd:PLN03102  406 YLKNPKATSEAFKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPH 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5328 AKGQKVLCAHFTAE-SELKLSELRSSL-----------SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PLN03102  479 PTWGETPCAFVVLEkGETTKEDRVDKLvtrerdlieycRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
4911-5308 1.37e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 87.74  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4911 DRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLt 4990
Cdd:PRK07768   28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGM- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4991 qthLQERAQQWGQTLQAALCLDDEAAY---------AEDASNVANVNEpHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA 5061
Cdd:PRK07768  107 ---IGAKAVVVGEPFLAAAPVLEEKGIrvltvadllAADPIDPVETGE-DDLALMQLTSGSTGSPKAVQITHGNLYANAE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5062 GYRREYRLDQFPVRLLQLASFSFDV-FVGDIARTLYNGGTMV-ICPKDDRIDP---ARLhywISEEKITIfESTP----A 5132
Cdd:PRK07768  183 AMFVAAEFDVETDVMVSWLPLFHDMgMVGFLTVPMYFGAELVkVTPMDFLRDPllwAEL---ISKYRGTM-TAAPnfayA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5133 LIIPFMDYVAEHG-LDMSSMVLLITSSDSCSVTDYRVLQE---RFGsqFR---IINAYGVTEAAIDSSL--------YDE 5197
Cdd:PRK07768  259 LLARRLRRQAKPGaFDLSSLRFALNGAEPIDPADVEDLLDagaRFG--LRpeaILPAYGMAEATLAVSFspcgaglvVDE 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5198 PLAKLPEAGN--VPIGKAALNA-----------KFYIVDAHLNPVPVGVLGELCIGGIGVARGYlnrpeLTEEKFVdsPF 5264
Cdd:PRK07768  337 VDADLLAALRraVPATKGNTRRlatlgpplpglEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFI--PA 409
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 386647928 5265 VEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIE 5308
Cdd:PRK07768  410 QDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
4897-5291 1.45e-16

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 88.01  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4897 AECTPEAAAVVYEND-----RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 4971
Cdd:PRK08180   49 AQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4972 ---PSD--RIQFMLEdsaasvLLTQTHL-QERAQQWGQTLQAALCLDDEAAYAEDASN---------------VANVNE- 5029
Cdd:PRK08180  129 slvSQDfgKLRHVLE------LLTPGLVfADDGAAFARALAAVVPADVEVVAVRGAVPgraatpfaallatppTAAVDAa 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 -----PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYR-LDQFPVRLLQLASFSfDVFVG--DIARTLYNGGTM 5101
Cdd:PRK08180  203 haavgPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfLAEEPPVLVDWLPWN-HTFGGnhNLGIVLYNGGTL 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5102 VICpkDDRIDPARLhywisEEKI--------TIFESTPA---LIIPFM---DYVAEHGLDMSSMVLLITSSDSCSVTD-- 5165
Cdd:PRK08180  282 YID--DGKPTPGGF-----DETLrnlreispTVYFNVPKgweMLVPALerdAALRRRFFSRLKLLFYAGAALSQDVWDrl 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5166 YRVLQERFGSQFRIINAYGVTEAAIDSSLYDEPLAKlpeAGNVPIGKAALNAKFyivdahlnpVPVGVLGELCIGGIGVA 5245
Cdd:PRK08180  355 DRVAEATCGERIRMMTGLGMTETAPSATFTTGPLSR---AGNIGLPAPGCEVKL---------VPVGGKLEVRVKGPNVT 422
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 5246 RGYLNRPELTEEKFVDspfvEGerLYRTGDLARWM----PDGNVDFIGRI 5291
Cdd:PRK08180  423 PGYWRAPELTAEAFDE----EG--YYRSGDAVRFVdpadPERGLMFDGRI 466
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
5945-6420 1.57e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 87.44  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTF--EDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPED 6022
Cdd:PRK13391    7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6023 RIRYMLEDSGAKLLLVQGHLLDRASFADKL-------VNLNDDGA------YHEDGSNLEPVNGPEHL--TYVIYTSGTT 6087
Cdd:PRK13391   87 EAAYIVDDSGARALITSAAKLDVARALLKQcpgvrhrLVLDGDGElegfvgYAEAVAGLPATPIADESlgTDMLYSSGTT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6088 GRPKGVMVEHRNvVRLVKNTNYVEL-------NEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVRNetiLDAVSLKNA 6160
Cdd:PRK13391  167 GRPKGIKRPLPE-QPPDTPLPLTAFlqrlwgfRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEH---FDAEQYLAL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6161 IQQYGI-NTMWLTAPLYNQL----SQQDSGMFAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTENTTFStthTI 6235
Cdd:PRK13391  243 IEEYGVtHTQLVPTMFSRMLklpeEVRDKYDLSSLEVAIHAAAPCP-PQVKEQMIDWWGPIIHEYYAATEGLGFT---AC 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6236 VGEQKEAVP--IGKPInNSTAYIVDSKLSLLPVGVWGELIVGGdGVARGYLNRPELTAEkfvesSFLPGERCYRTGDLAR 6313
Cdd:PRK13391  319 DSEEWLAHPgtVGRAM-FGDLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAE-----ARHPDGTWSTVGDIGY 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6314 WLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQK-----QLCAYFVAERELTiGELRAA 6387
Cdd:PRK13391  392 VDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFgVPNEDLGEEvkavvQPVDGVDPGPALA-AELIAF 470
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 6388 LSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PRK13391  471 CRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
2338-2824 1.66e-16

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 88.48  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2338 AADYeaDKTIHQLFEEQAERI-PDHPAVV-FEGQQLTYRELNERANRLARTLQAlGVKTDQPVGLMLERSLEMVVGMFAV 2415
Cdd:PRK06814  626 TSDY--DRTLFEALIEAAKIHgFKKLAVEdPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFAL 702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2416 LKAGgaYVPIdpeypedrisyMLEDSS-----------AQV--------LLAQRRLQERV---SFAGTVVTVDDEQAYAG 2473
Cdd:PRK06814  703 QSAG--RVPA-----------MINFSAgianilsackaAQVktvltsraFIEKARLGPLIealEFGIRIIYLEDVRAQIG 769
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2474 DGSNLESAVG------------PNDLAYIIYTSGTTGKPKGVMVEHhglcslKQMFANTLQI------NAQDRVvqFASL 2535
Cdd:PRK06814  770 LADKIKGLLAgrfplvyfcnrdPDDPAVILFTSGSEGTPKGVVLSH------RNLLANRAQVaaridfSPEDKV--FNAL 841
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2536 SfdascweVFQTlfFGAT--LYIPTKETI--------LDYQWFERYMSDNGIT----TATLPPTYAVYLNPdhmPDFK-- 2599
Cdd:PRK06814  842 P-------VFHS--FGLTggLVLPLLSGVkvflypspLHYRIIPELIYDTNATilfgTDTFLNGYARYAHP---YDFRsl 909
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2600 RLIAAGsASSL--ELLQQWKDK--VKYFNAYGPTEDSICTTIWTPSTediSQLKSVPIGGPIVNHRIyivdahyQPVPvG 2675
Cdd:PRK06814  910 RYVFAG-AEKVkeETRQTWMEKfgIRILEGYGVTETAPVIALNTPMH---NKAGTVGRLLPGIEYRL-------EPVP-G 977
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2676 V--AGELCIAGVGLARGYLNrpdltaekfVDNPF---EPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEI 2750
Cdd:PRK06814  978 IdeGGRLFVRGPNVMLGYLR---------AENPGvlePPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAV 1048
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2751 EE--------QLLKVASVQ-----EAIVIAHDDASG-QKQLCAYFvadRTMTVGELrgelsgelpgyMIPAHFVQLERMP 2816
Cdd:PRK06814 1049 EElaaelwpdALHAAVSIPdarkgERIILLTTASDAtRAAFLAHA---KAAGASEL-----------MVPAEIITIDEIP 1114

                  ....*...
gi 386647928 2817 LTPNGKID 2824
Cdd:PRK06814 1115 LLGTGKID 1122
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
6080-6416 1.73e-16

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 85.05  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6080 VIYTSGTTGRPKGVMVEHRNVvrLVKNTNYV---ELNEQTHILQTGAVVFDASTFEIWGALLNGGR-LYVVRnetiLDAV 6155
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQAL--LAQALVLAvlqAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTnVFVRR----VDAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6156 SLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTLIVG------GDVLSVPhinrvlrEHAGLSIVNGYGPTENTTF 6229
Cdd:cd17636    79 EVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSpaapewNDMATVD-------TSPWGRKPGGYGQTEVMGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6230 STTHTIVGEQKEAVpiGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVessflpgERCYRTG 6309
Cdd:cd17636   152 ATFAALGGGAIGGA--GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GGWHHTN 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6310 DLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE--RELTIGELRAA 6387
Cdd:cd17636   223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKpgASVTEAELIEH 302
                         330       340
                  ....*....|....*....|....*....
gi 386647928 6388 LSQELPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:cd17636   303 CRARIASYKKPKSVEFADALPRTAGGADD 331
PRK08308 PRK08308
acyl-CoA synthetase; Validated
7809-7932 1.79e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 86.24  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7809 AGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFVADRELT 7888
Cdd:PRK08308  288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID 367
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 386647928 7889 VSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPAPE 7932
Cdd:PRK08308  368 PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
PLN02479 PLN02479
acetate-CoA ligase
5940-6422 1.99e-16

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 87.21  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5940 LFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDY 6019
Cdd:PLN02479   25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6020 PEDRIRYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDGAYHEDGSNL--EPVNGPEHLTYVI---------------- 6081
Cdd:PLN02479  105 NAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSSFKPPLLIVigDPTCDPKSLQYALgkgaieyekfletgdp 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6082 -----------------YTSGTTGRPKGVMVEHRnvvrlvkntnyvelneqthilqtGAVVFDASTFEIWGalLNGGRLY 6144
Cdd:PLN02479  185 efawkppadewqsialgYTSGTTASPKGVVLHHR-----------------------GAYLMALSNALIWG--MNEGAVY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6145 V--------------------VRNETILDAVSLK---NAIQQYGInTMWLTAPLYnqlsqqdsgmfagLKTLI---VGGD 6198
Cdd:PLN02479  240 LwtlpmfhcngwcftwtlaalCGTNICLRQVTAKaiySAIANYGV-THFCAAPVV-------------LNTIVnapKSET 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6199 VLSVPHINRVLREHA-------------GLSIVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNS---TAYI------ 6256
Cdd:PLN02479  306 ILPLPRVVHVMTAGAapppsvlfamsekGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNArqgVRYIglegld 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6257 -VDSKlSLLPV----GVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYKGRIDEQVK 6331
Cdd:PLN02479  386 vVDTK-TMKPVpadgKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWF-------HSGDLGVKHPDGYIEIKDRSKDIII 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6332 IRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAyFVAERELTIGELRAALSQE--------LPNYMIPSHFV- 6402
Cdd:PLN02479  458 SGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCA-FVTLKPGVDKSDEAALAEDimkfcrerLPAYWVPKSVVf 536
                         570       580
                  ....*....|....*....|.
gi 386647928 6403 -PLermPLTPNGKIDRRALPA 6422
Cdd:PLN02479  537 gPL---PKTATGKIQKHVLRA 554
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
3864-4337 2.00e-16

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 86.66  E-value: 2.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRi 3943
Cdd:cd05929     2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAE- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 rymledsgAQALLTQRHLRERVSFAGTFVAVDDEQAYHA--DGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCS 4021
Cdd:cd05929    81 --------ACAIIEIKAAALVCGLFTGGGALDGLEDYEAaeGGSPETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4022 ---LKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPT---STTILDypLFESYmnenGITATILPPT- 4094
Cdd:cd05929   153 dndTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEkfdPEEFLR--LIERY----RVTFAQFVPTm 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4095 -------YAAYLNPDRMPSLKKLITGGSAASVEFVQQWKD---KVLYfNAYGPTEASIVTSIwdEASDSLGDRKSVpiGR 4164
Cdd:cd05929   227 fvrllklPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDwggPIIW-EYYGGTEGQGLTII--NGEEWLTHPGSV--GR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4165 PLANhRIYVVDSHNRMLPVGVAGELCISGvGLARGYLNRPELTAEKFvdnpfepGERMYRT-GDLVRWLPDGNLEYLGRI 4243
Cdd:cd05929   302 AVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAAR-------NEGGWSTlGDVGYLDEDGYLYLTDRR 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4244 DHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYF------VAQRELtAAELRATMSQELPNYMIPSY 4317
Cdd:cd05929   373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapgaDAGTAL-AEELIAFLRDRLSRYKCPRS 451
                         490       500
                  ....*....|....*....|
gi 386647928 4318 FVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05929   452 IEFVAELPRDDTGKLYRRLL 471
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
3879-4243 2.02e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 87.41  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3879 QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY---PED--RIRYMLE----- 3948
Cdd:PRK12582   80 KVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmSHDhaKLKHLFDlvkpr 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3949 ----DSGAQ---ALLTQRHL-------------RERVSF---AGTFVAVDDEQAYHAdgsnlepvVGPNHLAYVIYTSGT 4005
Cdd:PRK12582  160 vvfaQSGAPfarALAALDLLdvtvvhvtgpgegIASIAFadlAATPPTAAVAAAIAA--------ITPDTVAKYLFTSGS 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4006 TGKPKGVMVEHHglcslklMFANTLQMTEQdrVVQFA-----SLSFDASCWE-------IFKALFF-GATLYI----PT- 4067
Cdd:PRK12582  232 TGMPKAVINTQR-------MMCANIAMQEQ--LRPREpdpppPVSLDWMPWNhtmggnaNFNGLLWgGGTLYIddgkPLp 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4068 ---STTILDypLFEsymnengitatILPPTY----AAY--LNP--DRMPSLKK--------LITGGSAASVEFVQQWKD- 4127
Cdd:PRK12582  303 gmfEETIRN--LRE-----------ISPTVYgnvpAGYamLAEamEKDDALRRsffknlrlMAYGGATLSDDLYERMQAl 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4128 -------KVLYFNAYGPTEAS--IVTSIWDEASDSLgdrksvpIGRPLANHRIyvvdshnRMLPVGVAGELCISGVGLAR 4198
Cdd:PRK12582  370 avrttghRIPFYTGYGATETAptTTGTHWDTERVGL-------IGLPLPGVEL-------KLAPVGDKYEVRVKGPNVTP 435
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 4199 GYLNRPELTAEKFVDNPFepgermYRTGDLVRWL----PDGNLEYLGRI 4243
Cdd:PRK12582  436 GYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGRV 478
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
1294-1701 2.14e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 87.48  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1294 PENEVFHALFEKQAERTPEVAA---VVYENDR------LTYRELNERaNRlARMLRAQGV-KPNQLVGILADRSADLLVG 1363
Cdd:PRK07769   18 PPNTNLVRHVERWAKVRGDKLAyrfLDFSTERdgvardLTWSQFGAR-NR-AVGARLQQVtKPGDRVAILAPQNLDYLIA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1364 ALAVWKAGGAYVPL-DPDYP--SDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQA-----VLCLD---DEAAyaedAS 1432
Cdd:PRK07769   96 FFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAkerprVIAVDavpDEVG----AT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1433 NVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLvntaagyrreyrldqfPVRLLQLASfSFDVFVGDIART---LYN-- 1507
Cdd:PRK07769  172 WVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNL----------------PTNVLQVID-ALEGQEGDRGVSwlpFFHdm 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1508 GGTMVICPK--DDRI---DPA----RLHYWISE------EKITIFESTPALIipfMDYVAEHG--------LDMSSMELL 1564
Cdd:PRK07769  235 GLITVLLPAllGHYItfmSPAafvrRPGRWIRElarkpgGTGGTFSAAPNFA---FEHAAARGlpkdgeppLDLSNVKGL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1565 ITSSDSCSVTDYRVLQERFG----SQFRIINAYGVTEAAIDSS---LYDEP---------LAK------LPEAGN----V 1618
Cdd:PRK07769  312 LNGSEPVSPASMRKFNEAFApyglPPTAIKPSYGMAEATLFVSttpMDEEPtviyvdrdeLNAgrfvevPADAPNavaqV 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1619 PIGKAALNAKFYIVDAH-LNPVPVGVLGELCIGGIGVARGYLNRPELTEEKF---VDSPFVE--------GERLYRTGDL 1686
Cdd:PRK07769  392 SAGKVGVSEWAVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSEshaegapdDALWVRTGDY 471
                         490
                  ....*....|....*
gi 386647928 1687 ARWMpDGNVDFIGRI 1701
Cdd:PRK07769  472 GVYF-DGELYITGRV 485
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
3875-4333 2.17e-16

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 88.10  E-value: 2.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3875 FEKSQLTYGELNERANRLARTLRDaGVRPDQLVGLMVERSLEMVVGIMAIMKAGgayipidpeypedRIRYMLE-DSGAQ 3953
Cdd:PRK06814  654 PVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAG-------------RVPAMINfSAGIA 719
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3954 ALL------------TQRHLRER---------VSFAGTFVAVDDEQAYHADGSNLEPVVG------------PNHLAYVI 4000
Cdd:PRK06814  720 NILsackaaqvktvlTSRAFIEKarlgplieaLEFGIRIIYLEDVRAQIGLADKIKGLLAgrfplvyfcnrdPDDPAVIL 799
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4001 YTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVvqFASLSfdascweIFKAlfFGAT--LYIPTSTTILDY---- 4074
Cdd:PRK06814  800 FTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKV--FNALP-------VFHS--FGLTggLVLPLLSGVKVFlyps 868
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4075 PLFESYMNE--NGITATILPPT------YAAYLNPDRMPSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEASIVT 4144
Cdd:PRK06814  869 PLHYRIIPEliYDTNATILFGTdtflngYARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKfgIRILEGYGVTETAPVI 948
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4145 SIWDEASDSLGdrkSVpiGR--PLANHRiyvvdshnrMLPV-GV--AGELCISGVGLARGYLNrpeltaekfVDNPF--- 4216
Cdd:PRK06814  949 ALNTPMHNKAG---TV--GRllPGIEYR---------LEPVpGIdeGGRLFVRGPNVMLGYLR---------AENPGvle 1005
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4217 EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVaYFVAQREL 4296
Cdd:PRK06814 1006 PPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERII-LLTTASDA 1084
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 386647928 4297 TAAELRATMSQE-LPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:PRK06814 1085 TRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
2371-2772 2.18e-16

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 86.89  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGgayVPIDPEYP---EDRISYMLEDSSAQvll 2447
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECS--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2448 aqrrlqervsfagTVVTvddeqayagDGSnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCS--LKQMFANTLQINA 2525
Cdd:cd17639    80 -------------AIFT---------DGK-------PDDLACIMYTSGSTGNPKGVMLTHGNLVAgiAGLGDRVPELLGP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2526 QDRVVQFASLS--FDASCWEVFqtLFFGATLYIPTKETILDyqwfERYMSDNGITTAtLPPTY-----AVY--------- 2589
Cdd:cd17639   131 DDRYLAYLPLAhiFELAAENVC--LYRGGTIGYGSPRTLTD----KSKRGCKGDLTE-FKPTLmvgvpAIWdtirkgvla 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2590 -LNPdhMPDFKRLIAAGS-ASSLELLQQWKD------------------KVKYF-----------------------NAY 2626
Cdd:cd17639   204 kLNP--MGGLKRTLFWTAyQSKLKALKEGPGtplldelvfkkvraalggRLRYMlsggaplsadtqeflnivlcpviQGY 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2627 GPTEDSICTTI-----WTPST-------EDIsQLKSVPIGGpivnhriYIVDAhyqPVPvgvAGELCIAGVGLARGYLNR 2694
Cdd:cd17639   282 GLTETCAGGTVqdpgdLETGRvgpplpcCEI-KLVDWEEGG-------YSTDK---PPP---RGEILIRGPNVFKGYYKN 347
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2695 PDLTAEKFVdnpfepGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIR-GYRIELGEIEEQLLKVASVQEAIVIAHDDAS 2772
Cdd:cd17639   348 PEKTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKS 420
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
6992-7411 2.21e-16

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 86.15  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6992 LTPMQKgmWFHtALDKEAGAYFEQ-MRFTVQGSLDAEQFARSWNDLVARHAILRTNFFSGPRGepLQIVYRD---KRIGF 7067
Cdd:cd19534     4 LTPIQR--WFF-EQNLAGRHHFNQsVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGG--WQQRIRGdveELFRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7068 VYEDLSHLPADERqasVERLEQEdIARGFDLEQDALVRVAVIRTQETSYRVLWSFHHILMDG--WclPLVVKELfETyeA 7145
Cdd:cd19534    79 EVVDLSSLAQAAA---IEALAAE-AQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsW--RILLEDL-EA--A 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7146 YVQGDRPEQKAAPAYSQYIEWLENQDSAAAS-------AYWSNYLAG-YEGqtaLP--QEKAQKRsegyvAEHVVCELDK 7215
Cdd:cd19534   150 YEQALAGEPIPLPSKTSFQTWAELLAEYAQSpalleelAYWRELPAAdYWG---LPkdPEQTYGD-----ARTVSFTLDE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7216 ELSERMNRAAKQ-CRVTVNTLMQAVWGVILQKYNATDDVvygsVVS----GRPAEIPGIE--EMIGLFINTIPVRVACQP 7288
Cdd:cd19534   222 EETEALLQEANAaYRTEINDLLLAALALAFQDWTGRAPP----AIFleghGREEIDPGLDlsRTVGWFTSMYPVVLDLEA 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7289 EESFADVMGRMQE------------------AALESGRYDFYPLYEI------QTQSAQKQELinhLLVFEnypmdeqVE 7344
Cdd:cd19534   298 SEDLGDTLKRVKEqlrripnkgigygilrylTPEGTKRLAFHPQPEIsfnylgQFDQGERDDA---LFVSA-------VG 367
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7345 QAGGDDSGTL-SITDVDVaehtnyNFTVTvfpGDEIVVRFDYNSFVFERADMERLKGHLLHMLEQIVA 7411
Cdd:cd19534   368 GGGSDIGPDTpRFALLDI------NAVVE---GGQLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
7467-7928 2.72e-16

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 86.33  E-value: 2.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7467 FENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAyvpidPEYpedrIRYMLEDSGaq 7545
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF----INYNLSGDP-- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7546 vlltqrhLQECVSFDG-KVIAADDEQaygedgsnlepvvgpnhLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRI 7624
Cdd:cd05937    70 -------LIHCLKLSGsRFVIVDPDD-----------------PAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7625 TEEDRV-----VQFASLSFDASCweifKALFFGATLYIPAK--------DTILDYPLFESYMNENGITAAILPPtyaiyl 7691
Cdd:cd05937   126 KNGDRTytcmpLYHGTAAFLGAC----NCLMSGGTLALSRKfsasqfwkDVRDSGATIIQYVGELCRYLLSTPP------ 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7692 SP-DRLPSLKKLITGGSAASVefvqqWKDKVRYFNA------YGPTEASIVTSVWAASPDGLDL--RSVPIGRPIANHQI 7762
Cdd:cd05937   196 SPyDRDHKVRVAWGNGLRPDI-----WERFRERFNVpeigefYAATEGVFALTNHNVGDFGAGAigHHGLIRRWKFENQV 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7763 FIV--DSQNHM------------LPVGVAGELCI----SGAGLARGYLNRPELTAEKFVDNPFLAGERMYRTGDLARWLP 7824
Cdd:cd05937   271 VLVkmDPETDDpirdpktgfcvrAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDA 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7825 DGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIV--IARGDANGQQQLCAYFVADR-----ELTVSELRGTLS 7897
Cdd:cd05937   351 DGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESsavptEFTKSLLASLAR 430
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 7898 QELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05937   431 KNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2937-3131 2.80e-16

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 85.59  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2937 WFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHKSENGYTAWnRAIGEGELYGLEVVDLkgieE 3016
Cdd:cd19532    12 WFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPM-QGVLASSPLRLEHVQI----S 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3017 SAQAVEAKANEIQSSI-DLEAGPFVKAGLFQCADGDHLLIV-IHHGVVDGVSWRILLEDLAIGYEqavkGEELRFPAKTd 3094
Cdd:cd19532    87 DEAEVEEEFERLKNHVyDLESGETMRIVLLSLSPTEHYLIFgYHHIAMDGVSFQIFLRDLERAYN----GQPLLPPPLQ- 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 386647928 3095 aYRTWSE-QLAAYaQSPVIERELAYWKRVAQTEVQPLP 3131
Cdd:cd19532   162 -YLDFAArQRQDY-ESGALDEDLAYWKSEFSTLPEPLP 197
PRK09192 PRK09192
fatty acyl-AMP ligase;
4913-5065 2.91e-16

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 86.98  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP-------SDRIQFMLEDSAA 4985
Cdd:PRK09192   50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQP 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4986 SVLLTQTHLQERAQQWGQTLQAALCLDDEAAYAEDASNVA-NVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYR 5064
Cdd:PRK09192  130 AAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVAlPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIS 209

                  .
gi 386647928 5065 R 5065
Cdd:PRK09192  210 H 210
PRK07867 PRK07867
acyl-CoA synthetase; Validated
2343-2830 2.92e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 86.66  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2343 ADKTIHQLFEEQAEriPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQP-VGLMLERSLEMVVGMFAVLKAGGA 2421
Cdd:PRK07867    3 SAPTVAELLLPLAE--DDDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2422 YVPIDPEYPEDRISYMLEDSSAQVLL---AQRRLQERVSFAGTVVTVDDEQ------AYAGDGSNLeSAVGPNDLAYIIY 2492
Cdd:PRK07867   81 PVGLNPTRRGAALARDIAHADCQLVLtesAHAELLDGLDPGVRVINVDSPAwadelaAHRDAEPPF-RVADPDDLFMLIF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2493 TSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDrvVQFASLSFDAS-----CWEVfqTLFFGATLYIPTKetildyqw 2567
Cdd:PRK07867  160 TSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD--VCYVSMPLFHSnavmaGWAV--ALAAGASIALRRK-------- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2568 F--ERYMSD---NGITTATL---PPTY--AVYLNPDHMPDFKRLIAA--GSASSLELLQQWKDkVKYFNAYGPTEDSICT 2635
Cdd:PRK07867  228 FsaSGFLPDvrrYGATYANYvgkPLSYvlATPERPDDADNPLRIVYGneGAPGDIARFARRFG-CVVVDGFGSTEGGVAI 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2636 TiWTPSTedisqlksvPIG--GPIVNHrIYIVDAHY-QPVPVGVA------------GELC-IAGVGLARGYLNRPDLTA 2699
Cdd:PRK07867  307 T-RTPDT---------PPGalGPLPPG-VAIVDPDTgTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADA 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2700 EKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCA 2779
Cdd:PRK07867  376 ERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMA 448
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 2780 YFVA--DRTMTVGELRGELSG--ELPGYMIPAHFVQLERMPLTPNGKIDRKALPA 2830
Cdd:PRK07867  449 ALVLapGAKFDPDAFAEFLAAqpDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
1446-1699 2.93e-16

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 84.28  E-value: 2.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1446 VIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIArTLYNGGTMVICPkddRIDPARL 1525
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLA-TFHAGGTNVFVR---RVDAEEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1526 HYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDyrVLQERFGSQFRiinAYGVTEAAIDSSLy 1605
Cdd:cd17636    81 LELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMAT--VDTSPWGRKPG---GYGQTEVMGLATF- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1606 deplAKLPEAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegeRLYRTGD 1685
Cdd:cd17636   155 ----AALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GWHHTND 223
                         250
                  ....*....|....
gi 386647928 1686 LARWMPDGNVDFIG 1699
Cdd:cd17636   224 LGRREPDGSLSFVG 237
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
4913-5291 3.04e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 87.09  E-value: 3.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERaNRlARTLRAQGV-KPNQLVGILADRSADLLVGALAVWKAGGAYVPL-DPDYP--SDRIQFMLEDSAASVL 4988
Cdd:PRK07769   56 LTWSQFGAR-NR-AVGARLQQVtKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAI 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4989 LTQTHLQERAQQWGQTLQAAlclDDEAAYAEDA--SNVANVNEP-----HDLAYVIYTSGTTGRPKGVMIEHRSLvntaa 5061
Cdd:PRK07769  134 LTTTDSAEGVRKFFRARPAK---ERPRVIAVDAvpDEVGATWVPpeaneDTIAYLQYTSGSTRIPAGVQITHLNL----- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5062 gyrreyrldqfPVRLLQLASfSFDVFVGDIART---LYN--GGTMVICPK--DDRI---DPA----RLHYWISE------ 5121
Cdd:PRK07769  206 -----------PTNVLQVID-ALEGQEGDRGVSwlpFFHdmGLITVLLPAllGHYItfmSPAafvrRPGRWIRElarkpg 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5122 EKITIFESTPALIipfMDYVAEHG--------LDMSSMVLLITSSDSCSVTDYRVLQERFG----SQFRIINAYGVTEAA 5189
Cdd:PRK07769  274 GTGGTFSAAPNFA---FEHAAARGlpkdgeppLDLSNVKGLLNGSEPVSPASMRKFNEAFApyglPPTAIKPSYGMAEAT 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5190 IDSS---LYDEP---------LAK------LPEAGN----VPIGKAALNAKFYIVDAH-LNPVPVGVLGELCIGGIGVAR 5246
Cdd:PRK07769  351 LFVSttpMDEEPtviyvdrdeLNAgrfvevPADAPNavaqVSAGKVGVSEWAVIVDPEtASELPDGQIGEIWLHGNNIGT 430
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 5247 GYLNRPELTEEKF---VDSPFVE--------GERLYRTGDLARWMpDGNVDFIGRI 5291
Cdd:PRK07769  431 GYWGKPEETAATFqniLKSRLSEshaegapdDALWVRTGDYGVYF-DGELYITGRV 485
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
5030-5385 3.12e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 86.74  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRR--EYRLDQ------FPVRLLQLASFSFDVFVgdiarTLYNGGTM 5101
Cdd:PRK05677  206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRAlmGSNLNEgceiliAPLPLYHIYAFTFHCMA-----MMLIGNHN 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5102 VICPkDDRIDPARLHYwISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIIN 5181
Cdd:PRK05677  281 ILIS-NPRDLPAMVKE-LGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCA--ICE 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5182 AYGVTEAAidsslydePLAKLPEAGNVPIGKAAL---NAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEK 5258
Cdd:PRK05677  357 GYGMTETS--------PVVSVNPSQAIQVGTIGIpvpSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEI 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5259 FVDSPFVegerlyRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHF 5338
Cdd:PRK05677  429 LDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFV 502
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 5339 TAESELKLSE--LRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK05677  503 VVKPGETLTKeqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
3867-4337 3.48e-16

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 86.92  E-value: 3.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3867 NPDAVAVVFEKSQ------LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPI----DP 3936
Cdd:TIGR02188   70 RPDKVAIIWEGDEpgevrkITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVfggfSA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3937 EYPEDRIrymlEDSGAQALLT-------------QRHLRERVSFAGTFV--------------------------AVDDE 3977
Cdd:TIGR02188  150 EALADRI----NDAGAKLVITadeglrggkviplKAIVDEALEKCPVSVehvlvvrrtgnpvvpwvegrdvwwhdLMAKA 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  3978 QAYHAdgsnLEPVvGPNHLAYVIYTSGTTGKPKGVMvehHGLCSLKLMFANTLQMTeqdrvvqfaslsFDASCWEIF--- 4054
Cdd:TIGR02188  226 SAYCE----PEPM-DSEDPLFILYTSGSTGKPKGVL---HTTGGYLLYAAMTMKYV------------FDIKDGDIFwct 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4055 --------------KALFFGATLYIPTSTtiLDYP---LFESYMNENGITATILPPTYAAYL------NPDR--MPSLKK 4109
Cdd:TIGR02188  286 advgwitghsyivyGPLANGATTVMFEGV--PTYPdpgRFWEIIEKHKVTIFYTAPTAIRALmrlgdeWVKKhdLSSLRL 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4110 LITGGSAASVEfvqQWKdkvLYFNAYGPTEASIVTSIWDEASDS--------LGDRKSVPIGRPLANHRIYVVDSHNRML 4181
Cdd:TIGR02188  364 LGSVGEPINPE---AWM---WYYKVVGKERCPIVDTWWQTETGGimitplpgATPTKPGSATLPFFGIEPAVVDEEGNPV 437
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4182 P-VGVAGELCISGV--GLARGYLNRPeltaEKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGE 4258
Cdd:TIGR02188  438 EgPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAE 513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4259 VETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELT-----AAELRATMSQELPNYMIPS--YFVqlAQMPLTPNGK 4331
Cdd:TIGR02188  514 IESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEpddelRKELRKHVRKEIGPIAKPDkiRFV--PGLPKTRSGK 591

                   ....*.
gi 386647928  4332 IDRKAL 4337
Cdd:TIGR02188  592 IMRRLL 597
PRK08308 PRK08308
acyl-CoA synthetase; Validated
2710-2830 3.67e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 85.09  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2710 GERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFVADRTMTV 2789
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP 368
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 386647928 2790 GELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALPA 2830
Cdd:PRK08308  369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
5036-5289 4.27e-16

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 83.89  E-value: 4.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5036 VIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIArTLYNGGTMVICPkddRIDPARL 5115
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLA-TFHAGGTNVFVR---RVDAEEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5116 HYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSmvLLITSSDSCSVTDYRVLQERFGSQFRiinAYGVTEAAIDSSLy 5195
Cdd:cd17636    81 LELIEAERCTHAFLLPPTIDQIVELNADGLYDLSS--LRSSPAAPEWNDMATVDTSPWGRKPG---GYGQTEVMGLATF- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5196 deplAKLPEAGNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDspfvegeRLYRTGD 5275
Cdd:cd17636   155 ----AALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GWHHTND 223
                         250
                  ....*....|....
gi 386647928 5276 LARWMPDGNVDFIG 5289
Cdd:cd17636   224 LGRREPDGSLSFVG 237
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
2366-2828 4.50e-16

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 85.56  E-value: 4.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2366 FEGQQLTYRELNERANRLARTLQ-ALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQ 2444
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2445 VLLaqrrlqervsfagtvvtvddeqayagdgsnlesaVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQIN 2524
Cdd:cd05937    81 FVI----------------------------------VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLK 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2525 AQDRV-----VQFASLSFDASCwevfQTLFFGATLYIPTKETILDYqWFERYmsDNGITTATLPPTYAVYL-----NPDH 2594
Cdd:cd05937   127 NGDRTytcmpLYHGTAAFLGAC----NCLMSGGTLALSRKFSASQF-WKDVR--DSGATIIQYVGELCRYLlstppSPYD 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2595 MpDFKRLIAAGSASSLELLQQWKDKvkyFNA------YGPTEDSIctTIWTPSTEDISqLKSVPIGGPIV----NHRIYI 2664
Cdd:cd05937   200 R-DHKVRVAWGNGLRPDIWERFRER---FNVpeigefYAATEGVF--ALTNHNVGDFG-AGAIGHHGLIRrwkfENQVVL 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2665 V-------DAHYQP-------VPVGVAGELCIA----GVGLARGYLNRPDLTAEKFVDNPFEPGERMYRTGDLAKWLPDG 2726
Cdd:cd05937   273 VkmdpetdDPIRDPktgfcvrAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADG 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2727 TIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA-----HDDASGqkqlCAYFVADR------TMTVGELRGE 2795
Cdd:cd05937   353 RWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvpgHDGRAG----CAAITLEEssavptEFTKSLLASL 428
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 2796 LSGELPGYMIPAhFVQL-ERMPLTPNGKIDRKAL 2828
Cdd:cd05937   429 ARKNLPSYAVPL-FLRLtEEVATTDNHKQQKGVL 461
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
3999-4334 4.58e-16

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 83.86  E-value: 4.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3999 VIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLsFDAScweifkALFFG-ATLYIPTSTTILDYplF 4077
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPL-FHIA------GLNLAlATFHAGGANVVMEK--F 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4078 ESYMNENGITA---TIL---PPTYAAYL-----NPDRMPSLKkLITGGSAAsvEFVQQWKDKV--LYFNAYGPTEASIVT 4144
Cdd:cd17637    76 DPAEALELIEEekvTLMgsfPPILSNLLdaaekSGVDLSSLR-HVLGLDAP--ETIQRFEETTgaTFWSLYGQTETSGLV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4145 SIwdeasdSLGDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVDNpfepgerMYR 4224
Cdd:cd17637   153 TL------SPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4225 TGDLVRWLPDGNLEYLGRIDHQ--VKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV--AQRELTAAE 4300
Cdd:cd17637   220 TGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVlkPGATLTADE 299
                         330       340       350
                  ....*....|....*....|....*....|....
gi 386647928 4301 LRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDR 4334
Cdd:cd17637   300 LIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
269-747 4.72e-16

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 86.08  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  269 QAERRPDAVAVTFE------DRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDP 342
Cdd:cd05966    62 HLKERGDKVAIIWEgdepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  343 EYPEERIRYMLEDSGTQVLLS--QG------------------------------HLQERVSFSG---TWirLDDEEAYH 387
Cdd:cd05966   142 GFSAESLADRINDAQCKLVITadGGyrggkviplkeivdealekcpsvekvlvvkRTGGEVPMTEgrdLW--WHDLMAKQ 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  388 EDGSNLESVNgPEHLTYVIYTSGTTGKPKGnltthrniirVVKNTN----YIDVTGQdkllqlssYSFD----------- 452
Cdd:cd05966   220 SPECEPEWMD-SEDPLFILYTSGSTGKPKG----------VVHTTGgyllYAATTFK--------YVFDyhpddiywcta 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  453 ------GSTFDIFGALLNGAKLVL---VPkeTVLDVAKLAGLIEKQQISVmFIT--TAffnvlvdmnpdclrhARAILFG 521
Cdd:cd05966   281 digwitGHSYIVYGPLANGATTVMfegTP--TYPDPGRYWDIVEKHKVTI-FYTapTA---------------IRALMKF 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  522 GERVSVSHVRKALGHLG----PgkI---------KHVYG---PTESTVFATsydvhevEEGAVSI-PIGG-----PISNT 579
Cdd:cd05966   343 GDEWVKKHDLSSLRVLGsvgeP--InpeawmwyyEVIGKercPIVDTWWQT-------ETGGIMItPLPGatplkPGSAT 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  580 ------AIYIVNAQNKLQPIGVAGELCVAGD--GLARGYLNRPdltaEKFADNPFAPGERMYRTGDLARWLPDGTIEYVG 651
Cdd:cd05966   414 rpffgiEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITG 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  652 RIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESA-NGEKqLCAY------YVADRSLpANEVRSTLSQELPAYML 724
Cdd:cd05966   490 RVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGEA-IYAFvtlkdgEEPSDEL-RKELRKHVRKEIGPIAT 567
                         570       580
                  ....*....|....*....|...
gi 386647928  725 PSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05966   568 PDKIQFVPGLPKTRSGKIMRRIL 590
PLN03102 PLN03102
acyl-activating enzyme; Provisional
7456-7928 4.97e-16

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 86.23  E-value: 4.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRI 7535
Cdd:PLN03102   24 SECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 RYMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQ----------------AYGEDgSNLEPVV-----GPNHLAYVI-- 7592
Cdd:PLN03102  104 AAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNlnlpvifiheidfpkrPSSEE-LDYECLIqrgepTPSLVARMFri 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7593 ----------YTSGTTGKPKGVMVEHHG--LCSLKLMFAETLRITEedrVVQFASLSFDASCWeifkALFFGATLYIPAK 7660
Cdd:PLN03102  183 qdehdpislnYTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCP---VYLWTLPMFHCNGW----TFTWGTAARGGTS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7661 DTILDYPLFESYMN--ENGIT-AAILPPTYAIYLSPDRLPSLKK-----LITGGS---AASVEFVQQWKDKVryFNAYGP 7729
Cdd:PLN03102  256 VCMRHVTAPEIYKNieMHNVThMCCVPTVFNILLKGNSLDLSPRsgpvhVLTGGSpppAALVKKVQRLGFQV--MHAYGL 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7730 TEAS--IVTSVWAAS----PDGLDLRsVPIGRPIANHQIFIVDSQNHMLPVGVA------GELCISGAGLARGYLNRPEL 7797
Cdd:PLN03102  334 TEATgpVLFCEWQDEwnrlPENQQME-LKARQGVSILGLADVDVKNKETQESVPrdgktmGEIVIKGSSIMKGYLKNPKA 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7798 TAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQL 7877
Cdd:PLN03102  413 TSEAFKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETP 485
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 7878 CAYFVADR-ELTVSELRGTL-----------SQELPGYMIPSYFVQLEQMPLTPNGKIDRNAL 7928
Cdd:PLN03102  486 CAFVVLEKgETTKEDRVDKLvtrerdlieycRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3399-3817 5.22e-16

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 85.00  E-value: 5.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3399 ALTPMQKgmWFHNTlNRHGGAYIEQT-LFNVRGALNIELFSRSWNELAARHAVLRTNF---HSGW----RGEPLQivyry 3470
Cdd:cd19534     3 PLTPIQR--WFFEQ-NLAGRHHFNQSvLLRVPQGLDPDALRQALRALVEHHDALRMRFrreDGGWqqriRGDVEE----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3471 kPVEFAYEDLRHLAeaeWSAYLDQLVNDDKtRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDG--WclPLIAKELF 3548
Cdd:cd19534    75 -LFRLEVVDLSSLA---QAAAIEALAAEAQ-SSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsW--RILLEDLE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3549 DTYEAYLRNDLSERPAAPSYSHYIEWL----EKQDMEAAARYWTGfLAGYDSQtTLPqgklhnKDGEYTEAN---ILRSL 3621
Cdd:cd19534   148 AAYEQALAGEPIPLPSKTSFQTWAELLaeyaQSPALLEELAYWRE-LPAADYW-GLP------KDPEQTYGDartVSFTL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3622 GKSLTERMSRIAKQ-HQVTVNTLMQAAWGIILQKYNGTDDavfgSVVS----GRSAEIAGIE--EMIGLFINTIPVRVSC 3694
Cdd:cd19534   220 DEEETEALLQEANAaYRTEINDLLLAALALAFQDWTGRAP----PAIFleghGREEIDPGLDlsRTVGWFTSMYPVVLDL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3695 EAEQSFADVMKRVQEA--ALESGGYDYYPLYEIQAQsaQKQDLITHIMA------FENFpmdEQIEQAGSYEDGKLAITD 3766
Cdd:cd19534   296 EASEDLGDTLKRVKEQlrRIPNKGIGYGILRYLTPE--GTKRLAFHPQPeisfnyLGQF---DQGERDDALFVSAVGGGG 370
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 3767 VDIAEQTN----YDFTLVVMPGeELAVRFYYNASVYEHSAMERLMGHLIHVLEQV 3817
Cdd:cd19534   371 SDIGPDTPrfalLDINAVVEGG-QLVITVSYSRNMYHEETIQQLADSYKEALEAL 424
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
3867-4355 5.53e-16

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 86.22  E-value: 5.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3867 NPDAVAVVFE------KSQLTYGELNERANRLARTLRDAGVRPDQLVGL---MVErslEMVVGIMAIMKAG-------GA 3930
Cdd:cd05967    64 RGDQIALIYDspvtgtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympMIP---EAAIAMLACARIGaihsvvfGG 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3931 YIP------ID---PEY---------PEDRIRY--MLEDSGAQALLTQRHL----RERVSFAGTFVAVD-DEQAYHADGS 3985
Cdd:cd05967   141 FAAkelasrIDdakPKLivtascgiePGKVVPYkpLLDKALELSGHKPHHVlvlnRPQVPADLTKPGRDlDWSELLAKAE 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3986 NLEPV-VGPNHLAYVIYTSGTTGKPKGVMVEHHGLC-SLKLMFANTLQMTEQDrvVQFAslsfdAS--CWEI------FK 4055
Cdd:cd05967   221 PVDCVpVAATDPLYILYTSGTTGKPKGVVRDNGGHAvALNWSMRNIYGIKPGD--VWWA-----ASdvGWVVghsyivYG 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4056 ALFFGAT--LY--IPTSTTilDYPLFESYMNENGITATILPPT----------YAAYLNPDRMPSLKKLITGGS---AAS 4118
Cdd:cd05967   294 PLLHGATtvLYegKPVGTP--DPGAFWRVIEKYQVNALFTAPTairairkedpDGKYIKKYDLSSLRTLFLAGErldPPT 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4119 VEFVQQwKDKVLYFNAYGPTEasivtSIWDEASDSLG-DRKSVPIG---RPLANHRIYVVDSHNRMLPVGVAGELCISGv 4194
Cdd:cd05967   372 LEWAEN-TLGVPVIDHWWQTE-----TGWPITANPVGlEPLPIKAGspgKPVPGYQVQVLDEDGEPVGPNELGNIVIKL- 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4195 GLARGYLNRPELTAEKFVDNPFE--PGerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEA 4272
Cdd:cd05967   445 PLPPGCLLTLWKNDERFKKLYLSkfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEC 522
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4273 IVLAREDANGQQQLVAYFVAQRELTAA------ELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPApegsMHA 4346
Cdd:cd05967   523 AVVGVRDELKGQVPLGLVVLKEGVKITaeelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK----IAD 598

                  ....*....
gi 386647928 4347 GGEYVAPRT 4355
Cdd:cd05967   599 GEDYTIPST 607
PRK08308 PRK08308
acyl-CoA synthetase; Validated
6302-6422 5.70e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 84.70  E-value: 5.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6302 GERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAERELTI 6381
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP 368
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 386647928 6382 GELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPA 6422
Cdd:PRK08308  369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
5958-6398 6.07e-16

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 85.10  E-value: 6.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5958 DKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLL 6037
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6038 VqghllDRAsfadklvnlnddgayhedgsnlepvngpehltYVIYTSGTTGRPKGVMVEHRNVVRLVKNTNYVELNEQTH 6117
Cdd:cd05940    81 V-----DAA--------------------------------LYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6118 ILQTGAVVFDASTFEI-WGALLNGGRLYVVRNEtiLDAVSLKNAIQQYGInTMW-----LTAPLYNQLSQQDSgmfAGLK 6191
Cdd:cd05940   124 VLYTCLPLYHSTALIVgWSACLASGATLVIRKK--FSASNFWDDIRKYQA-TIFqyigeLCRYLLNQPPKPTE---RKHK 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6192 TLIVGGDVLSvPHINRVLREHAGL-SIVNGYGPTENTT-----FSTTHTI---VGEQKEAVPI---------GKPINNST 6253
Cdd:cd05940   198 VRMIFGNGLR-PDIWEEFKERFGVpRIAEFYAATEGNSgfinfFGKPGAIgrnPSLLRKVAPLalvkydlesGEPIRDAE 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6254 AYIVDSklsllPVGVWGELI--VGGDGVARGYLNrPELTAEKFVESSFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVK 6331
Cdd:cd05940   277 GRCIKV-----PRGEPGLLIsrINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFR 350
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6332 IRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQKQLCAYFV--AERELTIGELRAALSQELPNYMIP 6398
Cdd:cd05940   351 WKGENVSTTEVAAVLGAFPGVEEANVYgVQVPGTDGRAGMAAIVlqPNEEFDLSALAAHLEKNLPGYARP 420
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
284-652 6.28e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 84.82  E-value: 6.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  284 RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLS 363
Cdd:cd05910     1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  364 qghlqervsfsgtwIRLDDEEAYhedgsnlesvngpehltyVIYTSGTTGKPKGNLTTHRNIirvvknTNYIDVTGQdkL 443
Cdd:cd05910    81 --------------IPKADEPAA------------------ILFTSGSTGTPKGVVYRHGTF------AAQIDALRQ--L 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  444 LQLSSYSFDGSTFDIFgALLNGAKLV--LVP-----KETVLDVAKLAGLIEKQQISVMFITTAFFNVLVDMnpdCLRHA- 515
Cdd:cd05910   121 YGIRPGEVDLATFPLF-ALFGPALGLtsVIPdmdptRPARADPQKLVGAIRQYGVSIVFGSPALLERVARY---CAQHGi 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  516 -----RAILFGGERVSVSHVRKALGHLGPG-KIKHVYGPTES---------TVFATSYDVHEVEEGA-VSIPIGG----- 574
Cdd:cd05910   197 tlpslRRVLSAGAPVPIALAARLRKMLSDEaEILTPYGATEAlpvssigsrELLATTTAATSGGAGTcVGRPIPGvrvri 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  575 -PISNTAIYIVNAQNKLqPIGVAGELCVAGDGLARGYLNRPDLTA-EKFADnpfaPGERM-YRTGDLARWLPDGTIEYVG 651
Cdd:cd05910   277 iEIDDEPIAEWDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATAlAKIDD----NSEGFwHRMGDLGYLDDEGRLWFCG 351

                  .
gi 386647928  652 R 652
Cdd:cd05910   352 R 352
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
762-833 6.51e-16

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 76.05  E-value: 6.51e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928  762 EPRTELEAGIVNIWKEILKI--EKISVKDSFF-ELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAI 833
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
3993-4295 6.79e-16

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 85.23  E-value: 6.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3993 PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFD---ASCWeiFKALFFGATLYI-PTS 4068
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDmglIAFH--LAPLIAGMNQYLmPTR 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4069 TTILDYPLFESYMNENGITATILPPTYAAY----LNPDR-----MPSLKKLITGGSAASVEFVQQWKDKVLYFN------ 4133
Cdd:cd05908   183 LFIRRPILWLKKASEHKATIVSSPNFGYKYflktLKPEKandwdLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrnai 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4134 --AYGPTEASIVTSIWDEASD----SLG-------------DRKS------VPIGRPLANHRIYVVDSHNRMLPVGVAGE 4188
Cdd:cd05908   263 lpVYGLAEASVGASLPKAQSPfktiTLGrrhvthgepepevDKKDsecltfVEVGKPIDETDIRICDEDNKILPDGYIGH 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4189 LCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLvRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDA 4268
Cdd:cd05908   343 IQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDL-GFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG 415
                         330       340
                  ....*....|....*....|....*....
gi 386647928 4269 VQEAIVLA--REDANGQQQLVAYFVAQRE 4295
Cdd:cd05908   416 VELGRVVAcgVNNSNTRNEEIFCFIEHRK 444
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
7471-7867 9.42e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 85.48  E-value: 9.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7471 QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEY---PED--RIRYMLE----- 7540
Cdd:PRK12582   80 KVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmSHDhaKLKHLFDlvkpr 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7541 ----DSGAQVlltQRHLQEcVSFDGKVIAADDEQAYGEDGSNLE-----PV----------VGPNHLAYVIYTSGTTGKP 7601
Cdd:PRK12582  160 vvfaQSGAPF---ARALAA-LDLLDVTVVHVTGPGEGIASIAFAdlaatPPtaavaaaiaaITPDTVAKYLFTSGSTGMP 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7602 KGVMVEHHGLCSLKLMfAETLRITEEDRVVqfaSLSFDASCWE-------IFKALFF-GATLYIPA--------KDTILD 7665
Cdd:PRK12582  236 KAVINTQRMMCANIAM-QEQLRPREPDPPP---PVSLDWMPWNhtmggnaNFNGLLWgGGTLYIDDgkplpgmfEETIRN 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7666 ypLFE---SYMNENGITAAILPPtyAIYLSPDRLPS----LKKLITGGSAASVEFVQQWKD--------KVRYFNAYGPT 7730
Cdd:PRK12582  312 --LREispTVYGNVPAGYAMLAE--AMEKDDALRRSffknLRLMAYGGATLSDDLYERMQAlavrttghRIPFYTGYGAT 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7731 EAS--IVTSVWAASPDGLdlrsvpIGRPIANHQIfivdsqnHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDNPFl 7808
Cdd:PRK12582  388 ETAptTTGTHWDTERVGL------IGLPLPGVEL-------KLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF- 453
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 7809 agermYRTGDLARWL----PDGNIEYLGRIDHQVKI-RGYRIELGEIEEQLLKIAS-VQETIVIA 7867
Cdd:PRK12582  454 -----YRLGDAARFVdpddPEKGLIFDGRVAEDFKLsTGTWVSVGTLRPDAVAACSpVIHDAVVA 513
PLN03102 PLN03102
acyl-activating enzyme; Provisional
1303-1795 9.92e-16

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 85.07  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1303 FEKQA-ERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 1381
Cdd:PLN03102   19 FLKRAsECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1382 PSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQA--------VLCLDD----EAAYAEDA-------------SNVAN 1436
Cdd:PLN03102   99 DATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSedsnlnlpVIFIHEidfpKRPSSEELdyecliqrgeptpSLVAR 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1437 ---VNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFV---GDIARtlynGGT 1510
Cdd:PLN03102  179 mfrIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTftwGTAAR----GGT 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1511 MViCPKddRIDPARLHYWISEEKITIFESTPALiipFMDYVAEHGLDMS----SMELLITSSDSCSVTDYRVlqERFGsq 1586
Cdd:PLN03102  255 SV-CMR--HVTAPEIYKNIEMHNVTHMCCVPTV---FNILLKGNSLDLSprsgPVHVLTGGSPPPAALVKKV--QRLG-- 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1587 FRIINAYGVTEAA--IDSSLYDEPLAKLPEAGNVPIG--KAALNAKFYIVDAH----LNPVPVG--VLGELCIGGIGVAR 1656
Cdd:PLN03102  325 FQVMHAYGLTEATgpVLFCEWQDEWNRLPENQQMELKarQGVSILGLADVDVKnketQESVPRDgkTMGEIVIKGSSIMK 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1657 GYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRE 1736
Cdd:PLN03102  405 GYLKNPKATSEAFKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMP 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 1737 DAKGQKVLCAYFTAE-SELKLSELRSSL-----------SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PLN03102  478 HPTWGETPCAFVVLEkGETTKEDRVDKLvtrerdlieycRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
405-685 1.06e-15

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 82.73  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 VIYTSGTTGKPKGNLTTHRNIIrvVKNTNYIDVTGQDkllqlSSYSF--------DGSTFDIFGALLNGAKLVLVPKetv 476
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALL--AQALVLAVLQAID-----EGTVFlnsgplfhIGTLMFTLATFHAGGTNVFVRR--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  477 LDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRHA---RAILFGGERVSVSHV-RKALGHLGPGkikhvYGPTEST 552
Cdd:cd17636    75 VDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLsslRSSPAAPEWNDMATVdTSPWGRKPGG-----YGQTEVM 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  553 VFATsydVHEVEEGAVSIpIGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADnpfapgeRM 632
Cdd:cd17636   150 GLAT---FAALGGGAIGG-AGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GW 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928  633 YRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV 685
Cdd:cd17636   219 HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
260-749 1.09e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 84.66  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  260 TTIHRLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVP 339
Cdd:PRK13383   35 TNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  340 IDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWIR-LDDEEAYHEDGSNLESVNGPEHLtyVIYTSGTTGKPKGN 418
Cdd:PRK13383  115 ISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAvIDPATAGAEESGGRPAVAAPGRI--VLLTSGTTGKPKGV 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  419 LTTHRniirvVKNTNYIDVTGQDKL-------LQLSSYSFDGSTFDIFGALLNGAKLVLVPKETVLDVA-KLAGLIEKQQ 490
Cdd:PRK13383  193 PRAPQ-----LRSAVGVWVTILDRTrlrtgsrISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAAlAQASLHRADA 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  491 ISVMFITTAFFNVLVDM----NPdcLRHARAILFGGERVSVSHVRKALGHLGpGKIKHVYGPTESTV--FATSYDVHEVE 564
Cdd:PRK13383  268 FTAVPVVLARILELPPRvrarNP--LPQLRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVGIgaLATPADLRDAP 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  565 EgavsiPIGGPISNTAIYIVNAQNKlqPIG--VAGELCVAGDGLARGYlnrPDLTAEKFADNpfapgerMYRTGDLARWL 642
Cdd:PRK13383  345 E-----TVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGGELAGTRY---TDGGGKAVVDG-------MTSTGDMGYLD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  643 PDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAI-EKATVVVRESANGEKqLCAYYVA--DRSLPANEVRSTLSQEL 719
Cdd:PRK13383  408 NAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDERFGHR-LAAFVVLhpGSGVDAAQLRDYLKDRV 486
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928  720 PAYMLPSYFVQLEQMPLTTNGKVDRRALPA 749
Cdd:PRK13383  487 SRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
PRK13382 PRK13382
bile acid CoA ligase;
1270-1798 1.16e-15

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 84.81  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1270 SLGILTVEEKAQLVhvfNPAAPDA---------PENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLR 1340
Cdd:PRK13382   10 TLGLIATLRRAGLI---APMRPDRylrivaamrREGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1341 AQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ---THLQERA-QQWGQTLQ 1416
Cdd:PRK13382   87 ALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDeefSATVDRAlADCPQATR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1417 AVLCLDDEAAYAEDASNVANVNE-----PHDLAYVIYTSGTTGRPKGVmieHRSLVNTAAGYRReyRLDQFPVRLLQLAS 1491
Cdd:PRK13382  167 IVAWTDEDHDLTVEVLIAAHAGQrpeptGRKGRVILLTSGTTGTPKGA---RRSGPGGIGTLKA--ILDRTPWRAEEPTV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1492 FSFDVF----VGDIARTLYNGGTMVIcpkDDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAEhGLDMSSMELL--I 1565
Cdd:PRK13382  242 IVAPMFhawgFSQLVLAASLACTIVT---RRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAE-VRNRYSGRSLrfA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1566 TSSDSCSVTD-YRVLQERFGSQfrIINAYGVTEAAIDSSLYDEPLAKLPEAGnvpiGKAALNAKFYIVDAHLNPVPVGVL 1644
Cdd:PRK13382  318 AASGSRMRPDvVIAFMDQFGDV--IYNNYNATEAGMIATATPADLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEV 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1645 GELCIGGIGVARGYlnrpelTEEKfvDSPFVEGerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKA 1724
Cdd:PRK13382  392 GTIFVRNDTQFDGY------TSGS--TKDFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATH 461
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1725 EGVREAVVVVREDAK-GQKvLCAYFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAP 1798
Cdd:PRK13382  462 PDVAEAAVIGVDDEQyGQR-LAAFVVLKPGASATpeTLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
5932-6331 1.19e-15

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 84.93  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5932 PSDKTIHQLFEEQAERIPDHLAVTFEDKQ-----LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAIL 6006
Cdd:PRK08180   36 DYPRRLTDRLVHWAQEAPDRVFLAERGADggwrrLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6007 KAGGAYVPIDPDY---PED--RIRYMLE-----------------------DSGAKLLLVQGHLLDRA--SFADKLvnln 6056
Cdd:PRK08180  116 YAGVPYAPVSPAYslvSQDfgKLRHVLElltpglvfaddgaafaralaavvPADVEVVAVRGAVPGRAatPFAALL---- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6057 dDGAYHEDGSNLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNvvrLVKNtnyvelneQTHILQTGAV------------ 6124
Cdd:PRK08180  192 -ATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRM---LCAN--------QQMLAQTFPFlaeeppvlvdwl 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6125 ----VFDAS-TFEIwgALLNGGRLYV-------------VRNetiLDAVSlknaiqqygiNTMWLTAPL-YNQLSQ---Q 6182
Cdd:PRK08180  260 pwnhTFGGNhNLGI--VLYNGGTLYIddgkptpggfdetLRN---LREIS----------PTVYFNVPKgWEMLVPaleR 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6183 DSG----MFAGLKTLIVGGDVLSVP---HINRVLREHAG--LSIVNGYGPTENTTFST-THtivGEQKEAVPIGKPINNS 6252
Cdd:PRK08180  325 DAAlrrrFFSRLKLLFYAGAALSQDvwdRLDRVAEATCGerIRMMTGLGMTETAPSATfTT---GPLSRAGNIGLPAPGC 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6253 TayivdskLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGDLARWL----PDGTLEYKGRIDE 6328
Cdd:PRK08180  402 E-------VKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRFVdpadPERGLMFDGRIAE 468

                  ...
gi 386647928 6329 QVK 6331
Cdd:PRK08180  469 DFK 471
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
399-760 1.31e-15

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 84.46  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  399 PEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKN-TNYIDVTGQDKLLQLSSYSFD-GSTFDIFGALLNGAKLVLVPKETV 476
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAiLNSTEWKTKDRILSWMPLTHDmGLIAFHLAPLIAGMNQYLMPTRLF 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  477 LDVAKL-AGLIEKQQISVMFITTAFFNVLVD-MNPDC-----LRHARAILFGGERVSVSHVRKALGHLGPGKIKH----- 544
Cdd:cd05908   185 IRRPILwLKKASEHKATIVSSPNFGYKYFLKtLKPEKandwdLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRnailp 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  545 VYGPTESTVFATSYDVHEV------------------------EEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVAGELC 600
Cdd:cd05908   265 VYGLAEASVGASLPKAQSPfktitlgrrhvthgepepevdkkdSECLTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQ 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  601 VAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLArWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIE 680
Cdd:cd05908   345 IRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVE 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  681 KATVV---VRESANGEKQLCAYYV----ADRSLP-ANEVRSTLSQELPAYMlpSYFVQLEQMPLTTNGKVDRRALpapEE 752
Cdd:cd05908   418 LGRVVacgVNNSNTRNEEIFCFIEhrksEDDFYPlGKKIKKHLNKRGGWQI--NEVLPIRRIPKTTSGKVKRYEL---AQ 492

                  ....*...
gi 386647928  753 SMETGvEF 760
Cdd:cd05908   493 RYQSG-EF 499
PRK07867 PRK07867
acyl-CoA synthetase; Validated
3863-4339 1.38e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 84.35  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3863 QALRNPDAVAVVFEKSQLTYGELNERANRLARTLRD--AGVRPDQlVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPE 3940
Cdd:PRK07867   12 LPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRArlDPTRPPH-VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3941 DRIRYMLEDSGAQALLT---QRHLRERVSFAGTFVAVD-----DEQAYHADGSNLEPVVGPNHLAYVIYTSGTTGKPKGV 4012
Cdd:PRK07867   91 AALARDIAHADCQLVLTesaHAELLDGLDPGVRVINVDspawaDELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4013 MVEHHGLCSLKLMFANTLQMTEQDrvVQFASLSFDAS-----CWEIfkALFFGATLYIP----TSTTILDYPLF-ESYMN 4082
Cdd:PRK07867  171 RCTHRKVASAGVMLAQRFGLGPDD--VCYVSMPLFHSnavmaGWAV--ALAAGASIALRrkfsASGFLPDVRRYgATYAN 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4083 ENG-----ITATilPPTyaaylnPDRMPSLKKLITGGSAASV---EFVQQWKDKVLyfNAYGPTEASI-VTSIWDEASDS 4153
Cdd:PRK07867  247 YVGkplsyVLAT--PER------PDDADNPLRIVYGNEGAPGdiaRFARRFGCVVV--DGFGSTEGGVaITRTPDTPPGA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4154 LGdrksvpigRPLANHRIY-----------VVDSHNRMLPVGVAGELC-ISGVGLARGYLNRPELTAEKFVDNpfepger 4221
Cdd:PRK07867  317 LG--------PLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRGG------- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4222 MYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQR--ELTAA 4299
Cdd:PRK07867  382 VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPgaKFDPD 461
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 386647928 4300 ELRATMSQ--ELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:PRK07867  462 AFAEFLAAqpDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
2346-2842 1.57e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 84.31  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERipDHPAVVFEGQQLTYRE-LNERANR--LARTLQAlgvkTDQP--VGLMLERSLEMVVGMFAVLKAGG 2420
Cdd:PRK13388    4 TIAQLLRDRAGD--DTIAVRYGDRTWTWREvLAEAAARaaALIALAD----PDRPlhVGVLLGNTPEMLFWLAAAALGGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2421 AYVPIDPEypeDRISYMLED---SSAQVLL---AQRRLQERVSFAGTVVTVDDEQAYA---GDGSNLE--SAVGPNDLAY 2489
Cdd:PRK13388   78 VLVGLNTT---RRGAALAADirrADCQLLVtdaEHRPLLDGLDLPGVRVLDVDTPAYAelvAAAGALTphREVDAMDPFM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2490 IIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDrvVQFASLS-FD----ASCWEVfqTLFFGATLYIPTKetild 2564
Cdd:PRK13388  155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD--VCYVSMPlFHsnavMAGWAP--AVASGAAVALPAK----- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2565 yqwFE--RYMSDNGITTATL------PPTYaVYLNPDHMPDF-KRL-IAAGSASSLELLQQWKDK--VKYFNAYGPTEDS 2632
Cdd:PRK13388  226 ---FSasGFLDDVRRYGATYfnyvgkPLAY-ILATPERPDDAdNPLrVAFGNEASPRDIAEFSRRfgCQVEDGYGSSEGA 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2633 iCTTIWTPSTEDISqlksvpIGGPIVNHRIYIVDAhYQPVPVGV-------------AGELC-IAGVGLARGYLNRPDLT 2698
Cdd:PRK13388  302 -VIVVREPGTPPGS------IGRGAPGVAIYNPET-LTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPEAT 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2699 AEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA-HDDASGQKQL 2777
Cdd:PRK13388  374 AERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAvPDERVGDQVM 446
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 2778 CAYFVAD-RTMTVGELRGELSG--ELPGYMIPAHFVQLERMPLTPNGKIDRKALPApQGNASAGADYV 2842
Cdd:PRK13388  447 AALVLRDgATFDPDAFAAFLAAqpDLGTKAWPRYVRIAADLPSTATNKVLKRELIA-QGWATGDPVTL 513
PLN02479 PLN02479
acetate-CoA ligase
1302-1797 1.59e-15

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 84.51  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1302 LFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 1381
Cdd:PLN02479   25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1382 PSDRIQFMLEDSAASVL--------LTQTHLQERAQQWGQTLQAVLCL---DD-------EAAYAEDASNVANVNEPHDL 1443
Cdd:PLN02479  105 NAPTIAFLLEHSKSEVVmvdqefftLAEEALKILAEKKKSSFKPPLLIvigDPtcdpkslQYALGKGAIEYEKFLETGDP 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1444 AYVI-------------YTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGT 1510
Cdd:PLN02479  185 EFAWkppadewqsialgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTN 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1511 mvICPKddRIDPARLHYWISEEKITIFESTPALIIPFMDY-VAEHGLDMSSMELLITSSDSCSVTDYRVLQERfgsQFRI 1589
Cdd:PLN02479  265 --ICLR--QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNApKSETILPLPRVVHVMTAGAAPPPSVLFAMSEK---GFRV 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1590 INAYGVTEAAIDSSLydepLAKLPEAGNVP-IGKAALNAK----------FYIVDAH-LNPVPV--GVLGELCIGGIGVA 1655
Cdd:PLN02479  338 THTYGLSETYGPSTV----CAWKPEWDSLPpEEQARLNARqgvryiglegLDVVDTKtMKPVPAdgKTMGEIVMRGNMVM 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1656 RGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVR 1735
Cdd:PLN02479  414 KGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVAR 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 1736 EDAKGQKVLCAYFTAESELKLSELRSSLS-------QELPGYMIPSYFVqLEQLPLTANGKIDRKALPA 1797
Cdd:PLN02479  487 PDERWGESPCAFVTLKPGVDKSDEAALAEdimkfcrERLPAYWVPKSVV-FGPLPKTATGKIQKHVLRA 554
PRK07867 PRK07867
acyl-CoA synthetase; Validated
1315-1797 1.62e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 84.35  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1315 AVVYENDRLTYRELNERANRLARMLRAQ---GVKPNqlVGILADRSADLLVGALAVWKAGGAYVPLDP---------DYP 1382
Cdd:PRK07867   21 GLYFEDSFTSWREHIRGSAARAAALRARldpTRPPH--VGVLLDNTPEFSLLLGAAALSGIVPVGLNPtrrgaalarDIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLEDSAASVLLTQT-----HLQERAQQWGQTLQAvlcLDDEAAYAEDASnvanvnePHDLAYVIYTSGTTGRPK 1457
Cdd:PRK07867   99 HADCQLVLTESAHAELLDGLdpgvrVINVDSPAWADELAA---HRDAEPPFRVAD-------PDDLFMLIFTSGTSGDPK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1458 GVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPK-------DDridparlhywis 1530
Cdd:PRK07867  169 AVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKfsasgflPD------------ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1531 eekITIFESTpaliipFMDYV---------AEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAId 1601
Cdd:PRK07867  237 ---VRRYGAT------YANYVgkplsyvlaTPERPDDADNPLRIVYGNEGAPGDIARFARRFGC--VVVDGFGSTEGGV- 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1602 sslydePLAKLPEAGNVPIGKAALNAKfyIVDAH-LNPVPVGVL------------GELC-IGGIGVARGYLNRPELTEE 1667
Cdd:PRK07867  305 ------AITRTPDTPPGALGPLPPGVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAE 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1668 KFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED-AKGQKVLCA 1746
Cdd:PRK07867  377 RMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpVVGDQVMAA 449
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 1747 YFTAE-SELKLSELRSSLSQ--ELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 1797
Cdd:PRK07867  450 LVLAPgAKFDPDAFAEFLAAqpDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
PLN02246 PLN02246
4-coumarate--CoA ligase
1277-1797 1.81e-15

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 83.88  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1277 EEKAQLVHVFNPAAPDA--PENEVFHA-LFEKQAERTPEVAAVVYENDR-LTYRELNERANRLARMLRAQGVKPNQLVGI 1352
Cdd:PLN02246    1 EASASEEFIFRSKLPDIyiPNHLPLHDyCFERLSEFSDRPCLIDGATGRvYTYADVELLSRRVAAGLHKLGIRQGDVVML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1353 LADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQA-VLCLDDEAAYAEDA 1431
Cdd:PLN02246   81 LLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVtVVTIDDPPEGCLHF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1432 SNVANVNE---------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA----GYRREYRLDQFPVRLLQLASF---SFD 1495
Cdd:PLN02246  161 SELTQADEnelpeveisPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILCVLPMFhiySLN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1496 --VFVGdiartLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTPALIIPFM--DYVAEHglDMSSMELLItssdSC 1571
Cdd:PLN02246  241 svLLCG-----LRVGAAILIMPK---FEIGALLELIQRHKVTIAPFVPPIVLAIAksPVVEKY--DLSSIRMVL----SG 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1572 SVTDYRVLQERFGSqfRIINA-----YGVTEA----AIDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLN-PVPV 1641
Cdd:PLN02246  307 AAPLGKELEDAFRA--KLPNAvlgqgYGMTEAgpvlAMCLAFAKEPFPVKSGS----CGTVVRNAELKIVDPETGaSLPR 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1642 GVLGELCIGGIGVARGYLNRPELTEekfvdspfvegerlyRTGDLARWMPDGNVDFI---------GRIDNQAKIRGYRI 1712
Cdd:PLN02246  381 NQPGEICIRGPQIMKGYLNDPEATA---------------NTIDKDGWLHTGDIGYIddddelfivDRLKELIKYKGFQV 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1713 ETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYF--TAESELKLSELRSSLSQELPGY-MIPS-YFVqlEQLPLTANG 1788
Cdd:PLN02246  446 APAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVvrSNGSEITEDEIKQFVAKQVVFYkRIHKvFFV--DSIPKAPSG 523

                  ....*....
gi 386647928 1789 KIDRKALPA 1797
Cdd:PLN02246  524 KILRKDLRA 532
PRK09192 PRK09192
fatty acyl-AMP ligase;
2370-2775 1.83e-15

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 84.29  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2370 QLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPID-PEYPEDRISY------MLEDSS 2442
Cdd:PRK09192   49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLASAQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2443 AQVLLAQRRLQERVSFAGT----VVTVDDEQAYAGDGSNLE-SAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCS-LKQM 2516
Cdd:PRK09192  129 PAAIITPDELLPWVNEATHgnplLHVLSHAWFKALPEADVAlPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMAnLRAI 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2517 FANTLQINAQDRVVQFASLSFDAScwevfqtL--FFGATL-------YIPTKE-TILDYQWFeRYMSDNGITTAtLPPTY 2586
Cdd:PRK09192  209 SHDGLKVRPGDRCVSWLPFYHDMG-------LvgFLLTPVatqlsvdYLPTRDfARRPLQWL-DLISRNRGTIS-YSPPF 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2587 AVYL------NPDHMP-DFKRLIAAGSAS---SLELLQQWKDKV-------KYFNA-YGPTEDSICTTIWTPS------T 2642
Cdd:PRK09192  280 GYELcarrvnSKDLAElDLSCWRVAGIGAdmiRPDVLHQFAEAFapagfddKAFMPsYGLAEATLAVSFSPLGsgivveE 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2643 EDISQL----KSVPIGGP------IVN-------HRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDN 2705
Cdd:PRK09192  360 VDRDRLeyqgKAVAPGAEtrrvrtFVNcgkalpgHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADG 439
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2706 PFEpgermyrTGDLAkWLPDGTIEYLGRIDHQVKIRGYRIELGEIE---EQLLKVASvQEAIVIAHDDASGQK 2775
Cdd:PRK09192  440 WLD-------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEwiaEQEPELRS-GDAAAFSIAQENGEK 503
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5960-6325 1.97e-15

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 83.28  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5960 QLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDypedrirymledsgaklllvq 6039
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG--------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6040 ghlLDRASFADKLVNLNDDGAYHEDGSnLEPVngpehltYVIYTSGTTGRPKGVMVEHRNVVrlvkntNYVELNEQTHIL 6119
Cdd:cd05910    61 ---MGRKNLKQCLQEAEPDAFIGIPKA-DEPA-------AILFTSGSTGTPKGVVYRHGTFA------AQIDALRQLYGI 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6120 QTGAVvfDASTFEIWgALLNG--GRLYVV-----RNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQ---QDSGMFAG 6189
Cdd:cd05910   124 RPGEV--DLATFPLF-ALFGPalGLTSVIpdmdpTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARycaQHGITLPS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6190 LKTLIVGGDVLSVPHINRVLRE-HAGLSIVNGYGPTENTTFS--------TTHTIVGEQKEAVPIGKPINNSTAYIV--- 6257
Cdd:cd05910   201 LRRVLSAGAPVPIALAARLRKMlSDEAEILTPYGATEALPVSsigsrellATTTAATSGGAGTCVGRPIPGVRVRIIeid 280
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6258 -------DSKLSlLPVGVWGELIVGGDGVARGYLNRPELTAekFVESSFLPGERCYRTGDLARWLPDGTLEYKGR 6325
Cdd:cd05910   281 depiaewDDTLE-LPRGEIGEITVTGPTVTPTYVNRPVATA--LAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGR 352
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
3400-3714 1.98e-15

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 83.30  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3400 LTPMQKGMWFHNTLNRHGGAYIEQTLFNVRGALNIELFSRSWNELAARHAVLRTNFHSGWRgeplQIVYRYKPVEFAYED 3479
Cdd:cd19546     7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGG----DVHQRILDADAARPE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3480 LRHLAEAEwsAYLDQLVNDDKTRGFDLEQDALMRVKVVRTQEESFHVLWSFHHILMDGWCLPLIAKELFDTYEAYLRNDL 3559
Cdd:cd19546    83 LPVVPATE--EELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3560 SER-PAAPSYSHYIEWLEK-----QDMEAAA----RYWTGFLAGYDSQTTLPQGKLHNKDGEYTEANILRSLGKSLTERM 3629
Cdd:cd19546   161 PERaPLPLQFADYALWEREllageDDRDSLIgdqiAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3630 SRIAKQHQVTVNTLMQAAWGIILQKYNGTDDAVFGSVVSgRSAEIAGIEEMIGLFINTIPVRVSCEAEQSFADVMKRVQE 3709
Cdd:cd19546   241 MEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLP-RDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVRE 319

                  ....*
gi 386647928 3710 AALES 3714
Cdd:cd19546   320 AVREA 324
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
4894-5257 2.01e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 83.59  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4894 EKQAECTPEAAAVVYENDR--LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY 4971
Cdd:PRK13391    4 GIHAQTTPDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4972 PSDRIQFMLEDSAASVLLTQT-HLQERAQQWGQTLQAALCLD-------------DEAAYAEDASNVANVNEPHDLayvI 5037
Cdd:PRK13391   84 TPAEAAYIVDDSGARALITSAaKLDVARALLKQCPGVRHRLVldgdgelegfvgyAEAVAGLPATPIADESLGTDM---L 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5038 YTSGTTGRPKGVMIEHRS-----------LVNTAAGYRREYRLDQfPVRLLQLASFSfdvFVGDIARTlynGGTMVICpk 5106
Cdd:PRK13391  161 YSSGTTGRPKGIKRPLPEqppdtplpltaFLQRLWGFRSDMVYLS-PAPLYHSAPQR---AVMLVIRL---GGTVIVM-- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5107 dDRIDPARLHYWISEEKITIFESTPALIIPFMDYVAE--HGLDMSSMVLLITSSDSCSVTDYRVLQERFGSqfrIINA-Y 5183
Cdd:PRK13391  232 -EHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEvrDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGP---IIHEyY 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 5184 GVTEA----AIDSslyDEPLAKLPEAGNVPIGkaalnaKFYIVDAHLNPVPVGVLGELCIGGiGVARGYLNRPELTEE 5257
Cdd:PRK13391  308 AATEGlgftACDS---EEWLAHPGTVGRAMFG------DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAE 375
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
7943-8017 2.20e-15

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 74.50  E-value: 2.20e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7943 EPRTPVEAELARIWQEVLGIGP--ISVKDNFF-ELGGHSLRATVLSSKVNKELNVNLPLRDIFRFPTVEALAQVIDGL 8017
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVDPeeITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
2369-2766 2.55e-15

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 83.29  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2369 QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLA 2448
Cdd:cd05932     5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2449 QR-------------RLQERVSFAGTVVTVDDE-QAYAGDGSNLESAV--GPNDLAYIIYTSGTTGKPKGVMVEHHGLCS 2512
Cdd:cd05932    85 GKlddwkamapgvpeGLISISLPPPSAANCQYQwDDLIAQHPPLEERPtrFPEQLATLIYTSGTTGQPKGVMLTFGSFAW 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2513 LKQMFANTLQINAQDR-------------------------VVQFA-SL-SFDASCWEVFQTLFFGAT-LYIPTKETILD 2564
Cdd:cd05932   165 AAQAGIEHIGTEENDRmlsylplahvtervfveggslyggvLVAFAeSLdTFVEDVQRARPTLFFSVPrLWTKFQQGVQD 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2565 ---YQWFERYMSDNgITTATLPPTYAVYLNPDHMpdfkRLIAAGSASSLELLQQWKDKV--KYFNAYGPTEDSICTTIWT 2639
Cdd:cd05932   245 kipQQKLNLLLKIP-VVNSLVKRKVLKGLGLDQC----RLAGCGSAPVPPALLEWYRSLglNILEAYGMTENFAYSHLNY 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2640 PSTEDISqlkSVPIGGPIVNHRIyivdahyqpvpvGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDL 2719
Cdd:cd05932   320 PGRDKIG---TVGNAGPGVEVRI------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGF------LRTGDK 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 2720 AKWLPDGTIEYLGRIDHQVKI-RGYRIELGEIEEQLLKVASVQEAIVI 2766
Cdd:cd05932   379 GELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
PRK07867 PRK07867
acyl-CoA synthetase; Validated
4905-5387 3.01e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 83.19  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4905 AVVYENDRLTYRELNERANRLARTLRAQ---GVKPNqlVGILADRSADLLVGALAVWKAGGAYVPLDP---------DYP 4972
Cdd:PRK07867   21 GLYFEDSFTSWREHIRGSAARAAALRARldpTRPPH--VGVLLDNTPEFSLLLGAAALSGIVPVGLNPtrrgaalarDIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLEDSAASVLLTQT-----HLQERAQQWGQTLQAalcLDDEAAYAEDASnvanvnePHDLAYVIYTSGTTGRPK 5047
Cdd:PRK07867   99 HADCQLVLTESAHAELLDGLdpgvrVINVDSPAWADELAA---HRDAEPPFRVAD-------PDDLFMLIFTSGTSGDPK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5048 GVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPK-------DDridparlhywis 5120
Cdd:PRK07867  169 AVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKfsasgflPD------------ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5121 eekITIFESTpaliipFMDYV---------AEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEAAId 5191
Cdd:PRK07867  237 ---VRRYGAT------YANYVgkplsyvlaTPERPDDADNPLRIVYGNEGAPGDIARFARRFGC--VVVDGFGSTEGGV- 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5192 sslydePLAKLPEAGNVPIGKAALNAKfyIVDAH-LNPVPVGVL------------GELC-IGGIGVARGYLNRPELTEE 5257
Cdd:PRK07867  305 ------AITRTPDTPPGALGPLPPGVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAE 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5258 KFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED-AKGQKVLCA 5336
Cdd:PRK07867  377 RMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpVVGDQVMAA 449
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 5337 -------HFTAEselKLSELRSSLSqELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 5387
Cdd:PRK07867  450 lvlapgaKFDPD---AFAEFLAAQP-DLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1324-1795 3.52e-15

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 82.96  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1324 TYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL-TQT 1402
Cdd:cd17642    46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFcSKK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 HLQE--RAQQWGQTLQAVLCLD---DEAAYAEDASNVAN---------------VNEPHDLAYVIYTSGTTGRPKGVMIE 1462
Cdd:cd17642   126 GLQKvlNVQKKLKIIKTIIILDskeDYKGYQCLYTFITQnlppgfneydfkppsFDRDEQVALIMNSSGSTGLPKGVQLT 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1463 HRSLVNTAAGYRREYRLDQF--PVRLLQLASF--SFDVFVgdIARTLYNGGTMVICPKddridparlhywiSEEKITI-- 1536
Cdd:cd17642   206 HKNIVARFSHARDPIFGNQIipDTAILTVIPFhhGFGMFT--TLGYLICGFRVVLMYK-------------FEEELFLrs 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1537 ---FESTPALIIP-FMDYVAEHGL----DMSSMELLITSSDSCSVTDYRVLQERFGSQFrIINAYGVTEAAIDSSLYDEP 1608
Cdd:cd17642   271 lqdYKVQSALLVPtLFAFFAKSTLvdkyDLSNLHEIASGGAPLSKEVGEAVAKRFKLPG-IRQGYGLTETTSAILITPEG 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1609 LAKLPEAGNVPIGKAAlnakfYIVDAHLNPVpVGV--LGELCIGGIGVARGYLNRPELTEEkfvdspFVEGERLYRTGDL 1686
Cdd:cd17642   350 DDKPGAVGKVVPFFYA-----KVVDLDTGKT-LGPneRGELCVKGPMIMKGYVNNPEATKA------LIDKDGWLHSGDI 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1687 ARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSEL------- 1759
Cdd:cd17642   418 AYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKevmdyva 497
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 1760 -RSSLSQELPGYMIpsyFVqlEQLPLTANGKIDRKAL 1795
Cdd:cd17642   498 sQVSTAKRLRGGVK---FV--DEVPKGLTGKIDRRKI 529
PRK08308 PRK08308
acyl-CoA synthetase; Validated
4219-4341 3.77e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 82.01  E-value: 3.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4219 GERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFVAQRELTA 4298
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP 368
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 386647928 4299 AELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPAPE 4341
Cdd:PRK08308  369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
3881-4337 3.97e-15

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 82.88  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3881 TYGELNERANRLARTLRDAGVRPDQLVGLM---VERSLEMVVGIMAImkaGGAYIPIDPEYPEDRIRYMLEDSGAQALLT 3957
Cdd:PRK06018   41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3958 Q-------RHLRERVSFAGTFVAVDDEQ-----------AYH-----ADGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMV 4014
Cdd:PRK06018  118 DltfvpilEKIADKLPSVERYVVLTDAAhmpqttlknavAYEewiaeADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLY 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4015 EHHG--LCSLKLMFANTLQMTEQDRVVQFASLsFDASCWEI-FKALFFGATLYIPTSTtiLD----YPLFESymneNGIT 4087
Cdd:PRK06018  198 SHRSnvLHALMANNGDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVMPGAK--LDgasvYELLDT----EKVT 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4088 ATILPPTYAAYL------NPDRMPSLKKLITGGSAASVEFVQQWKD-KVLYFNAYGPTEAS---IVTSIWDEASDSLGDR 4157
Cdd:PRK06018  271 FTAGVPTVWLMLlqymekEGLKLPHLKMVVCGGSAMPRSMIKAFEDmGVEVRHAWGMTEMSplgTLAALKPPFSKLPGDA 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4158 K---SVPIGRPLANHRIYVVDSHNRMLPV-GVA-GELCISGVGLARGYLnRPE---LTAEKFVDnpfepgermyrTGDLV 4229
Cdd:PRK06018  351 RldvLQKQGYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYY-RVDgeiLDDDGFFD-----------TGDVA 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4230 RWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQ--LVAYFVAQRELTAAELRATMSQ 4307
Cdd:PRK06018  419 TIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERplLIVQLKPGETATREEILKYMDG 498
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 4308 ELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PRK06018  499 KIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
PRK08308 PRK08308
acyl-CoA synthetase; Validated
629-751 4.23e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 82.01  E-value: 4.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  629 GERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKAtVVVR--ESANGEKqLCAYYVADRSL 706
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEA-VVYRgkDPVAGER-VKAKVISHEEI 366
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386647928  707 PANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAPE 751
Cdd:PRK08308  367 DPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
6529-6741 4.45e-15

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 81.93  E-value: 4.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6529 WFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFrKSENGyAAWNRAIGEGElyslEVADFRDVKS 6608
Cdd:cd19538    12 WFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVF-PEEDG-VPYQLILEEDE----ATPKLEIKEV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6609 AEQAVEAKANE-IQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEE---VRLPA 6683
Cdd:cd19538    86 DEEELESEINEaVRYPFDLSEEPPFRATLFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEApelAPLPV 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 6684 KTDSFRTWSEQLAAYAQSPA--MENERAYW-EQIAQTAVA-PLPKD--KQSDRSLQQDSESITI 6741
Cdd:cd19538   166 QYADYALWQQELLGDESDPDslIARQLAYWkKQLAGLPDEiELPTDypRPAESSYEGGTLTFEI 229
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4352-4426 4.80e-15

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 73.73  E-value: 4.80e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 4352 APRTPTEAKLAHIWQDVLGL--EKVGVKDNFF-ELGGHSLRATALASKVRKELNMELPLRHIFQFPTVEQLAEAIGQL 4426
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PRK05857 PRK05857
fatty acid--CoA ligase;
5936-6430 4.96e-15

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 82.75  E-value: 4.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTFED--KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYV 6013
Cdd:PRK05857   15 TVLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6014 PIDPDYPEDRI-RYMLEDSGAKLLLVQGHLLDRASFADKL-------VNLNDDGAYHE-----DGSNLEPVNGPEHLTYV 6080
Cdd:PRK05857   95 MADGNLPIAAIeRFCQITDPAAALVAPGSKMASSAVPEALhsipviaVDIAAVTRESEhsldaASLAGNADQGSEDPLAM 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6081 IYTSGTTGRPKGVMVEHR------NVVR---------LVKNTNYVELnEQTHIlqtgavvfdASTFEIWGALLNGGrLYV 6145
Cdd:PRK05857  175 IFTSGTTGEPKAVLLANRtffavpDILQkeglnwvtwVVGETTYSPL-PATHI---------GGLWWILTCLMHGG-LCV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6146 VRNEtilDAVSLKNAIQQYGINTMWLTAPLYNQL-SQQDSG--MFAGLKTLIVGGDVLSVPHINRVlrEHAGLSIVNGYG 6222
Cdd:PRK05857  244 TGGE---NTTSLLEILTTNAVATTCLVPTLLSKLvSELKSAnaTVPSLRLVGYGGSRAIAADVRFI--EATGVRTAQVYG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6223 -----------PTENTTFStthtivgeQKEAVPIGKPINNSTAYIVD------SKLSLLPVGVWGELIVGGDGVARGYLN 6285
Cdd:PRK05857  319 lsetgctalclPTDDGSIV--------KIEAGAVGRPYPGVDVYLAAtdgigpTAPGAGPSASFGTLWIKSPANMLGYWN 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6286 RPELTAEKFVESsflpgerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESG 6365
Cdd:PRK05857  391 NPERTAEVLIDG-------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEF 463
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 6366 QKQLCAYFVAEREL---TIGELR----AALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALPAPQGNAPVG 6430
Cdd:PRK05857  464 GALVGLAVVASAELdesAARALKhtiaARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKAR 535
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
7577-7926 5.53e-15

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 82.54  E-value: 5.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7577 SNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGAT-L 7655
Cdd:PLN02860  163 TELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAChV 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7656 YIPAKDTILdypLFESyMNENGITAAI-LPPTYAIYLSPDRL-------PSLKKLITGGSAASVEFVQQWKD---KVRYF 7724
Cdd:PLN02860  243 LLPKFDAKA---ALQA-IKQHNVTSMItVPAMMADLISLTRKsmtwkvfPSVRKILNGGGSLSSRLLPDAKKlfpNAKLF 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7725 NAYGPTEA-SIVT------------SVWAASPDGLDLRSVP------IGRPIANHQIFI-VDSQNHMlpvgvaGELCISG 7784
Cdd:PLN02860  319 SAYGMTEAcSSLTfmtlhdptlespKQTLQTVNQTKSSSVHqpqgvcVGKPAPHVELKIgLDESSRV------GRILTRG 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7785 AGLARGYLNRPELTAEKFVDNPFLAgermyrTGDLArWLPD-GNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQET 7863
Cdd:PLN02860  393 PHVMLGYWGQNSETASVLSNDGWLD------TGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASV 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7864 IVIARGDANGQQQLCAyFV--------ADRELTVSELRGTLSQE----------LPGYMIPSYFVQLE-QMPLTPNGKID 7924
Cdd:PLN02860  466 VVVGVPDSRLTEMVVA-CVrlrdgwiwSDNEKENAKKNLTLSSEtlrhhcreknLSRFKIPKLFVQWRkPFPLTTTGKIR 544

                  ..
gi 386647928 7925 RN 7926
Cdd:PLN02860  545 RD 546
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
4914-5385 5.73e-15

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 82.57  E-value: 5.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4914 TYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL-TQT 4992
Cdd:cd17642    46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFcSKK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 HLQE--RAQQWGQTLQAALCLD---DEAAYAEDASNVAN---------------VNEPHDLAYVIYTSGTTGRPKGVMIE 5052
Cdd:cd17642   126 GLQKvlNVQKKLKIIKTIIILDskeDYKGYQCLYTFITQnlppgfneydfkppsFDRDEQVALIMNSSGSTGLPKGVQLT 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5053 HRSLVNTAAGYRREYRLDQF--PVRLLQLASF--SFDVFVgdIARTLYNGGTMVICPKddridparlhywiSEEKITI-- 5126
Cdd:cd17642   206 HKNIVARFSHARDPIFGNQIipDTAILTVIPFhhGFGMFT--TLGYLICGFRVVLMYK-------------FEEELFLrs 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5127 ---FESTPALIIP-FMDYVAEHGL----DMSSMVLLITSSDSCSVTDYRVLQERFGSQFrIINAYGVTEAAIDSSLYDEP 5198
Cdd:cd17642   271 lqdYKVQSALLVPtLFAFFAKSTLvdkyDLSNLHEIASGGAPLSKEVGEAVAKRFKLPG-IRQGYGLTETTSAILITPEG 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5199 LAKLPEAGNVPIGKAAlnakfYIVDAHLNPVpVGV--LGELCIGGIGVARGYLNRPELTEEkfvdspFVEGERLYRTGDL 5276
Cdd:cd17642   350 DDKPGAVGKVVPFFYA-----KVVDLDTGKT-LGPneRGELCVKGPMIMKGYVNNPEATKA------LIDKDGWLHSGDI 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5277 ARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSEL------- 5349
Cdd:cd17642   418 AYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKevmdyva 497
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 386647928 5350 -RSSLSQELPGYMIpsyFVqlEQLPLTANGKIDRKAL 5385
Cdd:cd17642   498 sQVSTAKRLRGGVK---FV--DEVPKGLTGKIDRRKI 529
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
273-747 5.87e-15

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 82.75  E-value: 5.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  273 RPDAVA------VTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGL---MVErslEMIVGIMGILKAG-------GA 336
Cdd:cd05967    64 RGDQIAliydspVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympMIP---EAAIAMLACARIGaihsvvfGG 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  337 YVP------ID---PEY---------PEERIRYM------LEDSGTQ----VLLSQGHLQERVSFSGTWIRLDDEEAYHE 388
Cdd:cd05967   141 FAAkelasrIDdakPKLivtascgiePGKVVPYKplldkaLELSGHKphhvLVLNRPQVPADLTKPGRDLDWSELLAKAE 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  389 --DGSNLESvngpEHLTYVIYTSGTTGKPKGnltthrnIIRvvkntnyiDVTGQDKLLQLSSYSF----DGSTF----DI 458
Cdd:cd05967   221 pvDCVPVAA----TDPLYILYTSGTTGKPKG-------VVR--------DNGGHAVALNWSMRNIygikPGDVWwaasDV 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  459 ----------FGALLNGAKLVLV---PKETVlDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDC-------LRHARAI 518
Cdd:cd05967   282 gwvvghsyivYGPLLHGATTVLYegkPVGTP-DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGkyikkydLSSLRTL 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  519 LFGGERVSVSHVRKALGHLGPGKIKHvYGPTES----TVFATSYDVHEVEEGAVSIPIGGpisnTAIYIVNAQNKLQPIG 594
Cdd:cd05967   361 FLAGERLDPPTLEWAENTLGVPVIDH-WWQTETgwpiTANPVGLEPLPIKAGSPGKPVPG----YQVQVLDEDGEPVGPN 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  595 VAGELCVAGDgLARGYLNRPDLTAEKFADNPFA--PGerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAH 672
Cdd:cd05967   436 ELGNIVIKLP-LPPGCLLTLWKNDERFKKLYLSkfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEES 512
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  673 LLKLEAIEKATVV-VRESANGEKQLCaYYVADRSLP------ANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRR 745
Cdd:cd05967   513 VLSHPAVAECAVVgVRDELKGQVPLG-LVVLKEGVKitaeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRR 591

                  ..
gi 386647928  746 AL 747
Cdd:cd05967   592 TL 593
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
261-747 6.10e-15

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 82.42  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  261 TIHRLFEEQAERRPDAVAVTFED-----RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGG 335
Cdd:PRK08008    8 HLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  336 AYVPIDPEYPEERIRYMLEDSGTQVLLSQGhlqervSFSGTWIRLDDEEAYHEDG-----SNLESVNG-----------P 399
Cdd:PRK08008   88 IMVPINARLLREESAWILQNSQASLLVTSA------QFYPMYRQIQQEDATPLRHicltrVALPADDGvssftqlkaqqP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  400 EHLTY-----------VIYTSGTTGKPKGNLTTHRNIIRVVKNTNY-IDVTGQDKLLQ-LSSYSFDGSTFDIFGALLNGA 466
Cdd:PRK08008  162 ATLCYapplstddtaeILFTSGTTSRPKGVVITHYNLRFAGYYSAWqCALRDDDVYLTvMPAFHIDCQCTAAMAAFSAGA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  467 KLVLVPKETvldVAKLAGLIEKQQISV-----MFITTAffnVLVDMNPDCLRHA-RAILFG-----------GERVSVSh 529
Cdd:PRK08008  242 TFVLLEKYS---ARAFWGQVCKYRATItecipMMIRTL---MVQPPSANDRQHClREVMFYlnlsdqekdafEERFGVR- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  530 vrkalghlgpgkIKHVYGPTESTVFAtsydVHEVEEGAVSIP-IGGPISNTAIYIVNAQNKLQPIGVAGELC---VAGDG 605
Cdd:PRK08008  315 ------------LLTSYGMTETIVGI----IGDRPGDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICikgVPGKT 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  606 LARGYLNRPDLTAEKFAdnpfapGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV 685
Cdd:PRK08008  379 IFKEYYLDPKATAKVLE------ADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV 452
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928  686 -----VRESAngekqLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK08008  453 gikdsIRDEA-----IKAFVVlnEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
7591-7924 6.56e-15

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 80.04  E-value: 6.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7591 VIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLsFDASCWEIFKALFF--GATLYIPAKD--TILDy 7666
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTLMFTLATFHagGTNVFVRRVDaeEVLE- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7667 pLFESymnENGITAAILPPTYA--IYLSPDRLPSLKKLITGGSAASvefvqqWKDKV--------RYFNAYGPTEASIVT 7736
Cdd:cd17636    83 -LIEA---ERCTHAFLLPPTIDqiVELNADGLYDLSSLRSSPAAPE------WNDMAtvdtspwgRKPGGYGQTEVMGLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7737 sVWAASPDGLDLRSvpiGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKFVDnpflageRMYRT 7816
Cdd:cd17636   153 -TFAALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GWHHT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7817 GDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRG 7894
Cdd:cd17636   222 NDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkPGASVTEAELIE 301
                         330       340       350
                  ....*....|....*....|....*....|
gi 386647928 7895 TLSQELPGYMIPSYFVQLEQMPLTPNGKID 7924
Cdd:cd17636   302 HCRARIASYKKPKSVEFADALPRTAGGADD 331
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
1306-1667 6.97e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 81.98  E-value: 6.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1306 QAERTPEVAAVVYEN--DRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 1383
Cdd:PRK13390    6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1384 DRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAVLCLDDEA-AYAEDASNVANVNEPHDL----AYVIYTSGTTGRPKG 1458
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIdGFGSFEAALAGAGPRLTEqpcgAVMLYSSGTTGFPKG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1459 VM--IEHRSlvntaagyrreyrLDQFPVRLLQLASFSFDVFVGDI---ARTLYN-------------GGTMVICPKDDRI 1520
Cdd:PRK13390  166 IQpdLPGRD-------------VDAPGDPIVAIARAFYDISESDIyysSAPIYHaaplrwcsmvhalGGTVVLAKRFDAQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1521 DPARlhyWISEEKITIFESTPALIIPFMDYVAE--HGLDMSSMELLITSSDSCSVTDYRVLQERFGSqfrIINAYGVTEA 1598
Cdd:PRK13390  233 ATLG---HVERYRITVTQMVPTMFVRLLKLDADvrTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGP---IVYEYYSSTE 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 1599 AIDSSLYDEPlAKLPEAGNVpiGKAALnAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEE 1667
Cdd:PRK13390  307 AHGMTFIDSP-DWLAHPGSV--GRSVL-GDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA 371
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
4896-5257 7.15e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 81.98  E-value: 7.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4896 QAECTPEAAAVVYEN--DRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPS 4973
Cdd:PRK13390    6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4974 DRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQAALCLDDEA-AYAEDASNVANVNEPHDL----AYVIYTSGTTGRPKG 5048
Cdd:PRK13390   86 PEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIdGFGSFEAALAGAGPRLTEqpcgAVMLYSSGTTGFPKG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5049 VM--IEHRSlvntaagyrreyrLDQFPVRLLQLASFSFDVFVGDI---ARTLYN-------------GGTMVICPKDDRI 5110
Cdd:PRK13390  166 IQpdLPGRD-------------VDAPGDPIVAIARAFYDISESDIyysSAPIYHaaplrwcsmvhalGGTVVLAKRFDAQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5111 DPARlhyWISEEKITIFESTPALIIPFMDYVAE--HGLDMSSMVLLITSSDSCSVTDYRVLQERFGSqfrIINAYGVTEA 5188
Cdd:PRK13390  233 ATLG---HVERYRITVTQMVPTMFVRLLKLDADvrTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGP---IVYEYYSSTE 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5189 AIDSSLYDEPlAKLPEAGNVpiGKAALnAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEE 5257
Cdd:PRK13390  307 AHGMTFIDSP-DWLAHPGSV--GRSVL-GDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA 371
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
285-685 7.28e-15

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 82.13  E-value: 7.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  285 QLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLL-- 362
Cdd:cd05932     6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvg 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  363 ------SQGH-LQERV-----------SFSGTWIRLDDEEAYHEDgsnlESVNGPEHLTYVIYTSGTTGKPKGNLTTHRN 424
Cdd:cd05932    86 klddwkAMAPgVPEGLisislpppsaaNCQYQWDDLIAQHPPLEE----RPTRFPEQLATLIYTSGTTGQPKGVMLTFGS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  425 II----RVVkntNYIDVTGQDKLLqlsSY---------------SFDGST-------FDIFGALLNGAKLVL---VPKET 475
Cdd:cd05932   162 FAwaaqAGI---EHIGTEENDRML---SYlplahvtervfveggSLYGGVlvafaesLDTFVEDVQRARPTLffsVPRLW 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  476 VLDVAKLAGLIEKQQISVMfITTAFFNVLVD---MNPDCLRHARAILFGGERVSVS--HVRKALGHlgpgKIKHVYGPTE 550
Cdd:cd05932   236 TKFQQGVQDKIPQQKLNLL-LKIPVVNSLVKrkvLKGLGLDQCRLAGCGSAPVPPAllEWYRSLGL----NILEAYGMTE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  551 StvFATSYdvheveegavsipIGGPISNTAIYIVNAQNKLQ-PIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapg 629
Cdd:cd05932   311 N--FAYSH-------------LNYPGRDKIGTVGNAGPGVEvRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF--- 372
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  630 ermYRTGDLARWLPDGTIEYVGRIDDQVKI-RGFRIELGEIEAHLLKLEAIEKATVV 685
Cdd:cd05932   373 ---LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
255-675 8.92e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 82.02  E-value: 8.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  255 DYPRdTTIHRLfEEQAERRPDAV------AVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIM 328
Cdd:PRK12582   46 PYPR-SIPHLL-AKWAAEAPDRPwlaqrePGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  329 GILKAGGAYVPIDPEYPeerirymledsgtqvLLSQGHL----------------QERVSFSGTW--IRLDDEEAYHEDG 390
Cdd:PRK12582  124 AAMQAGVPAAPVSPAYS---------------LMSHDHAklkhlfdlvkprvvfaQSGAPFARALaaLDLLDVTVVHVTG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  391 S-----------------------NLESVnGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTNYIDVTGQDKLLQLS 447
Cdd:PRK12582  189 PgegiasiafadlaatpptaavaaAIAAI-TPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVS 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  448 ------SYSFDGSTfdIFGALL-NGAKLVLvpketvlDVAK-LAGLIEK-----QQIS--VMFITTAFFNVLVDM--NPD 510
Cdd:PRK12582  268 ldwmpwNHTMGGNA--NFNGLLwGGGTLYI-------DDGKpLPGMFEEtirnlREISptVYGNVPAGYAMLAEAmeKDD 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  511 CLRHA-----RAILFGGERVS-------VSHVRKALGHLGPgkIKHVYGPTESTvfATSYDVHEVEE--GAVSIPIGGpi 576
Cdd:PRK12582  339 ALRRSffknlRLMAYGGATLSddlyermQALAVRTTGHRIP--FYTGYGATETA--PTTTGTHWDTErvGLIGLPLPG-- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  577 sntaiyivnAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWL----PDGTIEYVGR 652
Cdd:PRK12582  413 ---------VELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGR 477
                         490       500
                  ....*....|....*....|....
gi 386647928  653 IDDQVKI-RGFRIELGEIEAHLLK 675
Cdd:PRK12582  478 VAEDFKLsTGTWVSVGTLRPDAVA 501
PLN02574 PLN02574
4-coumarate--CoA ligase-like
2359-2828 9.83e-15

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 81.81  E-value: 9.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVV--FEGQQLTYRELNERANRLARTL-QALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRIS 2435
Cdd:PLN02574   53 NGDTALIdsSTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2436 YMLEDSSAQVLLAQRRLQERVSFAGT-VVTVDDeqAYAGDGSNLESA-----------------VGPNDLAYIIYTSGTT 2497
Cdd:PLN02574  133 KRVVDCSVGLAFTSPENVEKLSPLGVpVIGVPE--NYDFDSKRIEFPkfyelikedfdfvpkpvIKQDDVAAIMYSSGTT 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2498 GKPKGVMVEHHGLCSLKQMF----ANTLQINAQDRVVQFASLSFDASCWEVFQT--LFFGATLYIPTKETILD-YQWFER 2570
Cdd:PLN02574  211 GASKGVVLTHRNLIAMVELFvrfeASQYEYPGSDNVYLAALPMFHIYGLSLFVVglLSLGSTIVVMRRFDASDmVKVIDR 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2571 YmsdnGITT-ATLPPTYAVYLN---PDHMPDFKRL--IAAGSA-SSLELLQQWKD---KVKYFNAYGPTEDsicTTIWTP 2640
Cdd:PLN02574  291 F----KVTHfPVVPPILMALTKkakGVCGEVLKSLkqVSCGAApLSGKFIQDFVQtlpHVDFIQGYGMTES---TAVGTR 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2641 --STEDISQLKSVPIGGPivNHRIYIVDAHYQP-VPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfepgERMYRTG 2717
Cdd:PLN02574  364 gfNTEKLSKYSSVGLLAP--NMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDK------DGWLRTG 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2718 DLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVGELRGE 2795
Cdd:PLN02574  436 DIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVrrQGSTLSQEAVINY 515
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 2796 LSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PLN02574  516 VAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
PRK13382 PRK13382
bile acid CoA ligase;
265-750 1.11e-14

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 81.73  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  265 LFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEY 344
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  345 PEERIRYMLEDSGTQVLLSQGHLQERV--SFSGT--------WIRLDDE---EAYHEDGSNLESVNGPEHLTYVIYTSGT 411
Cdd:PRK13382  128 AGPALAEVVTREGVDTVIYDEEFSATVdrALADCpqatrivaWTDEDHDltvEVLIAAHAGQRPEPTGRKGRVILLTSGT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  412 TGKPKGNLTTHRNIIRVVKNTnyIDVTG--QDKLLQLSSYSFDGSTFD--IFGALLngaKLVLVPKETVLDVAKLAgLIE 487
Cdd:PRK13382  208 TGTPKGARRSGPGGIGTLKAI--LDRTPwrAEEPTVIVAPMFHAWGFSqlVLAASL---ACTIVTRRRFDPEATLD-LID 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  488 KQQISVMFITTAFFNVLVD-----MNPDCLRHARAILFGGERVSVSHVRKALGHLGPgKIKHVYGPTESTVFATSY--DV 560
Cdd:PRK13382  282 RHRATGLAVVPVMFDRIMDlpaevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD-VIYNNYNATEAGMIATATpaDL 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  561 HEVEEGAvsipiGGPISNTAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRpdltaekfADNPFAPGerMYRTGDLAR 640
Cdd:PRK13382  361 RAAPDTA-----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG--------STKDFHDG--FMASGDVGY 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  641 WLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKqLCAYYV--ADRSLPANEVRSTLSQ 717
Cdd:PRK13382  426 LDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIgVDDEQYGQR-LAAFVVlkPGASATPETLKQHVRD 504
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928  718 ELPAYMLPSYFVQLEQMPLTTNGKVDRRALPAP 750
Cdd:PRK13382  505 NLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
2962-3161 1.46e-14

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 80.39  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2962 DEAAIRKVLQKLVEHHDALRVVFhKSENGyTAWNRAIGEGElyGLEVVDLKGIEESAQAVEAKAnEIQSSIDLEAGPFVK 3041
Cdd:cd19538    37 DVQALQQALYDVVERHESLRTVF-PEEDG-VPYQLILEEDE--ATPKLEIKEVDEEELESEINE-AVRYPFDLSEEPPFR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3042 AGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYR---TWSEQLAAYAQSPV--IERE 3115
Cdd:cd19538   112 ATLFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLPVQYAdyaLWQQELLGDESDPDslIARQ 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 3116 LAYWK-RVAQTEVQ-PLPKDEQVDVSLQQDSESISIEWTREETEQLLK 3161
Cdd:cd19538   192 LAYWKkQLAGLPDEiELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQ 239
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2930-3247 1.55e-14

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 80.11  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2930 SLTPIQH--WFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFHKSENGYTAWnraIGEGELYGLE 3007
Cdd:cd19533     3 PLTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQW---IDPYTPVPIR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3008 VVDLKGIEESAQAVEA-KANEIQSSIDLEAGPFVKAGLFQCADGDHLLIV-IHHGVVDGVSWRILLEDLAIGYEQAVKGE 3085
Cdd:cd19533    80 HIDLSGDPDPEGAAQQwMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFALFGQRVAEIYTALLKGR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3086 ELRFPAKTDaYRTWSEQLAAYAQSPVIERELAYWKRVAQTEVQPlpkdeqvdVSLQQDSESISIEWTR------EETEQL 3159
Cdd:cd19533   160 PAPPAPFGS-FLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEP--------VSLARRAPGRSLAFLRrtaelpPELTRT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3160 LKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGResimTDIDITRTVGWFTSKYPVVLELEQGKDISYLLKK 3239
Cdd:cd19533   231 LLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR----LGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQ 306

                  ....*...
gi 386647928 3240 TKEDLRGI 3247
Cdd:cd19533   307 VSRELRSL 314
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
399-747 1.55e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 79.45  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  399 PEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNTNYIDVTGQDKLL--QLSSYSFDGSTFDIFGALLNGAKLVLVP---- 472
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLlcGLPLFHVNGSVVTLLTPLASGAHVVLAGpagy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  473 -KETVLDvaKLAGLIEKQQI----SVMFITTAFFNVLVDMNPDCLRHAraiLFGGERVSVSHVRKALGHLGPgKIKHVYG 547
Cdd:cd05944    81 rNPGLFD--NFWKLVERYRItslsTVPTVYAALLQVPVNADISSLRFA---MSGAAPLPVELRARFEDATGL-PVVEGYG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  548 PTEST-VFATSYDVHEVEEGAVSIPIggPISNTAIYIVNAQ-NKLQPIGV--AGELCVAGDGLARGYLNRPDltaekfAD 623
Cdd:cd05944   155 LTEATcLVAVNPPDGPKRPGSVGLRL--PYARVRIKVLDGVgRLLRDCAPdeVGEICVAGPGVFGGYLYTEG------NK 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  624 NPFApGERMYRTGDLARWLPDGTIEYVGRIDDQVkIR-GFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAY--Y 700
Cdd:cd05944   227 NAFV-ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYvqL 304
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928  701 VADRSLPANEVRSTLSQELPAY-MLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05944   305 KPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
270-742 1.57e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 80.82  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPdAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERI 349
Cdd:PRK13390   10 APDRP-AVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  350 RYMLEDSGTQVLLSQ-----------GHLQERVSFSGtwiRLDDEEAYHedgSNLESVnGPEhLT------YVIYTSGTT 412
Cdd:PRK13390   89 DYIVGDSGARVLVASaaldglaakvgADLPLRLSFGG---EIDGFGSFE---AALAGA-GPR-LTeqpcgaVMLYSSGTT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  413 GKPKGnltthrniIRVVKNTNYIDVTGqDKLLQLSSYSFDGSTFDIF--------GALLNGAKLVLVPKETVL-----DV 479
Cdd:PRK13390  161 GFPKG--------IQPDLPGRDVDAPG-DPIVAIARAFYDISESDIYyssapiyhAAPLRWCSMVHALGGTVVlakrfDA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  480 AKLAGLIEKQQISVMFITTAFFNVLVDMNPDC-----LRHARAILFGGERVSVSHVRKALGHLGPgKIKHVYGPTES--- 551
Cdd:PRK13390  232 QATLGHVERYRITVTQMVPTMFVRLLKLDADVrtrydVSSLRAVIHAAAPCPVDVKHAMIDWLGP-IVYEYYSSTEAhgm 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  552 TVFAT-SYDVHeveEGAVSIPIGGpisntAIYIVNAQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEkfADNPFAPge 630
Cdd:PRK13390  311 TFIDSpDWLAH---PGSVGRSVLG-----DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP-- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  631 rMYRT-GDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKQLCAYYVADRSLPA 708
Cdd:PRK13390  379 -FWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgVPDPEMGEQVKAVIQLVEGIRGS 457
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 386647928  709 NEVRSTL----SQELPAYMLPSYFVQLEQMPLTTNGKV 742
Cdd:PRK13390  458 DELARELidytRSRIAHYKAPRSVEFVDELPRTPTGKL 495
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
2490-2825 1.99e-14

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 78.85  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2490 IIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDrvVQFASLSFdascwevFQT--LFFG-ATLYIPTKETILDY- 2565
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEAD--VYLNMLPL-------FHIagLNLAlATFHAGGANVVMEKf 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2566 ---QWFERYMSDNGITTATLPPTYAVYLNP--DHMPDFKRLIAAGSASSLELLQQWKDKV--KYFNAYGPTEDSICTTIw 2638
Cdd:cd17637    76 dpaEALELIEEEKVTLMGSFPPILSNLLDAaeKSGVDLSSLRHVLGLDAPETIQRFEETTgaTFWSLYGQTETSGLVTL- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2639 TPSTEdisqlKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGD 2718
Cdd:cd17637   155 SPYRE-----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHTGD 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2719 LAKWLPDGTIEYLGRIDHQ--VKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDA---SGQKQLCAyFVADRTMTVGELR 2793
Cdd:cd17637   223 LGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPkwgEGIKAVCV-LKPGATLTADELI 301
                         330       340       350
                  ....*....|....*....|....*....|..
gi 386647928 2794 GELSGELPGYMIPAHFVQLERMPLTPNGKIDR 2825
Cdd:cd17637   302 EFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
5936-6446 2.10e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 80.84  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERipDHLAVTFEDKQLTYGE-LNERANR--LARTLRNAGVQPDqmVGLMVERSLEMVVGMIAILKAGGAY 6012
Cdd:PRK13388    4 TIAQLLRDRAGD--DTIAVRYGDRTWTWREvLAEAAARaaALIALADPDRPLH--VGVLLGNTPEMLFWLAAAALGGYVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6013 VPIDP----DYPEDRIRYmledSGAKLLLV-QGH--LLDRASFADKLVNLNDDGAYHE---DGSNLEPVN--GPEHLTYV 6080
Cdd:PRK13388   80 VGLNTtrrgAALAADIRR----ADCQLLVTdAEHrpLLDGLDLPGVRVLDVDTPAYAElvaAAGALTPHRevDAMDPFML 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6081 IYTSGTTGRPKGVMVEHRNVVRL-VKNTNYVELNEQ------THILQTGAVVfdastfEIWG-ALLNGGRLYVVRNetiL 6152
Cdd:PRK13388  156 IFTSGTTGAPKAVRCSHGRLAFAgRALTERFGLTRDdvcyvsMPLFHSNAVM------AGWApAVASGAAVALPAK---F 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6153 DAVSLKNAIQQYGINTM-WLTAPLYNQLSQQDSGMFAGlKTLIVG-GDVLSVPHINRVLREHaGLSIVNGYGPTENTTfs 6230
Cdd:PRK13388  227 SASGFLDDVRRYGATYFnYVGKPLAYILATPERPDDAD-NPLRVAfGNEASPRDIAEFSRRF-GCQVEDGYGSSEGAV-- 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6231 tthTIVGEqkEAVP---IGKPINNSTAYIVDSkLSLLPVGVW-------------GELI-VGGDGVARGYLNRPELTAEK 6293
Cdd:PRK13388  303 ---IVVRE--PGTPpgsIGRGAPGVAIYNPET-LTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPEATAER 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6294 FVESSflpgercYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQKQLCAY 6372
Cdd:PRK13388  377 MRHGM-------YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYaVPDERVGDQVMAAL 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6373 FVAE-RELTIGELRAALS--QELPNYMIPSHFVPLERMPLTPNGKIDRRALPApQGNAPVGAEYV---------APRTEQ 6440
Cdd:PRK13388  450 VLRDgATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA-QGWATGDPVTLwvrrggpayRLMSEP 528

                  ....*.
gi 386647928 6441 EKALAA 6446
Cdd:PRK13388  529 AKAALA 534
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
260-765 2.33e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 80.46  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  260 TTIHRLFEEQAERrpDAVAVTFEDRQLTYGE-LNERANR--LARTLRNAGVQADqlVGLMVERSLEMIVGIMGILKAGGA 336
Cdd:PRK13388    3 DTIAQLLRDRAGD--DTIAVRYGDRTWTWREvLAEAAARaaALIALADPDRPLH--VGVLLGNTPEMLFWLAAAALGGYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  337 YVPIDP----EYPEERIRYmledSGTQVLLS-QGHLQ--ERVSFSGTWIRLDDEEAYHEDGSNLESVN-----GPEHLTY 404
Cdd:PRK13388   79 LVGLNTtrrgAALAADIRR----ADCQLLVTdAEHRPllDGLDLPGVRVLDVDTPAYAELVAAAGALTphrevDAMDPFM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 VIYTSGTTGKPKGNLTTHRNIIRV-VKNTNYIDVTGQDkLLQLSSYSFDGSTF--DIFGALLNGAKLVLVPKetvldvak 481
Cdd:PRK13388  155 LIFTSGTTGAPKAVRCSHGRLAFAgRALTERFGLTRDD-VCYVSMPLFHSNAVmaGWAPAVASGAAVALPAK-------- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  482 lagliekqqisvmFITTAFFnvlvdmnPDcLRHARAILFggervsvSHVRKALGHL--GPGK-------IKHVYG----P 548
Cdd:PRK13388  226 -------------FSASGFL-------DD-VRRYGATYF-------NYVGKPLAYIlaTPERpddadnpLRVAFGneasP 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  549 TESTVFATSYDVHEVE-----EGAVSI---------PIGGPISNTAIYivNAQNkLQPIGVA---------------GEL 599
Cdd:PRK13388  278 RDIAEFSRRFGCQVEDgygssEGAVIVvrepgtppgSIGRGAPGVAIY--NPET-LTECAVArfdahgallnadeaiGEL 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  600 C-VAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEA 678
Cdd:PRK13388  355 VnTAGAGFFEGYYNNPEATAERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPA 427
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  679 IEKATV-VVRESANGEKQLCAYYVAD-RSLPANEVRSTLS--QELPAYMLPSYFVQLEQMPLTTNGKVDRRALpapeesM 754
Cdd:PRK13388  428 INRVAVyAVPDERVGDQVMAALVLRDgATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKREL------I 501
                         570
                  ....*....|.
gi 386647928  755 ETGVEFVEPRT 765
Cdd:PRK13388  502 AQGWATGDPVT 512
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1439-1795 2.44e-14

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 80.69  E-value: 2.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1439 EPHDLAYVIYTSGTTGRPKGVMIEHRSLVN---------TAAGYRREYR------LDQFPVRLLQLASFSFdVFVGDIAR 1503
Cdd:PRK08751  206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVAnmqqahqwlAGTGKLEEGCevvitaLPLYHIFALTANGLVF-MKIGGCNH 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1504 TLYNggtmvicPKDdridparLHYWISEEKITIFESTPALIIPFMDYVAEHG---LDMSSMEllITSSDSCSVTdyRVLQ 1580
Cdd:PRK08751  285 LISN-------PRD-------MPGFVKELKKTRFTAFTGVNTLFNGLLNTPGfdqIDFSSLK--MTLGGGMAVQ--RSVA 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1581 ERFG--SQFRIINAYGVTEAAIDSSLydEPLaKLPEAgNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGY 1658
Cdd:PRK08751  347 ERWKqvTGLTLVEAYGLTETSPAACI--NPL-TLKEY-NGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGY 422
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1659 LNRPELTEEkfvdspFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA 1738
Cdd:PRK08751  423 WKRPEETAK------VMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDE 496
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 1739 K-GQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK08751  497 KsGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
PLN02246 PLN02246
4-coumarate--CoA ligase
4867-5312 2.48e-14

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 80.41  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4867 DEKAQIVHVFNPAAPDA--PENEAFHA-LFEKQAECTPEAAAVVYENDR-LTYRELNERANRLARTLRAQGVKPNQLVGI 4942
Cdd:PLN02246    1 EASASEEFIFRSKLPDIyiPNHLPLHDyCFERLSEFSDRPCLIDGATGRvYTYADVELLSRRVAAGLHKLGIRQGDVVML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4943 LADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQT----HLQERAQQWGQTLqaaLCLDDEAAYA 5018
Cdd:PLN02246   81 LLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQScyvdKLKGLAEDDGVTV---VTIDDPPEGC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5019 EDASNVANVNE---------PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA----GYRREYRLDQFPVRLLQLASF--- 5082
Cdd:PLN02246  158 LHFSELTQADEnelpeveisPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFHSDDVILCVLPMFhiy 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5083 SFD--VFVGdiartLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTPALIIPFM--DYVAEHglDMSS--MVLlit 5156
Cdd:PLN02246  238 SLNsvLLCG-----LRVGAAILIMPK---FEIGALLELIQRHKVTIAPFVPPIVLAIAksPVVEKY--DLSSirMVL--- 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5157 ssdSCSVTDYRVLQERFGSqfRIINA-----YGVTEA----AIDSSLYDEPLAKLPEAgnvpIGKAALNAKFYIVDAHLN 5227
Cdd:PLN02246  305 ---SGAAPLGKELEDAFRA--KLPNAvlgqgYGMTEAgpvlAMCLAFAKEPFPVKSGS----CGTVVRNAELKIVDPETG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5228 -PVPVGVLGELCIGGIGVARGYLNRPELTEekfvdspfvegerlyRTGDLARWMPDGNVDFI---------GRIDNQAKI 5297
Cdd:PLN02246  376 aSLPRNQPGEICIRGPQIMKGYLNDPEATA---------------NTIDKDGWLHTGDIGYIddddelfivDRLKELIKY 440
                         490
                  ....*....|....*
gi 386647928 5298 RGYRIETGEIETQLL 5312
Cdd:PLN02246  441 KGFQVAPAELEALLI 455
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
7470-7821 2.81e-14

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 80.17  E-value: 2.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7470 TQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYP-----EDRIRYMLE---- 7540
Cdd:cd05921    24 RRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlmsqdLAKLKHLFEllkp 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7541 -------------------DSGAQVLLTQRHL--QECVSFdgkviAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTG 7599
Cdd:cd05921   104 glvfaqdaapfaralaaifPLGTPLVVSRNAVagRGAISF-----AELAATPPTAAVDAAFAAVGPDTVAKFLFTSGSTG 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7600 KPKGVMVEHHGLCSLKLMFAETL-RITEEDRV-VQFASLSFDASCWEIFKA-LFFGATLYI----PAKDTILdyplfESY 7672
Cdd:cd05921   179 LPKAVINTQRMLCANQAMLEQTYpFFGEEPPVlVDWLPWNHTFGGNHNFNLvLYNGGTLYIddgkPMPGGFE-----ETL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7673 MNENGITaailpPTY-----------AIYLSPDR------LPSLKKLITGGSAASVEF--------VQQWKDKVRYFNAY 7727
Cdd:cd05921   254 RNLREIS-----PTVyfnvpagwemlVAALEKDEalrrrfFKRLKLMFYAGAGLSQDVwdrlqalaVATVGERIPMMAGL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7728 GPTEA--SIVTSVWAASPDGLdlrsvpIGRPIANHQIFIVdsqnhmlPVGVAGELCISGAGLARGYLNRPELTAEKFVDN 7805
Cdd:cd05921   329 GATETapTATFTHWPTERSGL------IGLPAPGTELKLV-------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEE 395
                         410
                  ....*....|....*.
gi 386647928 7806 PFlagermYRTGDLAR 7821
Cdd:cd05921   396 GF------YCLGDAAK 405
PLN02479 PLN02479
acetate-CoA ligase
7450-7930 2.84e-14

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 80.27  E-value: 2.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7450 GLFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPE 7529
Cdd:PLN02479   24 WFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7530 YPEDRIRYMLEDSGAQVLLTQRHLQECVSFDGKVIAaddeqayGEDGSNLEP----VVG-----PNHLAYVI-------- 7592
Cdd:PLN02479  104 LNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILA-------EKKKSSFKPplliVIGdptcdPKSLQYALgkgaieye 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7593 -------------------------YTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEdrVVQFASLS-FDASCW--- 7643
Cdd:PLN02479  177 kfletgdpefawkppadewqsialgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEG--AVYLWTLPmFHCNGWcft 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7644 -------------------EIFKAL-FFGATLYIPAK---DTILDYPLFEsymnengitaAILPptyaiylspdrLPSLK 7700
Cdd:PLN02479  255 wtlaalcgtniclrqvtakAIYSAIaNYGVTHFCAAPvvlNTIVNAPKSE----------TILP-----------LPRVV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7701 KLITGGSA--ASVEFVQQWKDkVRYFNAYGPTEASIVTSVWAASP--DGLD------LRSVPIGRPIANHQIFIVDSQNh 7770
Cdd:PLN02479  314 HVMTAGAAppPSVLFAMSEKG-FRVTHTYGLSETYGPSTVCAWKPewDSLPpeeqarLNARQGVRYIGLEGLDVVDTKT- 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7771 MLPV----GVAGELCISGAGLARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIE 7846
Cdd:PLN02479  392 MKPVpadgKTMGEIVMRGNMVMKGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENIS 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7847 LGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV-------ADRELTVSELRGTLSQELPGYMIPSYFVqLEQMPLTP 7919
Cdd:PLN02479  465 SLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTA 543
                         570
                  ....*....|.
gi 386647928 7920 NGKIDRNALPA 7930
Cdd:PLN02479  544 TGKIQKHVLRA 554
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
3869-4342 2.91e-14

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 80.32  E-value: 2.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3869 DAVAVVF----EKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIR 3944
Cdd:PRK04319   59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3945 YMLEDSGAQALLTQRHLRERVSFAG-----TFVAVDDEQ-------------AYHADGSNLEPvVGPNHLAYVIYTSGTT 4006
Cdd:PRK04319  139 DRLEDSEAKVLITTPALLERKPADDlpslkHVLLVGEDVeegpgtldfnalmEQASDEFDIEW-TDREDGAILHYTSGST 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4007 GKPKGV------MVEHH--GLCSLKLmfantlqmTEQDRV--------VQFASlsfdascWEIFKALFFGATLyiptstt 4070
Cdd:PRK04319  218 GKPKGVlhvhnaMLQHYqtGKYVLDL--------HEDDVYwctadpgwVTGTS-------YGIFAPWLNGATN------- 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4071 ILDYPLFE-----SYMNENGITATILPPTyaAYlnpdRM--------------PSLKKLITGGSAASVEFVqQWKDKVL- 4130
Cdd:PRK04319  276 VIDGGRFSperwyRILEDYKVTVWYTAPT--AI----RMlmgagddlvkkydlSSLRHILSVGEPLNPEVV-RWGMKVFg 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4131 --YFNAYGPTE-ASIVtsIWDEASDslgDRKSVPIGRPLANHRIYVVDSHNRMLPVGVAGELCI-----SgvgLARGYLN 4202
Cdd:PRK04319  349 lpIHDNWWMTEtGGIM--IANYPAM---DIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkgwpS---MMRGIWN 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4203 RPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDA-N 4281
Cdd:PRK04319  421 NPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPvR 493
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 4282 GqqQLVAYFVAQRELTAA------ELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA-----PEG 4342
Cdd:PRK04319  494 G--EIIKAFVALRPGYEPseelkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwelglPEG 563
PRK03584 PRK03584
acetoacetate--CoA ligase;
3860-4332 2.97e-14

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 80.61  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3860 FEEQALRN--PDAVAVVF-----EKSQLTYGELNERANRLARTLRDAGVRP-DQLVGLMVERSlEMVVGIMAIMKAGGAY 3931
Cdd:PRK03584   88 YAENLLRHrrDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAYLPNIP-ETVVAMLATASLGAIW 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3932 IPIDPEYPE----DRI--------------RY------MLEDSGA--------QALLTQRHLRERVSFAGTFVAVDDEQA 3979
Cdd:PRK03584  167 SSCSPDFGVqgvlDRFgqiepkvliavdgyRYggkafdRRAKVAElraalpslEHVVVVPYLGPAAAAAALPGALLWEDF 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3980 Y-HADGSNLEPV-VGPNHLAYVIYTSGTTGKPK-------GVMVEH---HGL-CSLKlmfantlqmtEQDRVVQFASLS- 4045
Cdd:PRK03584  247 LaPAEAAELEFEpVPFDHPLWILYSSGTTGLPKcivhghgGILLEHlkeLGLhCDLG----------PGDRFFWYTTCGw 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4046 ----FDAScweifkALFFGATLYI----PTsttildYP----LFEsYMNENGITatiLPPTYAAYLN--------PDR-- 4103
Cdd:PRK03584  317 mmwnWLVS------GLLVGATLVLydgsPF------YPdpnvLWD-LAAEEGVT---VFGTSAKYLDacekaglvPGEth 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4104 -MPSLKKLITGGSAASVE---FV-QQWKDKVLYFNAYGPTEasIVTSIwdeasdSLGdrksvpigrplanhriyvvdshN 4178
Cdd:PRK03584  381 dLSALRTIGSTGSPLPPEgfdWVyEHVKADVWLASISGGTD--ICSCF------VGG----------------------N 430
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4179 RMLPVgVAGELCISGVGLA------RGylnRPeLTAEK---FVDNPF----------EPGER-------MY----RTGDL 4228
Cdd:PRK03584  431 PLLPV-YRGEIQCRGLGMAveawdeDG---RP-VVGEVgelVCTKPFpsmplgfwndPDGSRyrdayfdTFpgvwRHGDW 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4229 VRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVaYFVAQRE---LTaAELRATM 4305
Cdd:PRK03584  506 IEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMP-LFVVLAEgvtLD-DALRARI 583
                         570       580       590
                  ....*....|....*....|....*....|..
gi 386647928 4306 SQEL-----PNYmIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK03584  584 RTTIrtnlsPRH-VPDKIIAVPDIPRTLSGKK 614
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
3876-4330 3.21e-14

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 80.19  E-value: 3.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3876 EKSQLTYGELNERANRLARTLR-DAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPI-------------------- 3934
Cdd:cd17632    64 RFETITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLqagasaaqlapilaeteprl 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3935 ---DPEYPEDRIRYMLEDSGAQALLTQRHLRE-----------RVSFAGTFVAVDDEQAYHADGSNLEPV------VGPN 3994
Cdd:cd17632   144 lavSAEHLDLAVEAVLEGGTPPRLVVFDHRPEvdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAplfrpePDDD 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3995 HLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVV-QFASLSFDASCWEIFKALFFGATLYIPTS----- 4068
Cdd:cd17632   224 PLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITlNFMPMSHIAGRISLYGTLARGGTAYFAAAsdmst 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4069 ----------TTILDYP-----LFESYMNE------NGITATILPPTYAAYLNPDRMPslKKLITG--GSAASVEFVQQW 4125
Cdd:cd17632   304 lfddlalvrpTELFLVPrvcdmLFQRYQAEldrrsvAGADAETLAERVKAELRERVLG--GRLLAAvcGSAPLSAEMKAF 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4126 KDKVL---YFNAYGPTEASIVtsiwdeasdSLGDRKSVPigrPLANHRI--------YVVDS-HNRmlpvgvaGELCISG 4193
Cdd:cd17632   382 MESLLdldLHDGYGSTEAGAV---------ILDGVIVRP---PVLDYKLvdvpelgyFRTDRpHPR-------GELLVKT 442
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4194 VGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDHQVKirgyrIELGEVETqLAKIDAVQEAI 4273
Cdd:cd17632   443 DTLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLK-----LSQGEFVT-VARLEAVFAAS 510
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 4274 VLARE---DANGQQQ-LVAYFV----AQRELTAAELRA---------TMSQELPNYMIPSYFVqLAQMPLTP-NG 4330
Cdd:cd17632   511 PLVRQifvYGNSERAyLLAVVVptqdALAGEDTARLRAalaeslqriAREAGLQSYEIPRDFL-IETEPFTIaNG 584
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
3869-4357 3.81e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 79.69  E-value: 3.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3869 DAVAVVFEKSQLTYGE-LNERANR--LARTLRDAGVRPDqlVGLMVERSLEMVVGIMAIMKAGGAYIPIDP----EYPED 3941
Cdd:PRK13388   16 DTIAVRYGDRTWTWREvLAEAAARaaALIALADPDRPLH--VGVLLGNTPEMLFWLAAAALGGYVLVGLNTtrrgAALAA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3942 RIRYmledSGAQALLT---QRHLRERVSFAGTFVAVDDEQAYH---ADGSNLEPV--VGPNHLAYVIYTSGTTGKPKGV- 4012
Cdd:PRK13388   94 DIRR----ADCQLLVTdaeHRPLLDGLDLPGVRVLDVDTPAYAelvAAAGALTPHreVDAMDPFMLIFTSGTTGAPKAVr 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4013 ------------MVEHHGL-------CSLKLMFANTLQMTEQDRVVQFASLSFDAScweiFKA-------LFFGATlyip 4066
Cdd:PRK13388  170 cshgrlafagraLTERFGLtrddvcyVSMPLFHSNAVMAGWAPAVASGAAVALPAK----FSAsgflddvRRYGAT---- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4067 tsttildyplfesYMNENG-----ITATILPPTYAAylNPDRmpslkklITGGSAAS----VEFVQQWKDKVlyFNAYGP 4137
Cdd:PRK13388  242 -------------YFNYVGkplayILATPERPDDAD--NPLR-------VAFGNEASprdiAEFSRRFGCQV--EDGYGS 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4138 TE-ASIVTSiwdeasdslgDRKSVP--IGRPLANHRIY-----------VVDSHNRML-PVGVAGELC-ISGVGLARGYL 4201
Cdd:PRK13388  298 SEgAVIVVR----------EPGTPPgsIGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELVnTAGAGFFEGYY 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4202 NRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN 4281
Cdd:PRK13388  368 NNPEATAERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDER 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4282 GQQQLVAYFVAQRE--LTAAELRATMS--QELPNYMIPSYFVQLAQMPLTPNGKIDRKALPApEGSMHAGGEYVAPRTPT 4357
Cdd:PRK13388  441 VGDQVMAALVLRDGatFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA-QGWATGDPVTLWVRRGG 519
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
1318-1795 3.88e-14

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 79.40  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1318 YENDRLTYRELNERANRLARMLR-AQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAAS 1396
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1397 VLLTqthlqeraqqwgqtlqavlclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHR------SLVNTA 1470
Cdd:cd05937    81 FVIV--------------------------------------DPDDPAILIYTSGTTGLPKAAAISWRrtlvtsNLLSHD 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1471 AGYRREYRLdQFPVRLLQLASFsfdvFVGDIArTLYNGGTMVICPKDDridpARlHYW--ISEEKITIFEstpaliipfm 1548
Cdd:cd05937   123 LNLKNGDRT-YTCMPLYHGTAA----FLGACN-CLMSGGTLALSRKFS----AS-QFWkdVRDSGATIIQ---------- 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1549 dYVAEHGldmssmELLITSSDSCSVTDYRV---------------LQERFGSQfRIINAYGVTEAAIDS-SLYDEPLAKL 1612
Cdd:cd05937   182 -YVGELC------RYLLSTPPSPYDRDHKVrvawgnglrpdiwerFRERFNVP-EIGEFYAATEGVFALtNHNVGDFGAG 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1613 PEAGNVPIGKAALNAKFYIVDAHLNP--------------VPVGVLGELcIGGI-----GVARGYLNRPELTEEKFVDSP 1673
Cdd:cd05937   254 AIGHHGLIRRWKFENQVVLVKMDPETddpirdpktgfcvrAPVGEPGEM-LGRVpfknrEAFQGYLHNEDATESKLVRDV 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1674 FVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLK----AEGVREAVVVVREDAKGQKVLCAY-- 1747
Cdd:cd05937   333 FRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAhpdiAEANVYGVKVPGHDGRAGCAAITLee 412
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 1748 -FTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05937   413 sSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
PRK13382 PRK13382
bile acid CoA ligase;
4853-5388 4.14e-14

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 79.80  E-value: 4.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4853 DPAAKIA-SLGILTADEKAQivhVFNPAAPDA---------PENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERA 4922
Cdd:PRK13382    2 GIKDRLRdTLGLIATLRRAG---LIAPMRPDRylrivaamrREGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4923 NRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQthlqeraQQWG 5002
Cdd:PRK13382   79 DALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD-------EEFS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5003 QTLQAALcldDEAAYAedASNVANVNEPHDLAY---------------------VIYTSGTTGRPKGVmieHRSLVNTAA 5061
Cdd:PRK13382  152 ATVDRAL---ADCPQA--TRIVAWTDEDHDLTVevliaahagqrpeptgrkgrvILLTSGTTGTPKGA---RRSGPGGIG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5062 GYRReyRLDQFPVRLLQLASFSFDVF----VGDIARTLYNGGTMVIcpkDDRIDPARLHYWISEEKITIFESTPALIIPF 5137
Cdd:PRK13382  224 TLKA--ILDRTPWRAEEPTVIVAPMFhawgFSQLVLAASLACTIVT---RRRFDPEATLDLIDRHRATGLAVVPVMFDRI 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5138 MDYVAEhGLDMSSMVLL--ITSSDSCSVTD-YRVLQERFGSQfrIINAYGVTEAAIDSSLYDEPLAKLPEAGnvpiGKAA 5214
Cdd:PRK13382  299 MDLPAE-VRNRYSGRSLrfAAASGSRMRPDvVIAFMDQFGDV--IYNNYNATEAGMIATATPADLRAAPDTA----GRPA 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5215 LNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYlnrpelTEEKfvDSPFVEGerLYRTGDLARWMPDGNVDFIGRIDNQ 5294
Cdd:PRK13382  372 EGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------TSGS--TKDFHDG--FMASGDVGYLDENGRLFVVGRDDEM 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5295 AKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKvLCAHFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQ 5371
Cdd:PRK13382  442 IVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQyGQR-LAAFVVLKPGASATpeTLKQHVRDNLANYKVPRDIVVLDE 520
                         570
                  ....*....|....*..
gi 386647928 5372 LPLTANGKIDRKALPAP 5388
Cdd:PRK13382  521 LPRGATGKILRRELQAR 537
PLN02614 PLN02614
long-chain acyl-CoA synthetase
2350-2765 4.20e-14

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 80.06  E-value: 4.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2350 LFEEQAERIPDHPAV----VFEGQQ-----LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGG 2420
Cdd:PLN02614   50 VFRMSVEKYPNNPMLgrreIVDGKPgkyvwQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2421 AYVPIDPEYPEDRISYMLEDSSAQVLLAQRR---------------LQERVSFAGT-------------VVTVDDEQAYA 2472
Cdd:PLN02614  130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKkiselfktcpnsteyMKTVVSFGGVsreqkeeaetfglVIYAWDEFLKL 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2473 GDGSNLESAVG-PNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQ-----INAQDRVVQFASLS--FDASCWEV 2544
Cdd:PLN02614  210 GEGKQYDLPIKkKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAhiFDRVIEEC 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2545 FqtLFFGATLYI-------------PTKETI-------LD--YQWFERYMSDNGITTATLPPTYAVY------LNPDHM- 2595
Cdd:PLN02614  290 F--IQHGAAIGFwrgdvklliedlgELKPTIfcavprvLDrvYSGLQKKLSDGGFLKKFVFDSAFSYkfgnmkKGQSHVe 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2596 --PDFKRLI------------------AAGSASSLELLQQWKDKVKYFNAYGPTEDsiCTTIWTPSTEDISQLKSVPIGG 2655
Cdd:PLN02614  368 asPLCDKLVfnkvkqglggnvriilsgAAPLASHVESFLRVVACCHVLQGYGLTES--CAGTFVSLPDELDMLGTVGPPV 445
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2656 PIVNHRIYIV-DAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRI 2734
Cdd:PLN02614  446 PNVDIRLESVpEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDRK 518
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 2735 DHQVKI-RGYRIELGEIEEQLLKVASVQEAIV 2765
Cdd:PLN02614  519 KNIFKLsQGEYVAVENIENIYGEVQAVDSVWV 550
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1323-1795 4.45e-14

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 79.89  E-value: 4.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARML-RAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 1401
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 THLQERAQQWGQTLQAV---LCLDDEAA---------YAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNT 1469
Cdd:PLN02574  147 PENVEKLSPLGVPVIGVpenYDFDSKRIefpkfyeliKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAM 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1470 AAGYRR-EYRLDQFP----VRLLQLASF---SFDVFVGDIartLYNGGTMVICPKDDRIDPARLhywISEEKITIFESTP 1541
Cdd:PLN02574  227 VELFVRfEASQYEYPgsdnVYLAALPMFhiyGLSLFVVGL---LSLGSTIVVMRRFDASDMVKV---IDRFKVTHFPVVP 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 ALIIPFMDyvAEHGLDMSSMELLITSSDSCSVTDYRVLQE--RFGSQFRIINAYGVTEAAIDSS--LYDEPLAKLPEagn 1617
Cdd:PLN02574  301 PILMALTK--KAKGVCGEVLKSLKQVSCGAAPLSGKFIQDfvQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSS--- 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1618 vpIGKAALNAKFYIVDAHLNP-VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVegerlyRTGDLARWMPDGNVD 1696
Cdd:PLN02574  376 --VGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYFDEDGYLY 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1697 FIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKLSE--LRSSLSQELPGYMIPS 1774
Cdd:PLN02574  448 IVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQeaVINYVAKQVAPYKKVR 527
                         490       500
                  ....*....|....*....|.
gi 386647928 1775 YFVQLEQLPLTANGKIDRKAL 1795
Cdd:PLN02574  528 KVVFVQSIPKSPAGKILRREL 548
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
5959-6332 4.88e-14

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 79.40  E-value: 4.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5959 KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYP-----EDRIRYMLEDSGA 6033
Cdd:cd05921    24 RRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlmsqdLAKLKHLFELLKP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6034 KLLLVQghllDRASFADKLVNLNDDG--------------AYH----------EDGSNLEPVNGPEHLTYVIYTSGTTGR 6089
Cdd:cd05921   104 GLVFAQ----DAAPFARALAAIFPLGtplvvsrnavagrgAISfaelaatpptAAVDAAFAAVGPDTVAKFLFTSGSTGL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6090 PKGVMVEHRNVvrlvknTNYVELNEQTHILQTG--AVVFD----ASTF---EIWGALL-NGGRLYVVRNETI--LDAVSL 6157
Cdd:cd05921   180 PKAVINTQRML------CANQAMLEQTYPFFGEepPVLVDwlpwNHTFggnHNFNLVLyNGGTLYIDDGKPMpgGFEETL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6158 KNAiqqYGINTMW-LTAPL-YNQLSQ---QDSGM----FAGLKTLIVGGDVLSvPHI----NRVLREHAGLSI--VNGYG 6222
Cdd:cd05921   254 RNL---REISPTVyFNVPAgWEMLVAaleKDEALrrrfFKRLKLMFYAGAGLS-QDVwdrlQALAVATVGERIpmMAGLG 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6223 PTENTTFSTThtIVGEQKEAVPIGKPINNSTayivdskLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKFVESSFlpg 6302
Cdd:cd05921   330 ATETAPTATF--THWPTERSGLIGLPAPGTE-------LKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF--- 397
                         410       420       430
                  ....*....|....*....|....*....|....
gi 386647928 6303 ercYRTGDLARWL----PDGTLEYKGRIDEQVKI 6332
Cdd:cd05921   398 ---YCLGDAAKLAdpddPAKGLVFDGRVAEDFKL 428
PLN03102 PLN03102
acyl-activating enzyme; Provisional
5945-6420 5.05e-14

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 79.68  E-value: 5.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PLN03102   24 SECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 RYMLEDSGAKLLLVQGHLLDRASFADKLVNLNDDGAY------HEDGSNLEPVNgpEHLTY------------------- 6079
Cdd:PLN03102  104 AAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNlpvifiHEIDFPKRPSS--EELDYecliqrgeptpslvarmfr 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6080 ---------VIYTSGTTGRPKGVMVEHRNVVrlvkntnyveLNEQTHIL--QTGAVVFDASTFEI---------WGALLN 6139
Cdd:PLN03102  182 iqdehdpisLNYTSGTTADPKGVVISHRGAY----------LSTLSAIIgwEMGTCPVYLWTLPMfhcngwtftWGTAAR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6140 GGRLYVVRNETildAVSLKNAIQQYGINTMWLTAPLYNQL---SQQDSGMFAGLKTLIVGGDVLSVPHINRVlrEHAGLS 6216
Cdd:PLN03102  252 GGTSVCMRHVT---APEIYKNIEMHNVTHMCCVPTVFNILlkgNSLDLSPRSGPVHVLTGGSPPPAALVKKV--QRLGFQ 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6217 IVNGYGPTENT---TF----STTHTIVGEQKEAVPIGKPINNSTAYIVDSK----LSLLPVG--VWGELIVGGDGVARGY 6283
Cdd:PLN03102  327 VMHAYGLTEATgpvLFcewqDEWNRLPENQQMELKARQGVSILGLADVDVKnketQESVPRDgkTMGEIVIKGSSIMKGY 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6284 LNRPELTAEKFvESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDE 6363
Cdd:PLN03102  407 LKNPKATSEAF-KHGWL------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 6364 SGQKQLCAYFVAER-ELTIGELRAAL-----------SQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:PLN03102  480 TWGETPCAFVVLEKgETTKEDRVDKLvtrerdlieycRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
6520-6836 5.12e-14

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 78.58  E-value: 5.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6520 EIGLTPIQR--WFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGYAAwnRAIGEGELYS 6597
Cdd:cd19539     1 RIPLSFAQErlWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPR--QEILPPGPAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6598 LEVADFRDVKSA-EQAVEAKANEIQSSI-DLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQAA 6674
Cdd:cd19539    79 LEVRDLSDPDSDrERRLEELLRERESRGfDLDEEPPIRAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAALYAARR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6675 KGEEVRLPAKTDSFRTWSEQLAAYAQSPAMENERAYW-EQIAQTAVAPLPKDKQSDRSLQQDSESITIQWSRKETEQlLK 6753
Cdd:cd19539   159 KGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWrRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAA-LR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6754 KVHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGResimTDIDITRTVGWFTSKYPVLLQMEPGRSLSTRIKKVK 6833
Cdd:cd19539   238 ELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGR----NHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVR 313

                  ...
gi 386647928 6834 EDL 6836
Cdd:cd19539   314 KAL 316
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
5029-5385 5.25e-14

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 79.54  E-value: 5.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5029 EPHDLAYVIYTSGTTGRPKGVMIEHRSLVN---------TAAGYRREYR------LDQFPVRLLQLASFSFdVFVGDIAR 5093
Cdd:PRK08751  206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVAnmqqahqwlAGTGKLEEGCevvitaLPLYHIFALTANGLVF-MKIGGCNH 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5094 TLYNggtmvicPKDdridparLHYWISEEKITIFESTPALIIPFMDYVAEHG---LDMSSmvLLITSSDSCSVTdyRVLQ 5170
Cdd:PRK08751  285 LISN-------PRD-------MPGFVKELKKTRFTAFTGVNTLFNGLLNTPGfdqIDFSS--LKMTLGGGMAVQ--RSVA 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5171 ERFG--SQFRIINAYGVTEAAIDSSLydEPLaKLPEAgNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGY 5248
Cdd:PRK08751  347 ERWKqvTGLTLVEAYGLTETSPAACI--NPL-TLKEY-NGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGY 422
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5249 LNRPELTEEkfvdspFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA 5328
Cdd:PRK08751  423 WKRPEETAK------VMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDE 496
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 5329 K-GQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK08751  497 KsGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1810-1883 5.28e-14

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 70.65  E-value: 5.28e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1810 APRTPQEAKLASIWQEVLGL--EKVGVKDNFF-ELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIAR 1883
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1296-1791 5.52e-14

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 80.39  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1296 NEVFHALFEKQAERTP-EVAAVVYENDRLTYRELNERANRLARMLRAqGVKPNQLVGILADRSADLLVGALAVWKAGgaY 1374
Cdd:PRK06814  631 RTLFEALIEAAKIHGFkKLAVEDPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAG--R 707
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1375 VPLdpdypsdriqfMLEDSAAS-------------VLLT------QTHLQERAQQWGQTLqAVLCLDDEAAYAEDASNVA 1435
Cdd:PRK06814  708 VPA-----------MINFSAGIanilsackaaqvkTVLTsrafieKARLGPLIEALEFGI-RIIYLEDVRAQIGLADKIK 775
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1436 ------------NVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAgyrreyrldqfpvrllQLASfSFDVFVGDIAr 1503
Cdd:PRK06814  776 gllagrfplvyfCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRA----------------QVAA-RIDFSPEDKV- 837
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1504 tlYN-----------GGTMVicPKDDRID----PARLHYWISEEKI-----TIFESTPALIIPFMDYVaeHGLDMSSMEL 1563
Cdd:PRK06814  838 --FNalpvfhsfgltGGLVL--PLLSGVKvflyPSPLHYRIIPELIydtnaTILFGTDTFLNGYARYA--HPYDFRSLRY 911
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1564 LITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEA----AIDSSLYDEPlaklpeaGNVpiGKAALNakfyiVDAHLNPV 1639
Cdd:PRK06814  912 VFAGAEKVKEETRQTWMEKFG--IRILEGYGVTETapviALNTPMHNKA-------GTV--GRLLPG-----IEYRLEPV 975
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1640 PvGVL--GELCIGGIGVARGYLnrpeLTEEKFVDSPFVEGErlYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEI 1717
Cdd:PRK06814  976 P-GIDegGRLFVRGPNVMLGYL----RAENPGVLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAV 1048
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1718 ETQLLKAEGVREAVVVVREDA-KGQKVLcaYFTAESELKLSE-LRSSLSQELPGYMIPSYFVQLEQLPLTANGKID 1791
Cdd:PRK06814 1049 EELAAELWPDALHAAVSIPDArKGERII--LLTTASDATRAAfLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
3855-4358 5.88e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 79.39  E-value: 5.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3855 TIHGLFEEQALRNPDAVAVVF---------EKSQLTYGELNERANRLARTLRDAGVRPDQlVGLMVERSLEMVVGIMAIM 3925
Cdd:PRK07769   22 NLVRHVERWAKVRGDKLAYRFldfsterdgVARDLTWSQFGARNRAVGARLQQVTKPGDR-VAILAPQNLDYLIAFFGAL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3926 KAGGAYIPI-DPEYP--EDRIRYMLEDSGAQALLTQ-----------RHL----RERVsfagtfVAVD---DEQayhadG 3984
Cdd:PRK07769  101 YAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTtdsaegvrkffRARpakeRPRV------IAVDavpDEV-----G 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3985 SNLEPVVgPNH--LAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGAT 4062
Cdd:PRK07769  170 ATWVPPE-ANEdtIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHY 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4063 LYIPTSTTILDYPlfESYMNENGITATILPPTYAAYLN------------PDRMPSL-----KKLITGGSAASVEFVQQW 4125
Cdd:PRK07769  249 ITFMSPAAFVRRP--GRWIRELARKPGGTGGTFSAAPNfafehaaarglpKDGEPPLdlsnvKGLLNGSEPVSPASMRKF 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4126 KDKVLYFN--------AYGPTEAS--IVTSIWDEAS-------DSLGDRKSVPI-------------GRPLANHRIYVVD 4175
Cdd:PRK07769  327 NEAFAPYGlpptaikpSYGMAEATlfVSTTPMDEEPtviyvdrDELNAGRFVEVpadapnavaqvsaGKVGVSEWAVIVD 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4176 SHNRM-LPVGVAGELCISGVGLARGYLNRPELTAEKF---VDNPF--------EPGERMYRTGDLVRWLpDGNLEYLGRI 4243
Cdd:PRK07769  407 PETASeLPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLseshaegaPDDALWVRTGDYGVYF-DGELYITGRV 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4244 DHQVKIRGYR-----IELGEVET-----------------QLAKIDAVQEAIVLAREDANGQQQLVayFVAQRELTAAEL 4301
Cdd:PRK07769  486 KDLVIIDGRNhypqdLEYTAQEAtkalrtgyvaafsvpanQLPQVVFDDSHAGLKFDPEDTSEQLV--IVAERAPGAHKL 563
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 4302 ---------RATMSQelpNYMIPSYFVQLAQ---MPLTPNGKIDRKALPAP--EGSMHAGgeYVAPRTPTE 4358
Cdd:PRK07769  564 dpqpiaddiRAAIAV---RHGVTVRDVLLVPagsIPRTSSGKIARRACRAAylDGSLRSG--YGQPAFPDA 629
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
3818-4243 6.04e-14

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 79.54  E-value: 6.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3818 TASPNAPVSMLELVTEAEKAE--IIHVFNNTA-AEYQQeqTIHGLFEEQALRNPDAVAVVFEKSQ-----LTYGELNERA 3889
Cdd:PRK08180    2 TPARYRPVAFAPPAVEVERRAdgTIYLRSAEPlGDYPR--RLTDRLVHWAQEAPDRVFLAERGADggwrrLTYAEALERV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3890 NRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEY---PED--RIRYMLE---------DSGA--- 3952
Cdd:PRK08180   80 RAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYslvSQDfgKLRHVLElltpglvfaDDGAafa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3953 ---QALLT----------QRHLRERVSFA---GTFVAVDDEQAYHAdgsnlepvVGPNHLAYVIYTSGTTGKPKGVMVEH 4016
Cdd:PRK08180  160 ralAAVVPadvevvavrgAVPGRAATPFAallATPPTAAVDAAHAA--------VGPDTIAKFLFTSGSTGLPKAVINTH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4017 HGLCSLKLMFANTLQMTEQDRVVQFASL----SFDAScwEIFK-ALFFGATLYI----PTsttildyplfesymnENGIT 4087
Cdd:PRK08180  232 RMLCANQQMLAQTFPFLAEEPPVLVDWLpwnhTFGGN--HNLGiVLYNGGTLYIddgkPT---------------PGGFD 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4088 ATI-----LPPTY-----------AAYLNPDrmPSLK-------KLITGGSAASVEFVqqWKD-----------KVLYFN 4133
Cdd:PRK08180  295 ETLrnlreISPTVyfnvpkgwemlVPALERD--AALRrrffsrlKLLFYAGAALSQDV--WDRldrvaeatcgeRIRMMT 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4134 AYGPTEASIVTSIWDEASDSLGDrksvpIGRPLANHRIyvvdshnRMLPVGVAGELCISGVGLARGYLNRPELTAEKFVD 4213
Cdd:PRK08180  371 GLGMTETAPSATFTTGPLSRAGN-----IGLPAPGCEV-------KLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDE 438
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 4214 NPFepgermYRTGDLVRWL----PDGNLEYLGRI 4243
Cdd:PRK08180  439 EGY------YRSGDAVRFVdpadPERGLMFDGRI 466
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
1314-1795 6.54e-14

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 79.41  E-value: 6.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1314 AAVVYEND------RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAG-------GAYvplDPD 1380
Cdd:PRK00174   84 VAIIWEGDdpgdsrKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGF---SAE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1381 YPSDRIQfmleDSAASVLLTqthlqerA-QQW--GQTL---QAVlcldDEAAyaEDASNVANV------------NEPHD 1442
Cdd:PRK00174  161 ALADRII----DAGAKLVIT-------AdEGVrgGKPIplkANV----DEAL--ANCPSVEKVivvrrtggdvdwVEGRD 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1443 LAY-----------------------VIYTSGTTGRPKGVMieHrslvnTAAGYrreyrldqfpvrLLQlASFSF----- 1494
Cdd:PRK00174  224 LWWhelvagasdecepepmdaedplfILYTSGSTGKPKGVL--H-----TTGGY------------LVY-AAMTMkyvfd 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1495 ----DVF-----VGDIarT---------LYNGGTMVI---CPkdDRIDPARlhYW--ISEEKITIFESTPALIIPFM--- 1548
Cdd:PRK00174  284 ykdgDVYwctadVGWV--TghsyivygpLANGATTLMfegVP--NYPDPGR--FWevIDKHKVTIFYTAPTAIRALMkeg 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1549 -DYVAEHglDMSSMELLitssdsCSVTD----------YRVLQerfGSQFRIINAYGVTE-AAIdsslydePLAKLPeaG 1616
Cdd:PRK00174  358 dEHPKKY--DLSSLRLL------GSVGEpinpeawewyYKVVG---GERCPIVDTWWQTEtGGI-------MITPLP--G 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1617 NVPI--GKAAL-----NAKfyIVDAHLNPVPVGVLGELCIGGI--GVARGYLNRPElteeKFVDSPFVEGERLYRTGDLA 1687
Cdd:PRK00174  418 ATPLkpGSATRplpgiQPA--VVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGA 491
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1688 RWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLK----AE----GvreavvvVREDAKGQkVLCAYFT------AESE 1753
Cdd:PRK00174  492 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAhpkvAEaavvG-------RPDDIKGQ-GIYAFVTlkggeePSDE 563
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 1754 LKlSELRSSLSQEL-----PGYMipsYFVqlEQLPLTANGKIDRKAL 1795
Cdd:PRK00174  564 LR-KELRNWVRKEIgpiakPDVI---QFA--PGLPKTRSGKIMRRIL 604
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
4908-5385 7.55e-14

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 78.63  E-value: 7.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4908 YENDRLTYRELNERANRLARTLR-AQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAAS 4986
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4987 VLLTqthlqeraqqwgqtlqaalclddeaayaedasnvanvnEPHDLAYVIYTSGTTGRPKGVMIEHR------SLVNTA 5060
Cdd:cd05937    81 FVIV--------------------------------------DPDDPAILIYTSGTTGLPKAAAISWRrtlvtsNLLSHD 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5061 AGYRREYRLdQFPVRLLQLASFsfdvFVGDIArTLYNGGTMVICPKDDridpARlHYW--ISEEKITIFEstpaliipfm 5138
Cdd:cd05937   123 LNLKNGDRT-YTCMPLYHGTAA----FLGACN-CLMSGGTLALSRKFS----AS-QFWkdVRDSGATIIQ---------- 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5139 dYVAEHGLdmssmvLLITSSDSCSVTDYRV---------------LQERFGSQfRIINAYGVTEAAIDS-SLYDEPLAKL 5202
Cdd:cd05937   182 -YVGELCR------YLLSTPPSPYDRDHKVrvawgnglrpdiwerFRERFNVP-EIGEFYAATEGVFALtNHNVGDFGAG 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5203 PEAGNVPIGKAALNAKFYIVDAHLNP--------------VPVGVLGELcIGGI-----GVARGYLNRPELTEEKFVDSP 5263
Cdd:cd05937   254 AIGHHGLIRRWKFENQVVLVKMDPETddpirdpktgfcvrAPVGEPGEM-LGRVpfknrEAFQGYLHNEDATESKLVRDV 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5264 FVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLK----AEGVREAVVVVREDAKGQKVLCA--- 5336
Cdd:cd05937   333 FRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAhpdiAEANVYGVKVPGHDGRAGCAAITlee 412
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 5337 HFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05937   413 SSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
PRK05857 PRK05857
fatty acid--CoA ligase;
260-759 7.78e-14

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 78.90  E-value: 7.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  260 TTIHRLFEeQAERRPDAVAVTFED--RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAY 337
Cdd:PRK05857   15 TVLDRVFE-QARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  338 VPIDPEYPEERI-RYMLEDSGTQVLLSQG------HLQERVSfSGTWIRLDDEEAYHEDGSNLESVNGPEHLTY------ 404
Cdd:PRK05857   94 VMADGNLPIAAIeRFCQITDPAAALVAPGskmassAVPEALH-SIPVIAVDIAAVTRESEHSLDAASLAGNADQgsedpl 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 -VIYTSGTTGKPKGNLTTHR------NIIRvVKNTNYID-VTGQDKLLQLSSYSFdGSTFDIFGALLNGAKLVLVPKETv 476
Cdd:PRK05857  173 aMIFTSGTTGEPKAVLLANRtffavpDILQ-KEGLNWVTwVVGETTYSPLPATHI-GGLWWILTCLMHGGLCVTGGENT- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  477 ldvAKLAGLIEKQQISVMFITTAFFNVLV---DMNPDCLRHARAILFGGERVSVSHVR--KALGHlgpgKIKHVYGPTES 551
Cdd:PRK05857  250 ---TSLLEILTTNAVATTCLVPTLLSKLVselKSANATVPSLRLVGYGGSRAIAADVRfiEATGV----RTAQVYGLSET 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  552 TVFA-----TSYDVHEVEEGAVsipiGGPISNTAIYIVNAQN------KLQPIGVAGELCVAGDGLARGYLNRPDLTAEK 620
Cdd:PRK05857  323 GCTAlclptDDGSIVKIEAGAV----GRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  621 FADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAhllkleaiekatvvVRESANGEKQLCAYY 700
Cdd:PRK05857  399 LIDG-------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDR--------------IAEGVSGVREAACYE 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  701 VADRS---------LPANEVRSTLSQELP------------AYMLPSYFVQLEQMPLTTNGKVDRRALPAPEESMETGVE 759
Cdd:PRK05857  458 IPDEEfgalvglavVASAELDESAARALKhtiaarfrresePMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVV 537
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
1323-1701 7.98e-14

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 78.94  E-value: 7.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL--T 1400
Cdd:cd05933     9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVveN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1401 QTHLQERAQQWGQ--TLQAVLCLDDEAAYAEDA-------------------SNVANVNEPHDLAYVIYTSGTTGRPKGV 1459
Cdd:cd05933    89 QKQLQKILQIQDKlpHLKAIIQYKEPLKEKEPNlyswdefmelgrsipdeqlDAIISSQKPNQCCTLIYTSGTTGMPKGV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 MIEHRSLVNTAAGYRREYRLDQFPVR---------LLQLASFSFDVFVG-DIARTLYNG------GTMVICPKDDRidPA 1523
Cdd:cd05933   169 MLSHDNITWTAKAASQHMDLRPATVGqesvvsylpLSHIAAQILDIWLPiKVGGQVYFAqpdalkGTLVKTLREVR--PT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1524 RL----HYW--ISEE-KITIFESTP---ALIIPFMDYVAEHglDMSSMELLITSSDSCSVTDYRVLQE-----------R 1582
Cdd:cd05933   247 AFmgvpRVWekIQEKmKAVGAKSGTlkrKIASWAKGVGLET--NLKLMGGESPSPLFYRLAKKLVFKKvrkalgldrcqK 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1583 FGS----------QF------RIINAYGVTEAAIDSSLydeplaKLPEAGNV-PIGKAALNAKFYIVdahlNPVPVGVlG 1645
Cdd:cd05933   325 FFTgaapisretlEFflslniPIMELYGMSETSGPHTI------SNPQAYRLlSCGKALPGCKTKIH----NPDADGI-G 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1646 ELCIGGIGVARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRI 1701
Cdd:cd05933   394 EICFWGRHVFMGYLNMEDKTEEA------IDEDGWLHSGDLGKLDEDGFLYITGRI 443
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
5-219 8.05e-14

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 78.17  E-value: 8.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    5 AFERETAFWNKIFEGEEnPPTALPY----SKAQKQAPALVRRmstALSKEVSERIIQMSK--GAPLpaYMILLTGVQSLL 78
Cdd:cd19531   187 VLERQLAYWREQLAGAP-PVLELPTdrprPAVQSFRGARVRF---TLPAELTAALRALARreGATL--FMTLLAAFQVLL 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   79 YKYTSSSSILVGMPVVtkpneNR-RP---------VNQLViLREEVRDDSTFKALLGEAKNSVTSSINHQNVPFrlmtER 148
Cdd:cd19531   261 HRYSGQDDIVVGTPVA-----GRnRAelegligffVNTLV-LRTDLSGDPTFRELLARVRETALEAYAHQDLPF----EK 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  149 L--ELQ------YAdgvPVVNTLVAlkqLHITDYRQSAVSDVLFE----------FEL------DKDEVRLHLTYNGNLY 204
Cdd:cd19531   331 LveALQperdlsRS---PLFQVMFV---LQNAPAAALELPGLTVEplevdsgtakFDLtlslteTDGGLRGSLEYNTDLF 404
                         250
                  ....*....|....*
gi 386647928  205 TESFIAQAVDHLNRL 219
Cdd:cd19531   405 DAATIERMAGHFQTL 419
PRK05850 PRK05850
acyl-CoA synthetase; Validated
5936-6419 8.38e-14

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 78.83  E-value: 8.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5936 TIHQLFEEQAERIPDHLAVTFED---------KQLTYGELNERANRLARTLRNAGVQPDQMVGLmVERSLEMVVGMIAIL 6006
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGSTGDRAVIL-APQGLEYIVAFLGAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6007 KAGGAYVPIDPDYP---EDRIRYMLEDSGAKLLL------------VQGHLLDRASFADKLVNLNDDGayhEDGSNLEPV 6071
Cdd:PRK05850   81 QAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLttsavvddvteyVAPQPGQSAPPVIEVDLLDLDS---PRGSDARPR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6072 NGPEhLTYVIYTSGTTGRPKGVMVEHRNVVrlvknTNYVELnEQTHILQTGAVVFDASTFEIW-------GALLN----- 6139
Cdd:PRK05850  158 DLPS-TAYLQYTSGSTRTPAGVMVSHRNVI-----ANFEQL-MSDYFGDTGGVPPPDTTVVSWlpfyhdmGLVLGvcapi 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6140 -GGRLYVvrnetILDAVSL--KNA--IQQYGINT-MWLTAPlyN---QLSQQ---DSGMfAGL-----KTLIVGGDVLSV 6202
Cdd:PRK05850  231 lGGCPAV-----LTSPVAFlqRPArwMQLLASNPhAFSAAP--NfafELAVRktsDDDM-AGLdlggvLGIISGSERVHP 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6203 PHINRV--------LREHAglsIVNGYGPTENTTFSTThTIVGEQKEAVPI------------------------GKPiN 6250
Cdd:PRK05850  303 ATLKRFadrfapfnLRETA---IRPSYGLAEATVYVAT-REPGQPPESVRFdyeklsaghakrcetgggtplvsyGSP-R 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6251 NSTAYIVDSKLSL-LPVGVWGELIVGGDGVARGYLNRPELTAEKF----VE-SSFLPGERCYRTGDLArWLPDGTLEYKG 6324
Cdd:PRK05850  378 SPTVRIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlVDpSPGTPEGPWLRTGDLG-FISEGELFIVG 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6325 RIDEQVKIRGyR------IE----------------LGEIEEQLLKVASVKEATvivREDESGQKQLCAyfvAERELTig 6382
Cdd:PRK05850  457 RIKDLLIVDG-RnhypddIEatiqeitggrvaaisvPDDGTEKLVAIIELKKRG---DSDEEAMDRLRT---VKREVT-- 527
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 6383 elrAALSQelpnymipSH--------FVPLERMPLTPNGKIDRRA 6419
Cdd:PRK05850  528 ---SAISK--------SHglsvadlvLVAPGSIPITTSGKIRRAA 561
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
5400-5473 8.43e-14

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 70.27  E-value: 8.43e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 5400 APRTPQEAKLVSIWQEVLGL--EKVGVKDNFF-ELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIAR 5473
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1274-1724 8.64e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 78.93  E-value: 8.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1274 LTVEEKAQLVHVF-NPAAPDAPENEVFHALFEKQAERtPEVAAVVYEN------DRLTYRELNERANRLARMLRAQGVKP 1346
Cdd:PRK12582   26 ISVERRADGSIVIkSRHPLGPYPRSIPHLLAKWAAEA-PDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1347 NQLVGILADRSADLLVGALAVWKAGGAYVPLDPDY---PSD--RIQFMLEDSAASVLLTQTHLQ-ERA----QQWGQTL- 1415
Cdd:PRK12582  105 GRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmSHDhaKLKHLFDLVKPRVVFAQSGAPfARAlaalDLLDVTVv 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1416 --------QAVLCLDDEAAY---AEDASNVANVNePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA---GYRREYRLDQ 1481
Cdd:PRK12582  185 hvtgpgegIASIAFADLAATpptAAVAAAIAAIT-PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAmqeQLRPREPDPP 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1482 FPVrLLQLASFSfDVFVGDIA--RTLYNGGTMVIcpKDDRIDPARLHYWIS---EEKITIFESTP---ALIIPFMDYVAE 1553
Cdd:PRK12582  264 PPV-SLDWMPWN-HTMGGNANfnGLLWGGGTLYI--DDGKPLPGMFEETIRnlrEISPTVYGNVPagyAMLAEAMEKDDA 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1554 HGLDM-SSMELLITSSDSCSVTDYRVLQE----RFGSQFRIINAYGVTEAA-IDSSLYDEP----LAKLPEAGnvpigka 1623
Cdd:PRK12582  340 LRRSFfKNLRLMAYGGATLSDDLYERMQAlavrTTGHRIPFYTGYGATETApTTTGTHWDTervgLIGLPLPG------- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1624 alnakfyivdAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfvEGERLYRTGDLARWM----PDGNVDFIG 1699
Cdd:PRK12582  413 ----------VELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF------DEEGFYRLGDAARFVdpddPEKGLIFDG 476
                         490       500
                  ....*....|....*....|....*.
gi 386647928 1700 RIDNQAKI-RGYRIETGEIETQLLKA 1724
Cdd:PRK12582  477 RVAEDFKLsTGTWVSVGTLRPDAVAA 502
PLN03102 PLN03102
acyl-activating enzyme; Provisional
3868-4337 8.90e-14

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 78.91  E-value: 8.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML 3947
Cdd:PLN03102   28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3948 EDSGAQALLTQRHL----RERVSFAGT----------FVAVDD--------EQAYHADGSNLEPVvgPNHLAYVI----- 4000
Cdd:PLN03102  108 RHAKPKILFVDRSFeplaREVLHLLSSedsnlnlpviFIHEIDfpkrpsseELDYECLIQRGEPT--PSLVARMFriqde 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4001 -------YTSGTTGKPKGVMVEHHG--LCSLKLMFANTLQMTEqdrVVQFASLSFDASCWeifkALFFGATLYIPTSTTI 4071
Cdd:PLN03102  186 hdpislnYTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCP---VYLWTLPMFHCNGW----TFTWGTAARGGTSVCM 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4072 LDYPLFESYMN--ENGIT-ATILPPTYAAYLNPDRMPSLKK-----LITGGS---AASVEFVQQWKDKVLYfnAYGPTEA 4140
Cdd:PLN03102  259 RHVTAPEIYKNieMHNVThMCCVPTVFNILLKGNSLDLSPRsgpvhVLTGGSpppAALVKKVQRLGFQVMH--AYGLTEA 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4141 S--IVTSIWDEASDSLGDRKSVPIG--RPLANHRIYVVDSHNRMLPVGVA------GELCISGVGLARGYLNRPELTAEK 4210
Cdd:PLN03102  337 TgpVLFCEWQDEWNRLPENQQMELKarQGVSILGLADVDVKNKETQESVPrdgktmGEIVIKGSSIMKGYLKNPKATSEA 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4211 FVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYF 4290
Cdd:PLN03102  417 FKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 4291 VAQRELTAAELRATM------------SQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PLN03102  490 VLEKGETTKEDRVDKlvtrerdlieycRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PLN02574 PLN02574
4-coumarate--CoA ligase-like
286-747 1.14e-13

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 78.35  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLSQ 364
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  365 GHLQERVSFSGTWIRLDDEEAYHEDGSNLES----------------VNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIRV 428
Cdd:PLN02574  147 PENVEKLSPLGVPVIGVPENYDFDSKRIEFPkfyelikedfdfvpkpVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAM 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  429 VK-----NTNYIDVTGQDK--LLQLSSYSFDGSTFDIFGALLNGAKLVLVPKetvLDVAKLAGLIEKQQIS----VMFIT 497
Cdd:PLN02574  227 VElfvrfEASQYEYPGSDNvyLAALPMFHIYGLSLFVVGLLSLGSTIVVMRR---FDASDMVKVIDRFKVThfpvVPPIL 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  498 TAFFNVLVDMNPDCLRHARAILFGG---ERVSVSHVRKALGHLgpgKIKHVYGPTESTVFATSYDVHEVEEGAVSIPIGG 574
Cdd:PLN02574  304 MALTKKAKGVCGEVLKSLKQVSCGAaplSGKFIQDFVQTLPHV---DFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLA 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  575 PisNTAIYIVN-AQNKLQPIGVAGELCVAGDGLARGYLNRPDLTAEKfADNpfapgERMYRTGDLARWLPDGTIEYVGRI 653
Cdd:PLN02574  381 P--NMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQST-IDK-----DGWLRTGDIAYFDEDGYLYIVDRL 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  654 DDQVKIRGFRIELGEIEAHLLKLEAIEKATV---------------VVRESANGEKQLCAY-YVADRSLPANEVRSTlsq 717
Cdd:PLN02574  453 KEIIKYKGFQIAPADLEAVLISHPEIIDAAVtavpdkecgeipvafVVRRQGSTLSQEAVInYVAKQVAPYKKVRKV--- 529
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928  718 elpaymlpsyfVQLEQMPLTTNGKVDRRAL 747
Cdd:PLN02574  530 -----------VFVQSIPKSPAGKILRREL 548
PRK09192 PRK09192
fatty acyl-AMP ligase;
3877-4309 1.18e-13

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 78.51  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3877 KSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAG---------------GAYIpidpeypeD 3941
Cdd:PRK09192   47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvpvplplpmgfggrESYI--------A 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3942 RIRYMLEDSGAQALLTQRHLRERVS---------FAGTFVAVDDEQAYHADgsnlEPVVGPNHLAYVIYTSGTTGKPKGV 4012
Cdd:PRK09192  119 QLRGMLASAQPAAIITPDELLPWVNeathgnpllHVLSHAWFKALPEADVA----LPRPTPDDIAYLQYSSGSTRFPRGV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4013 MVEHHGLCS-LKLMFANTLQMTEQDRVVQFASLSFDAScweifkalFFGATLYIPTSTTILDY---------PL-FESYM 4081
Cdd:PRK09192  195 IITHRALMAnLRAISHDGLKVRPGDRCVSWLPFYHDMG--------LVGFLLTPVATQLSVDYlptrdfarrPLqWLDLI 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4082 NENGitATI-LPPTYAAYLNPDRMPSLKKLI----------TGGSAASVEFVQQWKDKV--LYFNA------YGPTEASI 4142
Cdd:PRK09192  267 SRNR--GTIsYSPPFGYELCARRVNSKDLAEldlscwrvagIGADMIRPDVLHQFAEAFapAGFDDkafmpsYGLAEATL 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4143 VTSIWDEAS---------DSL-GDRKSVPI-------------GRPLANHRIYVVDSHNRMLPVGVAGELCISGVGLARG 4199
Cdd:PRK09192  345 AVSFSPLGSgivveevdrDRLeYQGKAVAPgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSG 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4200 YLNRPELTAEKFVDNPFEpgermyrTGDLvRWLPDGNLEYLGRIDHQVKIRGYRI---ELGEVETQLAKIDAvQEAIVLA 4276
Cdd:PRK09192  425 YFRDEESQDVLAADGWLD-------TGDL-GYLLDGYLYITGRAKDLIIINGRNIwpqDIEWIAEQEPELRS-GDAAAFS 495
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 4277 REDANGQQQLVayfVAQRELTAAELRATMSQEL 4309
Cdd:PRK09192  496 IAQENGEKIVL---LVQCRISDEERRGQLIHAL 525
PRK08162 PRK08162
acyl-CoA synthetase; Validated
7453-7928 1.32e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 78.07  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7453 EEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPE 7532
Cdd:PRK08162   25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7533 DRIRYMLEDSGAQVLLTQRHLQECVS-----FDGK---VIAADD-EQAYGEDGSNLE----PVVGPNHLAYVI------- 7592
Cdd:PRK08162  105 ASIAFMLRHGEAKVLIVDTEFAEVARealalLPGPkplVIDVDDpEYPGGRFIGALDyeafLASGDPDFAWTLpadewda 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7593 ----YTSGTTGKPKGVMVEHHG--------------------LCSLKlMF--------------AET---LRiteedrvv 7631
Cdd:PRK08162  185 ialnYTSGTTGNPKGVVYHHRGaylnalsnilawgmpkhpvyLWTLP-MFhcngwcfpwtvaarAGTnvcLR-------- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7632 qfaslSFDAScwEIFKAL-------FFGA----TLYIPAKDT---ILDYPLfesymneNGITAAILPPTyaiylspdrlp 7697
Cdd:PRK08162  256 -----KVDPK--LIFDLIrehgvthYCGApivlSALINAPAEwraGIDHPV-------HAMVAGAAPPA----------- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7698 slkKLITGGSAASVEFVQqwkdkvryfnAYGPTEASIVTSV--WAASPDGLDL--RSVPIGRP-IANH---QIFIVDSQN 7769
Cdd:PRK08162  311 ---AVIAKMEEIGFDLTH----------VYGLTETYGPATVcaWQPEWDALPLdeRAQLKARQgVRYPlqeGVTVLDPDT 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7770 hMLPVG----VAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWLPDGNIeylgridhQVKIR---- 7841
Cdd:PRK08162  378 -MQPVPadgeTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYI--------KIKDRskdi 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7842 ----GYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAyFVADRE---LTVSELRGTLSQELPGYMIPSYFVqLEQ 7914
Cdd:PRK08162  442 iisgGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCA-FVELKDgasATEEEIIAHCREHLAGFKVPKAVV-FGE 519
                         570
                  ....*....|....
gi 386647928 7915 MPLTPNGKIDRNAL 7928
Cdd:PRK08162  520 LPKTSTGKIQKFVL 533
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1440-1795 1.58e-13

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 76.37  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1440 PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIC-PKDD 1518
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgPAGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1519 RIDPARLHYW--ISEEKITIFESTPALIIPFMDyvAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSQfrIINAYGVT 1596
Cdd:cd05944    81 RNPGLFDNFWklVERYRITSLSTVPTVYAALLQ--VPVNADISSLRFAMSGAAPLPVELRARFEDATGLP--VVEGYGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1597 EAAIDSSLYDEPLAKLPeaGNVPIGKAALNAKFYIVDA---HLNPVPVGVLGELCIGGIGVARGYLNRpELTEEKFVDsp 1673
Cdd:cd05944   157 EATCLVAVNPPDGPKRP--GSVGLRLPYARVRIKVLDGvgrLLRDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVA-- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1674 fvegERLYRTGDLARWMPDGNVDFIGRidnqAK---IRG-YRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFT 1749
Cdd:cd05944   232 ----DGWLNTGDLGRLDADGYLFITGR----AKdliIRGgHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQ 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 1750 AESELKLS--ELRSSLSQELPGY-MIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05944   304 LKPGAVVEeeELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
2490-2824 1.59e-13

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 76.19  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2490 IIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVV------QFASLSFdasCWEVFqtLFFGATLYIPTketiL 2563
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLnsgplfHIGTLMF---TLATF--HAGGTNVFVRR----V 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2564 DYQWFERYMSDNGITTATL-PPTYA--VYLNPDHMPDFKRLIAAGSASSlellqqWKDKV--------KYFNAYGPTEds 2632
Cdd:cd17636    76 DAEEVLELIEAERCTHAFLlPPTIDqiVELNADGLYDLSSLRSSPAAPE------WNDMAtvdtspwgRKPGGYGQTE-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2633 iCTTIWTPSTEDISQLKSVPIGGPIVnhRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDnpfepgeR 2712
Cdd:cd17636   148 -VMGLATFAALGGGAIGGAGRPSPLV--QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------G 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2713 MYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV--ADRTMTVG 2790
Cdd:cd17636   218 WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkPGASVTEA 297
                         330       340       350
                  ....*....|....*....|....*....|....
gi 386647928 2791 ELRGELSGELPGYMIPAHFVQLERMPLTPNGKID 2824
Cdd:cd17636   298 ELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
2357-2828 1.84e-13

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 77.48  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2357 RIPDHPAVVFEGQQL------------TYRELNERANRLARTLQALGVKTDQPVGLM---LERSLEMVVGMFAVlkaGGA 2421
Cdd:PRK06018   14 RIIDHAARIHGNREVvtrsvegpivrtTYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2422 YVPIDPEYPEDRISYMLEDSSAQVLLAQ-------RRLQERV-SFAGTVVTVDDEQ----------AY-----AGDGSNL 2478
Cdd:PRK06018   91 CHTVNPRLFPEQIAWIINHAEDRVVITDltfvpilEKIADKLpSVERYVVLTDAAHmpqttlknavAYeewiaEADGDFA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2479 ESAVGPNDLAYIIYTSGTTGKPKGVMVEHHG--LCSLKQMFANTLQINAQDRVVQFASLsFDASCWEV-FQTLFFGATLY 2555
Cdd:PRK06018  171 WKTFDENTAAGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2556 IPTKEtiLDYQWFERYMSDNGIT-TATLPPTYAVYLNpdHM-------PDFKRLIAAGSASSLELLQQWKD-KVKYFNAY 2626
Cdd:PRK06018  250 MPGAK--LDGASVYELLDTEKVTfTAGVPTVWLMLLQ--YMekeglklPHLKMVVCGGSAMPRSMIKAFEDmGVEVRHAW 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2627 GPTEDSICTTIWT--PSTEDISQLKSVPI----GGPIVNHRIYIVDAHYQPVPV-GVA-GELCIAGVGLARGYLNRPD-- 2696
Cdd:PRK06018  326 GMTEMSPLGTLAAlkPPFSKLPGDARLDVlqkqGYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYYRVDGei 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2697 LTAEKFVDnpfepgermyrTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA--HDDASGQ 2774
Cdd:PRK06018  406 LDDDGFFD-----------TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGvyHPKWDER 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2775 KQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK06018  475 PLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
7469-7928 1.84e-13

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 77.47  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7469 NTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLL 7548
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7549 TqRHLQECvsfdgkviaadDEQAYGEdgSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEED 7628
Cdd:cd05939    81 F-NLLDPL-----------LTQSSTE--PPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPED 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7629 RVvqFASLSFDASCWEIF---KALFFGATLYIPAK--------DTILDYPLFESYMNEngITAAILPPTYAIYLSPDRLp 7697
Cdd:cd05939   147 VV--YDCLPLYHSAGGIMgvgQALLHGSTVVIRKKfsasnfwdDCVKYNCTIVQYIGE--ICRYLLAQPPSEEEQKHNV- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7698 slkKLITG-GSAASVefvqqWKDKVRYFNA------YGPTE--ASIVTSVWAASPDGLDLRSVPIGRPIANHQI------ 7762
Cdd:cd05939   222 ---RLAVGnGLRPQI-----WEQFVRRFGIpqigefYGATEgnSSLVNIDNHVGACGFNSRILPSVYPIRLIKVdedtge 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7763 FIVDSQNHMLPV--GVAGELC---ISGAGLAR--GYLNRPElTAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRID 7835
Cdd:cd05939   294 LIRDSDGLCIPCqpGEPGLLVgkiIQNDPLRRfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTG 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7836 HQVKIRGYRIELGEIEEQLLKIASVQETIV--IARGDANGQQQLCAYFVADRELTVSELRGTLSQELPGYMIPSYFVQLE 7913
Cdd:cd05939   373 DTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLP 452
                         490
                  ....*....|....*
gi 386647928 7914 QMPLTPNGKIDRNAL 7928
Cdd:cd05939   453 EVDKTGTFKLQKTDL 467
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
283-747 2.29e-13

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 77.08  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  283 DRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLL 362
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  363 SQgHLQERVSFSgtwirldDEEAYHEDGSNLESVngpehLTYvIYTSGTTGKPKGNLTTHRNIIRVVKNTNY-IDVTGQD 441
Cdd:cd05939    81 FN-LLDPLLTQS-------STEPPSQDDVNFRDK-----LFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYaFGMRPED 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  442 KLLQ-LSSYSFDGSTFDIFGALLNGAKLVLVPKETV----LDVAKLAGLIeKQQISVMfittAFFNVLVDMNPDCLRHAR 516
Cdd:cd05939   147 VVYDcLPLYHSAGGIMGVGQALLHGSTVVIRKKFSAsnfwDDCVKYNCTI-VQYIGEI----CRYLLAQPPSEEEQKHNV 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  517 AILFG-GERVSVShvRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAVSI--PIGGPIS------NTAIYIVNAQ 587
Cdd:cd05939   222 RLAVGnGLRPQIW--EQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRilPSVYPIRlikvdeDTGELIRDSD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  588 NKLQPI--GVAGELC---VAGDGLAR--GYLNRPDlTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIR 660
Cdd:cd05939   300 GLCIPCqpGEPGLLVgkiIQNDPLRRfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWK 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  661 GFRIELGEIEAHLLKLEAIEKATV--VVRESANGEKQLCAYYVADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTT 738
Cdd:cd05939   379 GENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTG 458

                  ....*....
gi 386647928  739 NGKVDRRAL 747
Cdd:cd05939   459 TFKLQKTDL 467
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
5959-6358 2.51e-13

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 77.46  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5959 KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLV 6038
Cdd:cd17641    10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6039 Q------------------------------GHLLDRASFADKLVNLNDDGAYHEDGSNLEPVNG--PEHLTYVIYTSGT 6086
Cdd:cd17641    90 EdeeqvdklleiadripsvryviycdprgmrKYDDPRLISFEDVVALGRALDRRDPGLYEREVAAgkGEDVAVLCTTSGT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6087 TGRPKGVMVEHRNVVRlvKNTNYVELNEqthiLQTGAVVFD--------ASTFEIWGALLNGGRLYVVRNETildavSLK 6158
Cdd:cd17641   170 TGKPKLAMLSHGNFLG--HCAAYLAADP----LGPGDEYVSvlplpwigEQMYSVGQALVCGFIVNFPEEPE-----TMM 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6159 NAIQQYGINTMWLTAPLY-NQLSQ-----QDS----------GMFAGLKTLIVGGDVLSVPH------------INRVLR 6210
Cdd:cd17641   239 EDLREIGPTFVLLPPRVWeGIAADvrarmMDAtpfkrfmfelGMKLGLRALDRGKRGRPVSLwlrlaswladalLFRPLR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6211 EHAGLSIVNG--------------------------YGPTENTTFSTTHTivGEQKEAVPIGKPINNSTAYIVDSklsll 6264
Cdd:cd17641   319 DRLGFSRLRSaatggaalgpdtfrffhaigvplkqlYGQTELAGAYTVHR--DGDVDPDTVGVPFPGTEVRIDEV----- 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6265 pvgvwGELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKI-RGYRIELGEIE 6343
Cdd:cd17641   392 -----GEILVRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIE 460
                         490
                  ....*....|....*
gi 386647928 6344 EQLLKVASVKEATVI 6358
Cdd:cd17641   461 NKLKFSPYIAEAVVL 475
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1323-1795 2.58e-13

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 76.45  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPldpdypsdriqfmledsaASVLLTQT 1402
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 HLQERAQQWGqtlqAVLCLDDEAAYAEDASnvanvnephdLAYviYTSGTTGRPKGVMIEHRSlvntaagyrreyrldqF 1482
Cdd:cd05974    63 DLRDRVDRGG----AVYAAVDENTHADDPM----------LLY--FTSGTTSKPKLVEHTHRS----------------Y 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1483 PVRLLQlASFSFDVFVGDIARTL----------------YNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIP 1546
Cdd:cd05974   111 PVGHLS-TMYWIGLKPGDVHWNIsspgwakhawscffapWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRM 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1547 FMDYvaehglDMSSMEL----LITSSDSCSVTDYRVLQERFGSQFRiiNAYGVTEAAIdsslydeplaklpEAGNVP--- 1619
Cdd:cd05974   190 LIQQ------DLASFDVklreVVGAGEPLNPEVIEQVRRAWGLTIR--DGYGQTETTA-------------LVGNSPgqp 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1620 -----IGKAALNAKFYIVDAHLNPVPVGVLGeLCIGG---IGVARGYLNRPELTEEkfvdspfVEGERLYRTGDLARWMP 1691
Cdd:cd05974   249 vkagsMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDtrpVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDE 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1692 DGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA------KGQKVLCAYFTAESELKLSELRSSLSQ 1765
Cdd:cd05974   321 DGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPvrlsvpKAFIVLRAGYEPSPETALEIFRFSRER 400
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 1766 ELPGYMIPSyfVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05974   401 LAPYKRIRR--LEFAELPKTISGKIRRVEL 428
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1301-1701 2.77e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 77.29  E-value: 2.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1301 ALFEKQAERTPEVAAVV---YEND------RLTYRELNERANRLARMLRAQGVKPNQLVgILADRSADLLVGALAVWKAG 1371
Cdd:PRK05850    5 SLLRERASLQPDDAAFTfidYEQDpagvaeTLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1372 GAYVPLDPDYPS---DRIQFMLEDSAASVLLTQTHLQER-----AQQWGQTLQAVLCLDDEAAYAEDASNVANVNEPhDL 1443
Cdd:PRK05850   84 LIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAVVDDvteyvAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLP-ST 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1444 AYVIYTSGTTGRPKGVMIEHRSL-VN---TAAGYRREY----RLDQFPVRLLqlaSFSFD--VFVGDIArTLYNGgtmvi 1513
Cdd:PRK05850  163 AYLQYTSGSTRTPAGVMVSHRNViANfeqLMSDYFGDTggvpPPDTTVVSWL---PFYHDmgLVLGVCA-PILGG----- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1514 cpkddriDPARLHYWISeekitiFESTPAliiPFMDYVAEHGL--------------------DMSSMEL---LITSSDS 1570
Cdd:PRK05850  234 -------CPAVLTSPVA------FLQRPA---RWMQLLASNPHafsaapnfafelavrktsddDMAGLDLggvLGIISGS 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1571 CSVTDYRVlqERFGSQFRIIN--------AYGVTEAA--IDSSLYDEPlaklPEAGN-----VPIGKAALNAK------- 1628
Cdd:PRK05850  298 ERVHPATL--KRFADRFAPFNlretairpSYGLAEATvyVATREPGQP----PESVRfdyekLSAGHAKRCETgggtplv 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1629 ---------FYIVDAHLN-PVPVGVLGELCIGGIGVARGYLNRPELTEEKF----VD-SPFV-EGERLyRTGDLArWMPD 1692
Cdd:PRK05850  372 sygsprsptVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlVDpSPGTpEGPWL-RTGDLG-FISE 449

                  ....*....
gi 386647928 1693 GNVDFIGRI 1701
Cdd:PRK05850  450 GELFIVGRI 458
PRK05850 PRK05850
acyl-CoA synthetase; Validated
2346-2523 2.87e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 77.29  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2346 TIHQLFEEQAERIPDHPAVVF-------EG--QQLTYRELNERANRLARTLQALGVKTDQPVGLMlERSLEMVVGMFAVL 2416
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTFidyeqdpAGvaETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2417 KAGGAYVPIDPEYP---EDRISYMLEDSSAQVLLAQRRLQERV---------SFAGTVVTVDDEQAYAGDGSNLESAVGP 2484
Cdd:PRK05850   81 QAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSAVVDDVteyvapqpgQSAPPVIEVDLLDLDSPRGSDARPRDLP 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 386647928 2485 nDLAYIIYTSGTTGKPKGVMVEHHGLcslkqmFANTLQI 2523
Cdd:PRK05850  161 -STAYLQYTSGSTRTPAGVMVSHRNV------IANFEQL 192
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
4163-4337 3.13e-13

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 75.47  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4163 GRPLANHRIYVVDshnrmlpvgvaGELCISGVGLARGYLNRPEltaekfvDNPF-EPGerMYRTGDLVRwLPDGNLEYLG 4241
Cdd:PRK07824  195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFaEPG--WFRTDDLGA-LDDGVLTVLG 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4242 RIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDAN-GQQQLVAYFVAQREL-TAAELRATMSQELPNYMIPSYFV 4319
Cdd:PRK07824  254 RADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVAAVVGDGGPApTLEALRAHVARTLDRTAAPRELH 333
                         170
                  ....*....|....*...
gi 386647928 4320 QLAQMPLTPNGKIDRKAL 4337
Cdd:PRK07824  334 VVDELPRRGIGKVDRRAL 351
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
4909-5381 3.35e-13

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 77.70  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4909 ENDRLTYRELNERANRLARTLRAqGVKPNQLVGILADRSADLLVGALAVWKAGgaYVPLdpdypsdriqfMLEDSAAS-- 4986
Cdd:PRK06814  655 VNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAG--RVPA-----------MINFSAGIan 720
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4987 -----------VLLTQTHLQERAQQwgQTLQAALCLDDEAAYAEDASNVANV-------------------NEPHDLAYV 5036
Cdd:PRK06814  721 ilsackaaqvkTVLTSRAFIEKARL--GPLIEALEFGIRIIYLEDVRAQIGLadkikgllagrfplvyfcnRDPDDPAVI 798
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5037 IYTSGTTGRPKGVMIEHRSLVNTAAgyrreyrldqfpvrllQLASfSFDVFVGDIArtlYN-----------GGTMVicP 5105
Cdd:PRK06814  799 LFTSGSEGTPKGVVLSHRNLLANRA----------------QVAA-RIDFSPEDKV---FNalpvfhsfgltGGLVL--P 856
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5106 KDDRID----PARLHYWISEEKI-----TIFESTPALIIPFMDYVaeHGLDMSSMVLLITSSDSCSVTDYRVLQERFGsq 5176
Cdd:PRK06814  857 LLSGVKvflyPSPLHYRIIPELIydtnaTILFGTDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKFG-- 932
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5177 FRIINAYGVTEA----AIDSSLYDEPlaklpeaGNVpiGKAALNakfyiVDAHLNPVPvGVL--GELCIGGIGVARGYLn 5250
Cdd:PRK06814  933 IRILEGYGVTETapviALNTPMHNKA-------GTV--GRLLPG-----IEYRLEPVP-GIDegGRLFVRGPNVMLGYL- 996
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5251 rpeLTEEKFVDSPFVEGErlYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA-K 5329
Cdd:PRK06814  997 ---RAENPGVLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDArK 1071
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 5330 GQKVLCahFTAESELKLSE-LRSSLSQELPGYMIPSYFVQLEQLPLTANGKID 5381
Cdd:PRK06814 1072 GERIIL--LTTASDATRAAfLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1319-1795 3.41e-13

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 76.75  E-value: 3.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1319 ENDRLTYRELNERANRLARMLRAQ-GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASV 1397
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1398 LLTQTHLqerAQQWGQTLQAVLCL---------DDEAAYAEDASNVANVN-----------------EPHDLAYVIYTSG 1451
Cdd:PRK05620  115 IVADPRL---AEQLGEILKECPCVravvfigpsDADSAAAHMPEGIKVYSyealldgrstvydwpelDETTAAAICYSTG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1452 TTGRPKGVMIEHRSLVNTAAGYRREyrlDQFPVRLLQlaSF-----SFDVFVGDIARTLYNGGTMVICPKDDrIDPARLH 1526
Cdd:PRK05620  192 TTGAPKGVVYSHRSLYLQSLSLRTT---DSLAVTHGE--SFlccvpIYHVLSWGVPLAAFMSGTPLVFPGPD-LSAPTLA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1527 YWISEEKITIFESTPALIIPFM-DYVAEHGLDMSSMELLITSSDSCSVTdYRVLQERFGSQfrIINAYGVTEAAIDSSLY 1605
Cdd:PRK05620  266 KIIATAMPRVAHGVPTLWIQLMvHYLKNPPERMSLQEIYVGGSAVPPIL-IKAWEERYGVD--VVHVWGMTETSPVGTVA 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1606 DEPLAKLPEA--------GNVPigkAALNakFYIV-DAHLNPVPVGVLGELCIGGIGVARGYLNRPELTE----EKFVDS 1672
Cdd:PRK05620  343 RPPSGVSGEArwayrvsqGRFP---ASLE--YRIVnDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGggaaSTFRGE 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1673 PFVEGERLY------RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLC 1745
Cdd:PRK05620  418 DVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERPLA 497
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386647928 1746 AYFTAE----SELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK05620  498 VTVLAPgiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
7444-7947 3.57e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 76.60  E-value: 3.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7444 REQTIHGLFEEQAERmpEKAAVVFENTQLTYRE-LNERANR--LARTLRAegvqADQP--VGLMIERSLEMIVGAFAIMK 7518
Cdd:PRK13388    1 MRDTIAQLLRDRAGD--DTIAVRYGDRTWTWREvLAEAAARaaALIALAD----PDRPlhVGVLLGNTPEMLFWLAAAAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7519 AGGAYVPIDP----EYPEDRIRYmledSGAQVLLT---QRHLQECVSFDGKVIAADDEQAYGE---DGSNLEPV--VGPN 7586
Cdd:PRK13388   75 GGYVLVGLNTtrrgAALAADIRR----ADCQLLVTdaeHRPLLDGLDLPGVRVLDVDTPAYAElvaAAGALTPHreVDAM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7587 HLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDrvVQFASLS-FD----ASCWEIfkALFFGATLYIPAK- 7660
Cdd:PRK13388  151 DPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD--VCYVSMPlFHsnavMAGWAP--AVASGAAVALPAKf 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7661 ------DTILDYPlfESYMNENGITAAILPPTyaiylsPDRlP--SLKKLITG-GSAAS----VEFVQQWKdkVRYFNAY 7727
Cdd:PRK13388  227 sasgflDDVRRYG--ATYFNYVGKPLAYILAT------PER-PddADNPLRVAfGNEASprdiAEFSRRFG--CQVEDGY 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7728 GPTEASIVTSVWAASPDGldlrsvPIGRPIANhqIFIVDSQNhMLPVGVA---------------GELC-ISGAGLARGY 7791
Cdd:PRK13388  296 GSSEGAVIVVREPGTPPG------SIGRGAPG--VAIYNPET-LTECAVArfdahgallnadeaiGELVnTAGAGFFEGY 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7792 LNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDA 7871
Cdd:PRK13388  367 YNNPEATAERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7872 -NGQQQLCAYFVAD-RELTVSELRGTLS--QELPGYMIPSYFVQLEQMPLTPNGKIDRNALPApEGSMQTGADFVEPRTP 7947
Cdd:PRK13388  440 rVGDQVMAALVLRDgATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA-QGWATGDPVTLWVRRG 518
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
2355-2828 3.59e-13

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 76.26  E-value: 3.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDri 2434
Cdd:cd05929     2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRA-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 symledsSAQVLLAQRRLQERVSFAG----TVVTVDDEQAYAGDGSNLESAVGPNDlaYIIYTSGTTGKPKGVMVEHHGL 2510
Cdd:cd05929    80 -------EACAIIEIKAAALVCGLFTgggaLDGLEDYEAAEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGIKRGLPGG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2511 CS---LKQMFANTLQINAQDRVVQFASLSFDASCWEVFQTLFFGATLYIPTK---ETILdyQWFERYmsdnGITTATLPP 2584
Cdd:cd05929   151 PPdndTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKfdpEEFL--RLIERY----RVTFAQFVP 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2585 TYAVYLN--PDHMPD------FKRLIAAGSASSLELLQQWKD--KVKYFNAYGPTEDSICTTIwtPSTEDISQLKSVpig 2654
Cdd:cd05929   225 TMFVRLLklPEAVRNaydlssLKRVIHAAAPCPPWVKEQWIDwgGPIIWEYYGGTEGQGLTII--NGEEWLTHPGSV--- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2655 GPIVNHRIYIVDAHYQPVPVGVAGELCIAGvGLARGYLNRPDLTAEKFvdnpfepGERMYRT-GDLAKWLPDGTIEYLGR 2733
Cdd:cd05929   300 GRAVLGKVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAAR-------NEGGWSTlGDVGYLDEDGYLYLTDR 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2734 IDHQVKIRGYRIELGEIEEQLL---KVASV-----------QE--AIVIAHDDASGQKQLCAyfvadrtmtvgELRGELS 2797
Cdd:cd05929   372 RSDMIISGGVNIYPQEIENALIahpKVLDAavvgvpdeelgQRvhAVVQPAPGADAGTALAE-----------ELIAFLR 440
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 2798 GELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05929   441 DRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
2355-2771 3.76e-13

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 76.70  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPavvfeGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYP---- 2430
Cdd:cd05921    15 AEREGNGG-----WRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlmsq 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2431 -EDRISYMLEDSSAQVLLAQ-----RRLQERVSFAGTVVTV-----DDEQAYA----------GDGSNLESAVGPNDLAY 2489
Cdd:cd05921    90 dLAKLKHLFELLKPGLVFAQdaapfARALAAIFPLGTPLVVsrnavAGRGAISfaelaatpptAAVDAAFAAVGPDTVAK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2490 IIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASL----SFDAScwEVFQ-TLFFGATLYI----PT-- 2558
Cdd:cd05921   170 FLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLpwnhTFGGN--HNFNlVLYNGGTLYIddgkPMpg 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2559 --KETIldyqwfeRYMSDNGITT-ATLPPTYAVYLNpdHMPD--------FKRLI------AAGSASSLELLQQWKDK-- 2619
Cdd:cd05921   248 gfEETL-------RNLREISPTVyFNVPAGWEMLVA--ALEKdealrrrfFKRLKlmfyagAGLSQDVWDRLQALAVAtv 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2620 ---VKYFNAYGPTED--SICTTIWtpsTEDISQLKSVPIGGPIVnhriyivdahyQPVPVGVAGELCIAGVGLARGYLNR 2694
Cdd:cd05921   319 gerIPMMAGLGATETapTATFTHW---PTERSGLIGLPAPGTEL-----------KLVPSGGKYEVRVKGPNVTPGYWRQ 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2695 PDLTAEKFVDNPFepgermYRTGDLAKWL----PDGTIEYLGRIDHQVKIR-GYRIELGEIEEQLLKVAS--VQEAIVIA 2767
Cdd:cd05921   385 PELTAQAFDEEGF------YCLGDAAKLAdpddPAKGLVFDGRVAEDFKLAsGTWVSVGPLRARAVAACAplVHDAVVAG 458

                  ....
gi 386647928 2768 HDDA 2771
Cdd:cd05921   459 EDRA 462
PRK08308 PRK08308
acyl-CoA synthetase; Validated
5267-5391 3.77e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 75.84  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5267 GERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKL 5346
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP 368
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 5347 SELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDAS 5391
Cdd:PRK08308  369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVT 413
PRK08308 PRK08308
acyl-CoA synthetase; Validated
1677-1801 4.66e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 75.46  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1677 GERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESELKL 1756
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP 368
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 1757 SELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDAS 1801
Cdd:PRK08308  369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVT 413
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
5956-6420 4.66e-13

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 75.93  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5956 FEDKQLTYGELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAK 6034
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6035 LLLVQghlldrasfadklvnlnddgayhedgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNvvrlvkntNYVELNE 6114
Cdd:cd05937    81 FVIVD----------------------------------PDDPAILIYTSGTTGLPKAAAISWRR--------TLVTSNL 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6115 QTHIL--QTGAVVFDA-----STFEIWGA---LLNGGRLYVVRN---ETILDAVSLKNA--IQQYGINTMWLtapLYNQL 6179
Cdd:cd05937   119 LSHDLnlKNGDRTYTCmplyhGTAAFLGAcncLMSGGTLALSRKfsaSQFWKDVRDSGAtiIQYVGELCRYL---LSTPP 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6180 SQQDSGMfaglKTLIVGGDVLSvPHINRVLREHAGLSIVNG-YGPTENTTFSTTHT------------------IVGEQK 6240
Cdd:cd05937   196 SPYDRDH----KVRVAWGNGLR-PDIWERFRERFNVPEIGEfYAATEGVFALTNHNvgdfgagaighhglirrwKFENQV 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6241 EAVPI----GKPI-NNSTAYIVDsklslLPVGVWGELIV----GGDGVARGYLNRPELTAEKFVESSFLPGERCYRTGDL 6311
Cdd:cd05937   271 VLVKMdpetDDPIrDPKTGFCVR-----APVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6312 ARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATV--IVREDESGQKQLCAYFVAERELTIGELRAALS 6389
Cdd:cd05937   346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESSAVPTEFTKSLL 425
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 6390 QELPNYMIPSHFVPL-----ERMPLTPNGKIDRRAL 6420
Cdd:cd05937   426 ASLARKNLPSYAVPLflrltEEVATTDNHKQQKGVL 461
PRK05850 PRK05850
acyl-CoA synthetase; Validated
4891-5291 4.80e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 76.52  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4891 ALFEKQAECTPEAAAVV---YEND------RLTYRELNERANRLARTLRAQGVKPNQLVgILADRSADLLVGALAVWKAG 4961
Cdd:PRK05850    5 SLLRERASLQPDDAAFTfidYEQDpagvaeTLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4962 GAYVPLDPDYPS---DRIQFMLEDSAASVLLTQTHLQERAQQWGQTLQA----------ALCLDdeaayAEDASNVANVN 5028
Cdd:PRK05850   84 LIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGqsappvievdLLDLD-----SPRGSDARPRD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5029 EPhDLAYVIYTSGTTGRPKGVMIEHRSL-VN---TAAGYRREY----RLDQFPVRLLqlaSFSFD--VFVGDIArTLYNG 5098
Cdd:PRK05850  159 LP-STAYLQYTSGSTRTPAGVMVSHRNViANfeqLMSDYFGDTggvpPPDTTVVSWL---PFYHDmgLVLGVCA-PILGG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5099 gtmvicpkddriDPARLHYWISeekitiFESTPAliiPFMDYVAEH-------------------------GLDMSSMVL 5153
Cdd:PRK05850  234 ------------CPAVLTSPVA------FLQRPA---RWMQLLASNphafsaapnfafelavrktsdddmaGLDLGGVLG 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5154 LITSSDscsvtdyRVLQ---ERFGSQFRIIN--------AYGVTEAA--IDSSLYDEPlaklPEAGN-----VPIGKAAL 5215
Cdd:PRK05850  293 IISGSE-------RVHPatlKRFADRFAPFNlretairpSYGLAEATvyVATREPGQP----PESVRfdyekLSAGHAKR 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5216 NAK----------------FYIVDAHLN-PVPVGVLGELCIGGIGVARGYLNRPELTEEKF----VD-SPFV-EGERLyR 5272
Cdd:PRK05850  362 CETgggtplvsygsprsptVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlVDpSPGTpEGPWL-R 440
                         490
                  ....*....|....*....
gi 386647928 5273 TGDLArWMPDGNVDFIGRI 5291
Cdd:PRK05850  441 TGDLG-FISEGELFIVGRI 458
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
5961-6413 5.80e-13

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 76.34  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLR-NAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQ 6039
Cdd:cd17632    68 ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6040 GHLLD----------------------------------RASFADK--LVNLNDDGAYHEDGSNLEPVNGPE----HLTY 6079
Cdd:cd17632   148 AEHLDlaveavleggtpprlvvfdhrpevdahraalesaRERLAAVgiPVTTLTLIAVRGRDLPPAPLFRPEpdddPLAL 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6080 VIYTSGTTGRPKGVMVEHRNVVRL-VKNTNYVELNEQTHI-LQTGAVVFDASTFEIWGALLNGGRLYVVRN---ETILDA 6154
Cdd:cd17632   228 LIYTSGSTGTPKGAMYTERLVATFwLKVSSIQDIRPPASItLNFMPMSHIAGRISLYGTLARGGTAYFAAAsdmSTLFDD 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6155 VSLKNA-------------IQQYGINTMWLTAPLYNQLSQQDSgMFAGLKTLIVGGDVLSV--------PHINRVLREHA 6213
Cdd:cd17632   308 LALVRPtelflvprvcdmlFQRYQAELDRRSVAGADAETLAER-VKAELRERVLGGRLLAAvcgsaplsAEMKAFMESLL 386
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6214 GLSIVNGYGPTENTTFSTTHTIVGEQkeavpigkpinnstayIVDSKLSLLP-VGVW--------GELIVGGDGVARGYL 6284
Cdd:cd17632   387 DLDLHDGYGSTEAGAVILDGVIVRPP----------------VLDYKLVDVPeLGYFrtdrphprGELLVKTDTLFPGYY 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6285 NRPELTAEKFVESSFlpgercYRTGD-LARWLPDgTLEYKGRIDEQVKI-RGYRIELGEIEeqllkvaSVKEATVIVRE- 6361
Cdd:cd17632   451 KRPEVTAEVFDEDGF------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLE-------AVFAASPLVRQi 516
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 6362 ---DESGQKQLCAYFV----AERELTIGELRAALSQ---------ELPNYMIPSHFVpLERMPLTP-NG 6413
Cdd:cd17632   517 fvyGNSERAYLLAVVVptqdALAGEDTARLRAALAEslqriareaGLQSYEIPRDFL-IETEPFTIaNG 584
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
4904-5385 7.16e-13

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 75.95  E-value: 7.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4904 AAVVYEND------RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAG-------GAYvplDPD 4970
Cdd:PRK00174   84 VAIIWEGDdpgdsrKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGF---SAE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4971 YPSDRIQfmleDSAASVLLTqthlqerA-QQW--GQT--LQAALcldDEAAyaEDASNVANV------------NEPHDL 5033
Cdd:PRK00174  161 ALADRII----DAGAKLVIT-------AdEGVrgGKPipLKANV---DEAL--ANCPSVEKVivvrrtggdvdwVEGRDL 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5034 AY-----------------------VIYTSGTTGRPKGVMieHrslvnTAAGYrreyrldqfpvrLLQlASFSF------ 5084
Cdd:PRK00174  225 WWhelvagasdecepepmdaedplfILYTSGSTGKPKGVL--H-----TTGGY------------LVY-AAMTMkyvfdy 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5085 ---DVF-----VGDIarT---------LYNGGTMVI---CPkdDRIDPARlhYW--ISEEKITIFESTPALIIPFM---- 5138
Cdd:PRK00174  285 kdgDVYwctadVGWV--TghsyivygpLANGATTLMfegVP--NYPDPGR--FWevIDKHKVTIFYTAPTAIRALMkegd 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5139 DYVAEHglDMSSMVLLitssdsCSVTD----------YRVLQerfGSQFRIINAYGVTE-AAIdsslydePLAKLPeaGN 5207
Cdd:PRK00174  359 EHPKKY--DLSSLRLL------GSVGEpinpeawewyYKVVG---GERCPIVDTWWQTEtGGI-------MITPLP--GA 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5208 VPI--GKAAL-----NAKfyIVDAHLNPVPVGVLGELCIGGI--GVARGYLNRPElteeKFVDSPFVEGERLYRTGDLAR 5278
Cdd:PRK00174  419 TPLkpGSATRplpgiQPA--VVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGAR 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5279 WMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLK----AE----GvreavvvVREDAKGQK-----VLCAHFTAESELK 5345
Cdd:PRK00174  493 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAhpkvAEaavvG-------RPDDIKGQGiyafvTLKGGEEPSDELR 565
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 5346 lSELRSSLSQEL-----PGYMipsYFVqlEQLPLTANGKIDRKAL 5385
Cdd:PRK00174  566 -KELRNWVRKEIgpiakPDVI---QFA--PGLPKTRSGKIMRRIL 604
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
4877-5314 7.59e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 75.85  E-value: 7.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4877 NPAAPDAPENEAFHALFEKQAEcTPEAAAVVYEN------DRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADL 4950
Cdd:PRK12582   40 SRHPLGPYPRSIPHLLAKWAAE-APDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4951 LVGALAVWKAGGAYVPLDPDY---PSD--RIQFMLEDSAASVLLTQTHLQ-ERA----QQWGQTL---------QAALCL 5011
Cdd:PRK12582  119 ALMTLAAMQAGVPAAPVSPAYslmSHDhaKLKHLFDLVKPRVVFAQSGAPfARAlaalDLLDVTVvhvtgpgegIASIAF 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5012 DDEAAY---AEDASNVANVNePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAA---GYRREYRLDQFPVrLLQLASFSfD 5085
Cdd:PRK12582  199 ADLAATpptAAVAAAIAAIT-PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAmqeQLRPREPDPPPPV-SLDWMPWN-H 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5086 VFVGDIA--RTLYNGGTMVIcpKDDRIDPARLHYWIS---EEKITIFESTP---ALIIPFMDYVAEHGLDM-SSMVLLIT 5156
Cdd:PRK12582  276 TMGGNANfnGLLWGGGTLYI--DDGKPLPGMFEETIRnlrEISPTVYGNVPagyAMLAEAMEKDDALRRSFfKNLRLMAY 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5157 SSDSCSVTDYRVLQE----RFGSQFRIINAYGVTEAA-IDSSLYDEP----LAKLPEAGnvpigkaalnakfyivdAHLN 5227
Cdd:PRK12582  354 GGATLSDDLYERMQAlavrTTGHRIPFYTGYGATETApTTTGTHWDTervgLIGLPLPG-----------------VELK 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5228 PVPVGVLGELCIGGIGVARGYLNRPELTEEKFvdspfvEGERLYRTGDLARWM----PDGNVDFIGRIDNQAKI-RGYRI 5302
Cdd:PRK12582  417 LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF------DEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLsTGTWV 490
                         490
                  ....*....|..
gi 386647928 5303 ETGEIETQLLKA 5314
Cdd:PRK12582  491 SVGTLRPDAVAA 502
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
5944-6415 7.66e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 75.43  E-value: 7.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5944 QAERIPDHLAVTFED--KQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPE 6021
Cdd:PRK13390    6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6022 DRIRYMLEDSGAKLLL-----------VQGHLLDRASFADKLVNLND-DGAYHEDGSNL--EPVNGpehltYVIYTSGTT 6087
Cdd:PRK13390   86 PEADYIVGDSGARVLVasaaldglaakVGADLPLRLSFGGEIDGFGSfEAALAGAGPRLteQPCGA-----VMLYSSGTT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6088 GRPKGVM--VEHRNVVR----LVKNTNYVELNEQTHILQTGAVVFDASTFEiWGALLN--GGRLYVVRNetiLDAVSLKN 6159
Cdd:PRK13390  161 GFPKGIQpdLPGRDVDApgdpIVAIARAFYDISESDIYYSSAPIYHAAPLR-WCSMVHalGGTVVLAKR---FDAQATLG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6160 AIQQYGINTMWLTAPLYNQLSQQDSGM-----FAGLKTLIVGGDVLSVpHINRVLREHAGLSIVNGYGPTE--NTTFSTT 6232
Cdd:PRK13390  237 HVERYRITVTQMVPTMFVRLLKLDADVrtrydVSSLRAVIHAAAPCPV-DVKHAMIDWLGPIVYEYYSSTEahGMTFIDS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6233 HTIVGEQKEavpIGKPInNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEkfvesSFLPGERCYRT-GDL 6311
Cdd:PRK13390  316 PDWLAHPGS---VGRSV-LGDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA-----AQHPAHPFWTTvGDL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6312 ARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQK-----QLCAYFVAERELTiGELR 6385
Cdd:PRK13390  387 GSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgVPDPEMGEQvkaviQLVEGIRGSDELA-RELI 465
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 6386 AALSQELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:PRK13390  466 DYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
PLN02614 PLN02614
long-chain acyl-CoA synthetase
7473-7833 8.46e-13

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 75.83  E-value: 8.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7473 TYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQ-- 7550
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEek 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7551 -------------RHLQECVSFDGK-------------VIAADDEQAYGEDGSNLE-PVVGPNHLAYVIYTSGTTGKPKG 7603
Cdd:PLN02614  161 kiselfktcpnstEYMKTVVSFGGVsreqkeeaetfglVIYAWDEFLKLGEGKQYDlPIKKKSDICTIMYTSGTTGDPKG 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7604 VMVEHHGLCSL-----KLMFAETLRITEEDRVVQFASLS--FDASCWEIFKAL-----FFGATLYIPAKD---------- 7661
Cdd:PLN02614  241 VMISNESIVTLiagviRLLKSANAALTVKDVYLSYLPLAhiFDRVIEECFIQHgaaigFWRGDVKLLIEDlgelkptifc 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7662 ---TILD--YPLFESYMNENG-ITAAILPPTYA------------IYLSP--DRLPSLK---------KLITGGSAASVE 7712
Cdd:PLN02614  321 avpRVLDrvYSGLQKKLSDGGfLKKFVFDSAFSykfgnmkkgqshVEASPlcDKLVFNKvkqglggnvRIILSGAAPLAS 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7713 FVQQWKDKV---RYFNAYGPTEASIVTsvWAASPDGLDLRSVpIGRPIANHQIFI--VDSQNH-MLPVGVAGELCISGAG 7786
Cdd:PLN02614  401 HVESFLRVVaccHVLQGYGLTESCAGT--FVSLPDELDMLGT-VGPPVPNVDIRLesVPEMEYdALASTPRGEICIRGKT 477
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 7787 LARGYLNRPELTAEKFVDNpflagerMYRTGDLARWLPDGNIEYLGR 7833
Cdd:PLN02614  478 LFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDR 517
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4913-5385 8.57e-13

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 74.91  E-value: 8.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPldpdypsdriqfmledsaASVLLTQT 4992
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 HLQERAQQWGqtlqAALCLDDEAAYAEDASnvanvnephdLAYviYTSGTTGRPKGVMIEHRSlvntaagyrreyrldqF 5072
Cdd:cd05974    63 DLRDRVDRGG----AVYAAVDENTHADDPM----------LLY--FTSGTTSKPKLVEHTHRS----------------Y 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5073 PVRLLQlASFSFDVFVGDIARTL----------------YNGGTMVICPKDDRIDPARLHYWISEEKITIFESTPALIIP 5136
Cdd:cd05974   111 PVGHLS-TMYWIGLKPGDVHWNIsspgwakhawscffapWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRM 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5137 FMDYvaehglDMSSMVL----LITSSDSCSVTDYRVLQERFGSQFRiiNAYGVTEAAIdsslydeplaklpEAGNVP--- 5209
Cdd:cd05974   190 LIQQ------DLASFDVklreVVGAGEPLNPEVIEQVRRAWGLTIR--DGYGQTETTA-------------LVGNSPgqp 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5210 -----IGKAALNAKFYIVDAHLNPVPVGVLGeLCIGG---IGVARGYLNRPELTEEkfvdspfVEGERLYRTGDLARWMP 5281
Cdd:cd05974   249 vkagsMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDtrpVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDE 320
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5282 DGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDA------KGQKVLCAHFTAESELKLSELRSSLSQ 5355
Cdd:cd05974   321 DGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPvrlsvpKAFIVLRAGYEPSPETALEIFRFSRER 400
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 5356 ELPGYMIPSyfVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05974   401 LAPYKRIRR--LEFAELPKTISGKIRRVEL 428
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
2359-2823 8.68e-13

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 75.77  E-value: 8.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEG-----QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPE-- 2431
Cdd:cd05943    82 ADDPAAIYAAedgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVpg 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2432 --DRIS-------------------YMLEDSSAQVLLAQRRLQERV-------------SFAGTVVTVDDEQAYAGDGSN 2477
Cdd:cd05943   162 vlDRFGqiepkvlfavdaytyngkrHDVREKVAELVKGLPSLLAVVvvpytvaagqpdlSKIAKALTLEDFLATGAAGEL 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2478 LESAVGPNDLAYIIYTSGTTGKPKGvMVEHHGLCSLKQMFANTLQ--INAQDRVVQF------------ASLSFDASCwe 2543
Cdd:cd05943   242 EFEPLPFDHPLYILYSSGTTGLPKC-IVHGAGGTLLQHLKEHILHcdLRPGDRLFYYttcgwmmwnwlvSGLAVGATI-- 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2544 vfqTLFFGATLYiPTketiLDYQWfeRYMSDNGITT-ATLPPTYAVY----LNPDHMPDFKRLIAAGS------ASSLEL 2612
Cdd:cd05943   319 ---VLYDGSPFY-PD----TNALW--DLADEEGITVfGTSAKYLDALekagLKPAETHDLSSLRTILStgsplkPESFDY 388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2613 L-QQWKDKVKYFNAYGPTEdsICTTIwtpstedISQLKSVP-----IGGPIVNHRIYIVDAHYQPVpVGVAGEL-CIAGV 2685
Cdd:cd05943   389 VyDHIKPDVLLASISGGTD--IISCF-------VGGNPLLPvyrgeIQCRGLGMAVEAFDEEGKPV-WGEKGELvCTKPF 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2686 -GLARGYLNRPDltAEKFVDNPFE--PGerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQE 2762
Cdd:cd05943   459 pSMPVGFWNDPD--GSRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVED 534
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 2763 AIVIAHDDASGQKQLcAYFVADR---TMT---VGELRGELSGELPGYMIPAHFVQLERMPLTPNGKI 2823
Cdd:cd05943   535 SLVVGQEWKDGDERV-ILFVKLRegvELDdelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
PLN02574 PLN02574
4-coumarate--CoA ligase-like
4913-5385 1.05e-12

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 75.26  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTL-RAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ 4991
Cdd:PLN02574   67 ISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 THLQERAQQWGQTL---QAALCLDDEAA---------YAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNT 5059
Cdd:PLN02574  147 PENVEKLSPLGVPVigvPENYDFDSKRIefpkfyeliKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAM 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5060 AAGYRR-EYRLDQFP----VRLLQLASF---SFDVFVGDIartLYNGGTMVICPKDDRIDPARLhywISEEKITIFESTP 5131
Cdd:PLN02574  227 VELFVRfEASQYEYPgsdnVYLAALPMFhiyGLSLFVVGL---LSLGSTIVVMRRFDASDMVKV---IDRFKVTHFPVVP 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5132 aliiPFMDYVAEHGLDMSSMVL--LITSSDSCSVTDYRVLQE--RFGSQFRIINAYGVTEAAIDSS--LYDEPLAKLPEa 5205
Cdd:PLN02574  301 ----PILMALTKKAKGVCGEVLksLKQVSCGAAPLSGKFIQDfvQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSS- 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5206 gnvpIGKAALNAKFYIVDAHLNP-VPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVegerlyRTGDLARWMPDGN 5284
Cdd:PLN02574  376 ----VGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYFDEDGY 445
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5285 VDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESELKLSE--LRSSLSQELPGYMI 5362
Cdd:PLN02574  446 LYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQeaVINYVAKQVAPYKK 525
                         490       500
                  ....*....|....*....|...
gi 386647928 5363 PSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PLN02574  526 VRKVVFVQSIPKSPAGKILRREL 548
PRK09192 PRK09192
fatty acyl-AMP ligase;
7471-7852 1.11e-12

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 75.43  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7471 QLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPID-P------EYPEDRIRYMLEDSG 7543
Cdd:PRK09192   49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPmgfggrESYIAQLRGMLASAQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7544 AQVLLTQRHLQECV-----SFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHGLCS-LKLM 7617
Cdd:PRK09192  129 PAAIITPDELLPWVneathGNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMAnLRAI 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7618 FAETLRITEEDRVVQFASLSFDAscweifkAL--FFGATL-------YIPAKDTILDYPLFESYMNENGITAAILPP--- 7685
Cdd:PRK09192  209 SHDGLKVRPGDRCVSWLPFYHDM-------GLvgFLLTPVatqlsvdYLPTRDFARRPLQWLDLISRNRGTISYSPPfgy 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7686 -----------TYAIYLSPDRLPSLkklitGGSAASVEFVQQWKDKVR--YFNA------YGPTEASIVTSVwaaSP--- 7743
Cdd:PRK09192  282 elcarrvnskdLAELDLSCWRVAGI-----GADMIRPDVLHQFAEAFApaGFDDkafmpsYGLAEATLAVSF---SPlgs 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7744 --------------DGLDLRS----------VPIGRPIANHQIFIVDSQNHMLPVGVAGELCISGAGLARGYLNRPELTA 7799
Cdd:PRK09192  354 givveevdrdrleyQGKAVAPgaetrrvrtfVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQD 433
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 7800 EKFVDNpFLagermyRTGDLArWLPDGNIEYLGRIDHQVKIRGYRIELGEIEE 7852
Cdd:PRK09192  434 VLAADG-WL------DTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEW 478
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
771-827 1.12e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 66.43  E-value: 1.12e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928   771 IVNIWKEILKI--EKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVE 827
Cdd:pfam00550    3 LRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
7447-7842 1.27e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 75.15  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7447 TIHGLFEEQAERMPEKAAVVF---------ENTQLTYRELNERANRLARTLRaegvQADQP---VGLMIERSLEMIVGAF 7514
Cdd:PRK07769   22 NLVRHVERWAKVRGDKLAYRFldfsterdgVARDLTWSQFGARNRAVGARLQ----QVTKPgdrVAILAPQNLDYLIAFF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7515 AIMKAGGAYVPI-DPEYP--EDRIRYMLEDSGAQVLLTQRHLQECVS--FDG-------KVIAAD---DEQaygedGSNL 7579
Cdd:PRK07769   98 GALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVRkfFRArpakerpRVIAVDavpDEV-----GATW 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7580 EPVVgPNH--LAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGA--TL 7655
Cdd:PRK07769  173 VPPE-ANEdtIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHyiTF 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7656 YIPAKDT------ILDYPLFESYMNENgITAAilpPTYAIYLSPDR-----------LPSLKKLITGG---SAASVEfvq 7715
Cdd:PRK07769  252 MSPAAFVrrpgrwIRELARKPGGTGGT-FSAA---PNFAFEHAAARglpkdgeppldLSNVKGLLNGSepvSPASMR--- 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7716 qwkdkvRYFNAYGP--------------TEASIVTSV--WAASP-----DGLDLRS-----VPIGRPIANHQI------- 7762
Cdd:PRK07769  325 ------KFNEAFAPyglpptaikpsygmAEATLFVSTtpMDEEPtviyvDRDELNAgrfveVPADAPNAVAQVsagkvgv 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7763 ----FIVD-SQNHMLPVGVAGELCISGAGLARGYLNRPELTAEKF-------VDNPFLAG----ERMYRTGDLARWLpDG 7826
Cdd:PRK07769  399 sewaVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrLSESHAEGapddALWVRTGDYGVYF-DG 477
                         490
                  ....*....|....*.
gi 386647928 7827 NIEYLGRIDHQVKIRG 7842
Cdd:PRK07769  478 ELYITGRVKDLVIIDG 493
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
7456-7928 1.36e-12

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 74.72  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEypedri 7535
Cdd:cd05929     2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSR------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7536 ryMLEDSGAQVLLTQRHLQECVSFDGK----VIAADDEQAYGEDGSNLEPVVGPNhlaYVIYTSGTTGKPKGVMVEHHGL 7611
Cdd:cd05929    76 --APRAEACAIIEIKAAALVCGLFTGGgaldGLEDYEAAEGGSPETPIEDEAAGW---KMLYSGGTTGRPKGIKRGLPGG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7612 CS---LKLMFAETLRITEEDRVVQFASLSFDASCWEIFKALFFGATLYIPAK---DTILDypLFESYmnenGITAAILPP 7685
Cdd:cd05929   151 PPdndTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKfdpEEFLR--LIERY----RVTFAQFVP 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7686 TYAIYLSPdrLP----------SLKKLITGGSAASVEFVQQWKD--KVRYFNAYGPTEASIVTsvWAASPDGLDLRSvPI 7753
Cdd:cd05929   225 TMFVRLLK--LPeavrnaydlsSLKRVIHAAAPCPPWVKEQWIDwgGPIIWEYYGGTEGQGLT--IINGEEWLTHPG-SV 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7754 GRPIANhQIFIVDSQNHMLPVGVAGELCISGAGlARGYLNRPELTAEKFvdnpflaGERMYRT-GDLARWLPDGNIEYLG 7832
Cdd:cd05929   300 GRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAAR-------NEGGWSTlGDVGYLDEDGYLYLTD 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7833 RIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYF-----VADRELTVSELRGTLSQELPGYMIPS 7907
Cdd:cd05929   371 RRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapgADAGTALAEELIAFLRDRLSRYKCPR 450
                         490       500
                  ....*....|....*....|.
gi 386647928 7908 YFVQLEQMPLTPNGKIDRNAL 7928
Cdd:cd05929   451 SIEFVAELPRDDTGKLYRRLL 471
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1439-1791 1.45e-12

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 75.13  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1439 EPHDLAYVIYTSGTTGRPKGVMIEHRSL------VNTAAGYRREyrlDQFpvrLLQLASF-SFDVFVGDIARTLYngGTM 1511
Cdd:PRK08043  363 QPEDAALILFTSGSEGHPKGVVHSHKSLlanveqIKTIADFTPN---DRF---MSALPLFhSFGLTVGLFTPLLT--GAE 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1512 VIcpkddrIDPARLHYWISEEKI-----TIFESTPAliipFMDYVAE--HGLDMSSMELLITSSDSCSVTDYRVLQERFG 1584
Cdd:PRK08043  435 VF------LYPSPLHYRIVPELVydrncTVLFGTST----FLGNYARfaNPYDFARLRYVVAGAEKLQESTKQLWQDKFG 504
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1585 sqFRIINAYGVTEAAidsslydePLAKLpeagNVPIGkaalnAKFYIV-------DAHLNPVPvGVL--GELCIGGIGVA 1655
Cdd:PRK08043  505 --LRILEGYGVTECA--------PVVSI----NVPMA-----AKPGTVgrilpgmDARLLSVP-GIEqgGRLQLKGPNIM 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1656 RGYL--NRPELTEEKFVDSpfVEGER---LYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREA 1730
Cdd:PRK08043  565 NGYLrvEKPGVLEVPTAEN--ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQH 642
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1731 VVVVREDA-KGQK-VLcayFTAESELKLSEL----RSSLSQELPgymIPSYFVQLEQLPLTANGKID 1791
Cdd:PRK08043  643 ATAIKSDAsKGEAlVL---FTTDSELTREKLqqyaREHGVPELA---VPRDIRYLKQLPLLGSGKPD 703
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
4913-5291 1.47e-12

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 75.09  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL--T 4990
Cdd:cd05933     9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVveN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4991 QTHLQERAQQWGQ--TLQAALCLDDEAAYAEDA-------------------SNVANVNEPHDLAYVIYTSGTTGRPKGV 5049
Cdd:cd05933    89 QKQLQKILQIQDKlpHLKAIIQYKEPLKEKEPNlyswdefmelgrsipdeqlDAIISSQKPNQCCTLIYTSGTTGMPKGV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5050 MIEHRSLVNTAAGYRREYRLDQFPVR---------LLQLASFSFDVFVG-DIARTLYNG------GTMVICPKDDRidPA 5113
Cdd:cd05933   169 MLSHDNITWTAKAASQHMDLRPATVGqesvvsylpLSHIAAQILDIWLPiKVGGQVYFAqpdalkGTLVKTLREVR--PT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5114 RL----HYW--ISEE-KITIFESTP---ALIIPFMDYVAEHglDMSSMVLLITSSDSCSVTDYRVLQE-----------R 5172
Cdd:cd05933   247 AFmgvpRVWekIQEKmKAVGAKSGTlkrKIASWAKGVGLET--NLKLMGGESPSPLFYRLAKKLVFKKvrkalgldrcqK 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5173 FGS----------QF------RIINAYGVTEAAIDSSLydeplaKLPEAGNV-PIGKAALNAKFYIVdahlNPVPVGVlG 5235
Cdd:cd05933   325 FFTgaapisretlEFflslniPIMELYGMSETSGPHTI------SNPQAYRLlSCGKALPGCKTKIH----NPDADGI-G 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 5236 ELCIGGIGVARGYLNRPELTEEKfvdspfVEGERLYRTGDLARWMPDGNVDFIGRI 5291
Cdd:cd05933   394 EICFWGRHVFMGYLNMEDKTEEA------IDEDGWLHSGDLGKLDEDGFLYITGRI 443
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
281-747 1.64e-12

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 74.39  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  281 FEDRQLTYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGAyvpidPEYpeerIRYMLEDSGtq 359
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF----INYNLSGDP-- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  360 vllsqghLQERVSFSGTWIRLDDeeayhedgsnlesvngPEHLTYVIYTSGTTGKPKGN-LTTHRNIIRVVKNTNYIDVT 438
Cdd:cd05937    70 -------LIHCLKLSGSRFVIVD----------------PDDPAILIYTSGTTGLPKAAaISWRRTLVTSNLLSHDLNLK 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  439 GQDKLlqlssYS----FDGSTFDIFGA--LLNGAKLVLVPKETVLDVAKLAglIEKQQISVMFITTAFFNVL-VDMNPDC 511
Cdd:cd05937   127 NGDRT-----YTcmplYHGTAAFLGACncLMSGGTLALSRKFSASQFWKDV--RDSGATIIQYVGELCRYLLsTPPSPYD 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  512 LRHARAILFGG-----------ERVSVSHVRK--------------ALGHLGPGKIKHvYGPT-----ESTVFATSYDvH 561
Cdd:cd05937   200 RDHKVRVAWGNglrpdiwerfrERFNVPEIGEfyaategvfaltnhNVGDFGAGAIGH-HGLIrrwkfENQVVLVKMD-P 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  562 EVEEG--------AVSIPIGGPisNTAIYIVNAQNKlqpigvagelcvagdGLARGYLNRPDLTAEKFADNPFAPGERMY 633
Cdd:cd05937   278 ETDDPirdpktgfCVRAPVGEP--GEMLGRVPFKNR---------------EAFQGYLHNEDATESKLVRDVFRKGDIYF 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  634 RTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATV--VVRESANGEKQLCAYYVADRSLPA--- 708
Cdd:cd05937   341 RTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESSAVPtef 420
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 386647928  709 --NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:cd05937   421 tkSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
2372-2825 1.69e-12

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 74.45  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2372 TYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLE---DSSAQVLLA 2448
Cdd:cd05908    17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKLKLNKvwnTLKNPYLIT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2449 QRRLQERVsfagtvvtvddeqayagdgsnlesavgPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDR 2528
Cdd:cd05908    97 EEEVLCEL---------------------------ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2529 VVQFASLSFD---ASCWEVfqTLFFGATLYI-PTKETILDYQWFERYMSDNGITTATLPPTYAVY----LNPDHMPDFK- 2599
Cdd:cd05908   150 ILSWMPLTHDmglIAFHLA--PLIAGMNQYLmPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYflktLKPEKANDWDl 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2600 ---RLIAAGSAS-SLELLQQWKDKVKYFN--------AYGPTEDSICTTI-------WTPS----------------TED 2644
Cdd:cd05908   228 ssiRMILNGAEPiDYELCHEFLDHMSKYGlkrnailpVYGLAEASVGASLpkaqspfKTITlgrrhvthgepepevdKKD 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2645 ISQLKSVPIGGPIVNHRIYIVDAHYQPVPVGVAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAkWLP 2724
Cdd:cd05908   308 SECLTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLG-FIR 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2725 DGTIEYLGRIDHQVKIRGYRIELGEIE---EQLLKVASVQEAIVIAHDDASGQKQLCAYFV----ADRTMTVGELRGELS 2797
Cdd:cd05908   381 NGRLVITGREKDIIFVNGQNVYPHDIEriaEELEGVELGRVVACGVNNSNTRNEEIFCFIEhrksEDDFYPLGKKIKKHL 460
                         490       500
                  ....*....|....*....|....*...
gi 386647928 2798 GELPGYMIpAHFVQLERMPLTPNGKIDR 2825
Cdd:cd05908   461 NKRGGWQI-NEVLPIRRIPKTTSGKVKR 487
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
6435-6506 1.80e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 66.42  E-value: 1.80e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 6435 APRTEQEKALAAVWQAVLG--AERVGVTDHFF-ELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTLAQLSQHIQ 6506
Cdd:COG0236     1 MPREELEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLE 76
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
2372-2823 1.82e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 74.36  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2372 TYRELNERANRLARTLQALGVKTDQPVGLML---ERSLEM---VVGMFAVLKAggayvpIDPEYPEDRISYMLEDSSAQV 2445
Cdd:PRK07008   41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAyygVSGSGAVCHT------INPRLFPEQIAYIVNHAEDRY 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2446 LLAQrrlqerVSFA--------------GTVVTVDDEQAYAGDGSNL--ESAVGPNDLAY------------IIYTSGTT 2497
Cdd:PRK07008  115 VLFD------LTFLplvdalapqcpnvkGWVAMTDAAHLPAGSTPLLcyETLVGAQDGDYdwprfdenqassLCYTSGTT 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2498 GKPKGVMVEHHG--LCSLKQMFANTLQINAQDRVVQFASLsFDASCWEV-FQTLFFGATLYIPTKEtiLDYQWFERYMSD 2574
Cdd:PRK07008  189 GNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLpYSAPLTGAKLVLPGPD--LDGKSLYELIEA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2575 NGITTATLPPTyaVYLNP-DHMPD-------FKRLIAAGSASSLELLQQWKDK--VKYFNAYGPTEDS----ICTTIWTP 2640
Cdd:PRK07008  266 ERVTFSAGVPT--VWLGLlNHMREaglrfstLRRTVIGGSACPPAMIRTFEDEygVEVIHAWGMTEMSplgtLCKLKWKH 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2641 S--TEDISQLKSVPIGGPIVNHRIYIVDAHYQPVPV-GVA-GELCIAGVGLARGYLNRpdlTAEKFVDNPFEpgermyrT 2716
Cdd:PRK07008  344 SqlPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRG---DASPLVDGWFP-------T 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2717 GDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA--HDDASGQKQLCAYFVADRTMTVGELRG 2794
Cdd:PRK07008  414 GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIAcaHPKWDERPLLVVVKRPGAEVTREELLA 493
                         490       500
                  ....*....|....*....|....*....
gi 386647928 2795 ELSGELPGYMIPAHFVQLERMPLTPNGKI 2823
Cdd:PRK07008  494 FYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
3864-4334 1.99e-12

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 74.45  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRI 3943
Cdd:PLN02860   17 ATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 RYMLEDSGAQALLTQ---------------RHLRERV----------SFAGTFVAVDDEQAYHADGSNLEPVVGPNHLAY 3998
Cdd:PLN02860   97 KSAMLLVRPVMLVTDetcsswyeelqndrlPSLMWQVflespsssvfIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3999 VIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGAT-LYIPT--STTILDyp 4075
Cdd:PLN02860  177 ICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAChVLLPKfdAKAALQ-- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4076 lfesYMNENGITATI-LPPTYAAYLNPDRM-------PSLKKLITGGSAASVEFVQQWKD---KVLYFNAYGPTEA-SIV 4143
Cdd:PLN02860  255 ----AIKQHNVTSMItVPAMMADLISLTRKsmtwkvfPSVRKILNGGGSLSSRLLPDAKKlfpNAKLFSAYGMTEAcSSL 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4144 TSIwdeasdSLGDRKSVPIGRPLANHRIYVVDSHNrmLPVGV-AG------ELCI-----SGVG--LARGylnrPELTAE 4209
Cdd:PLN02860  331 TFM------TLHDPTLESPKQTLQTVNQTKSSSVH--QPQGVcVGkpaphvELKIgldesSRVGriLTRG----PHVMLG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4210 KFVDNPFEPGERM----YRTGDlVRWLPD-GNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQ 4284
Cdd:PLN02860  399 YWGQNSETASVLSndgwLDTGD-IGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTE 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 4285 QLVAyFVAQRE-----------------LTAAELRATMS-QELPNYMIPSYFVQL-AQMPLTPNGKIDR 4334
Cdd:PLN02860  478 MVVA-CVRLRDgwiwsdnekenakknltLSSETLRHHCReKNLSRFKIPKLFVQWrKPFPLTTTGKIRR 545
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
5960-6419 2.21e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 74.39  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5960 QLTYGELNERANRLARTLRNAgVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPI-DPDYP--EDRIRYMLEDSGAKLL 6036
Cdd:PRK12476   68 ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6037 LVQG-------HLLDRASFADKLVNLNDDGAYHEDGSNLEPVN-GPEHLTYVIYTSGTTGRPKGVMVEHRNVvrlvkNTN 6108
Cdd:PRK12476  147 LTTTaaaeaveGFLRNLPRLRRPRVIAIDAIPDSAGESFVPVElDTDDVSHLQYTSGSTRPPVGVEITHRAV-----GTN 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6109 YVE-------LNEQTHILQTGAVVFDASTFEIWGALLNGGRLyvvrneTILDAVSL----KNAIQQYGINT----MWLTA 6173
Cdd:PRK12476  222 LVQmilsidlLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHS------TLMSPTAFvrrpQRWIKALSEGSrtgrVVTAA 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6174 PLY-------NQLSQQDSGMFAGLKTLIVGGDVLSVPHINRVLREHA--GL---SIVNGYGPTENTTFSTT------HTI 6235
Cdd:PRK12476  296 PNFayewaaqRGLPAEGDDIDLSNVVLIIGSEPVSIDAVTTFNKAFApyGLprtAFKPSYGIAEATLFVATiapdaePSV 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6236 VGEQKE------AVPI-------------GKPINNSTAYIVDSKLSL-LPVGVWGELIVGGDGVARGYLNRPELTAEKFV 6295
Cdd:PRK12476  376 VYLDREqlgagrAVRVaadapnavahvscGQVARSQWAVIVDPDTGAeLPDGEVGEIWLHGDNIGRGYWGRPEETERTFG 455
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6296 ES--SFLP----------GERCYRTGDLARWLpDGTLEYKGRIDEQVKIRGYRIELGEIEeqllkvASVKEATVIVRE-- 6361
Cdd:PRK12476  456 AKlqSRLAegshadgaadDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIE------ATVAEASPMVRRgy 528
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 6362 ----DESGQKQLCAYFVAERELTIGE---------LRAALSQElpnYMIPSH---FVPLERMPLTPNGKIDRRA 6419
Cdd:PRK12476  529 vtafTVPAEDNERLVIVAERAAGTSRadpapaidaIRAAVSRR---HGLAVAdvrLVPAGAIPRTTSGKLARRA 599
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
7472-7840 2.29e-12

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 74.41  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEG-VQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVL-LT 7549
Cdd:cd17632    68 ITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLaVS 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7550 QRHL---QECVS----------FDGK-----------------------VIAADDEQAYGEDGSNLEPVVGPNH---LAY 7590
Cdd:cd17632   148 AEHLdlaVEAVLeggtpprlvvFDHRpevdahraalesarerlaavgipVTTLTLIAVRGRDLPPAPLFRPEPDddpLAL 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7591 VIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVV-QFASLSFDASCWEIFKALFFGATLYIPAK--------D 7661
Cdd:cd17632   228 LIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITlNFMPMSHIAGRISLYGTLARGGTAYFAAAsdmstlfdD 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7662 TILDYP------------LFESYMNE------NGITAAILPPTYAIYLSPDRLPslKKLITG--GSAA-SVE---FVQQW 7717
Cdd:cd17632   308 LALVRPtelflvprvcdmLFQRYQAEldrrsvAGADAETLAERVKAELRERVLG--GRLLAAvcGSAPlSAEmkaFMESL 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7718 KDkVRYFNAYGPTEASIVTSvwaaspDGLDLRSvpigrPIANHQI--------FIVDSQNhmlPvgvAGELCISGAGLAR 7789
Cdd:cd17632   386 LD-LDLHDGYGSTEAGAVIL------DGVIVRP-----PVLDYKLvdvpelgyFRTDRPH---P---RGELLVKTDTLFP 447
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386647928 7790 GYLNRPELTAEKFVDNPFlagermYRTGD-LARWLPDgNIEYLGRIDHQVKI 7840
Cdd:cd17632   448 GYYKRPEVTAEVFDEDGF------YRTGDvMAELGPD-RLVYVDRRNNVLKL 492
PRK05850 PRK05850
acyl-CoA synthetase; Validated
7447-7869 2.52e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 74.21  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7447 TIHGLFEEQAERMPEKAAVVFENTQ---------LTYRELNERANRLARTLRAEGVQADQPVGLMiERSLEMIVGAFAIM 7517
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTFIDYEqdpagvaetLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7518 KAGGAYVPIDPEYP---EDRIRYMLEDSGAQVLLTQR----HLQECVSFDG-----KVIAAD--DEQAygEDGSNLEPVV 7583
Cdd:PRK05850   81 QAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSavvdDVTEYVAPQPgqsapPVIEVDllDLDS--PRGSDARPRD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7584 GPNhLAYVIYTSGTTGKPKGVMVEHHGLCS--LKLM---FAETLRITEEDR-VVQFASLSFDAscweifkALFFGATLYI 7657
Cdd:PRK05850  159 LPS-TAYLQYTSGSTRTPAGVMVSHRNVIAnfEQLMsdyFGDTGGVPPPDTtVVSWLPFYHDM-------GLVLGVCAPI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7658 PAKD-TILDYPLfeSYM------------NENGITAAilpPTYAIYLSPDR----------LPSLKKLITGGSAASVEFV 7714
Cdd:PRK05850  231 LGGCpAVLTSPV--AFLqrparwmqllasNPHAFSAA---PNFAFELAVRKtsdddmagldLGGVLGIISGSERVHPATL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7715 QQWKDKVRYFN--------AYGPTEAS--IVTSVWAASPDG--LDLRSVPIGR----------PIANHQ------IFIVD 7766
Cdd:PRK05850  306 KRFADRFAPFNlretairpSYGLAEATvyVATREPGQPPESvrFDYEKLSAGHakrcetgggtPLVSYGsprsptVRIVD 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7767 SQNHM-LPVGVAGELCISGAGLARGYLNRPELTAEKF----VD-------NPFLagermyRTGDLArWLPDGNIEYLGRI 7834
Cdd:PRK05850  386 PDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlVDpspgtpeGPWL------RTGDLG-FISEGELFIVGRI 458
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 386647928 7835 DHQVKIRGYRIELGEIEeqllkiASVQEtivIARG 7869
Cdd:PRK05850  459 KDLLIVDGRNHYPDDIE------ATIQE---ITGG 484
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
4909-5385 2.57e-12

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 74.05  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4909 ENDRLTYRELNERANRLARTLRAQ-GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASV 4987
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4988 LLTQTHLqerAQQWGQTLQAALCL---------DDEAAYAEDASNVANVN-----------------EPHDLAYVIYTSG 5041
Cdd:PRK05620  115 IVADPRL---AEQLGEILKECPCVravvfigpsDADSAAAHMPEGIKVYSyealldgrstvydwpelDETTAAAICYSTG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5042 TTGRPKGVMIEHRSLVNTAAGYRREyrlDQFPVRLLQlaSF-----SFDVFVGDIARTLYNGGTMVICPKDDrIDPARLH 5116
Cdd:PRK05620  192 TTGAPKGVVYSHRSLYLQSLSLRTT---DSLAVTHGE--SFlccvpIYHVLSWGVPLAAFMSGTPLVFPGPD-LSAPTLA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5117 YWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAAIDSSLYD 5196
Cdd:PRK05620  266 KIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVD--VVHVWGMTETSPVGTVAR 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5197 EPLAKLPEA--------GNVPigkAALNakFYIV-DAHLNPVPVGVLGELCIGGIGVARGYLNRPELTE----EKFVDSP 5263
Cdd:PRK05620  344 PPSGVSGEArwayrvsqGRFP---ASLE--YRIVnDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGggaaSTFRGED 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5264 FVEGERLY------RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVL-- 5334
Cdd:PRK05620  419 VEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERPLav 498
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5335 --------CAHFTAEselklsELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK05620  499 tvlapgiePTRETAE------RLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
5957-6417 2.61e-12

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 73.68  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5957 EDKQ---LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRymledsga 6033
Cdd:cd05908     9 GDKKekfVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKL-------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6034 KLLLVQGHLldrasfaDKLVNLNDDGAYHEDgsnlepvngPEHLTYVIYTSGTTGRPKGVMVEHRNVVrlvknTNYVELN 6113
Cdd:cd05908    81 KLNKVWNTL-------KNPYLITEEEVLCEL---------ADELAFIQFSSGSTGDPKGVMLTHENLV-----HNMFAIL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6114 EQTHILQTgavvfdaSTFEIWGAL-----LNGGRLyvvrnetildaVSLKNAIQQYGINT--------MWLTAPLYNQLS 6180
Cdd:cd05908   140 NSTEWKTK-------DRILSWMPLthdmgLIAFHL-----------APLIAGMNQYLMPTrlfirrpiLWLKKASEHKAT 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6181 QQDSGMFAG---LKTL----------------IVGGDVLSVPHINRVLREHA--GL---SIVNGYGPTENT--------- 6227
Cdd:cd05908   202 IVSSPNFGYkyfLKTLkpekandwdlssirmiLNGAEPIDYELCHEFLDHMSkyGLkrnAILPVYGLAEASvgaslpkaq 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6228 ------TFSTTHTIVGEQKEA-----------VPIGKPINNSTAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELT 6290
Cdd:cd05908   282 spfktiTLGRRHVTHGEPEPEvdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEAT 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6291 AEKFVESSFLpgercyRTGDLArWLPDGTLEYKGRIDEQVKIRGYRIELGEIE---EQLLKVASVKEATVIVREDESGQK 6367
Cdd:cd05908   362 AKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIEriaEELEGVELGRVVACGVNNSNTRNE 434
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 6368 QLCAyFVAERElTIGELrAALSQELPNYMIP------SHFVPLERMPLTPNGKIDR 6417
Cdd:cd05908   435 EIFC-FIEHRK-SEDDF-YPLGKKIKKHLNKrggwqiNEVLPIRRIPKTTSGKVKR 487
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
2368-2828 2.71e-12

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 73.61  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2368 GQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLL 2447
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2448 AQRrlqervsfagtvvtVDDEQAYAGDGSNLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQD 2527
Cdd:cd05939    81 FNL--------------LDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPED 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2528 RVVQFASLSFDAS-CWEVFQTLFFGATLYIPTKETILDYqWFE--RYmsdnGITTATLPPTYAVY-LNPDHMPDFKR--- 2600
Cdd:cd05939   147 VVYDCLPLYHSAGgIMGVGQALLHGSTVVIRKKFSASNF-WDDcvKY----NCTIVQYIGEICRYlLAQPPSEEEQKhnv 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2601 LIAAGSAssleLLQQ-WKDKVKYFNA------YGPTEdsiCTTIWTPSTEDISQLKSVPIGGPIVnHRIYIV-------- 2665
Cdd:cd05939   222 RLAVGNG----LRPQiWEQFVRRFGIpqigefYGATE---GNSSLVNIDNHVGACGFNSRILPSV-YPIRLIkvdedtge 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2666 -----DAHYQPVPVGVAGELC---IAGVGLAR--GYLNRPDlTAEKFVDNPFEPGERMYRTGDLAKWLPDGTIEYLGRID 2735
Cdd:cd05939   294 lirdsDGLCIPCQPGEPGLLVgkiIQNDPLRRfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTG 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2736 HQVKIRGYRIELGEIEEQLLKVASVQEAIV----IAHddASGQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQ 2811
Cdd:cd05939   373 DTFRWKGENVSTTEVEGILSNVLGLEDVVVygveVPG--VEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRL 450
                         490
                  ....*....|....*..
gi 386647928 2812 LERMPLTPNGKIDRKAL 2828
Cdd:cd05939   451 LPEVDKTGTFKLQKTDL 467
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
398-749 2.73e-12

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 73.70  E-value: 2.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  398 GPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKNT-NYIDVTGQDKLLQ----LSSYSFDGSTfdIFgALLNGAKLV--- 469
Cdd:PRK06334  181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRAClKFFSPKEDDVMMSflppFHAYGFNSCT--LF-PLLSGVPVVfay 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  470 --LVPKetvldvaKLAGLIEKQQISVMFITTAFFNVLVDM---NPDCLRHARAILFGGERVSVSHVRKALGHLGPGKIKH 544
Cdd:PRK06334  258 npLYPK-------KIVEMIDEAKVTFLGSTPVFFDYILKTakkQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQ 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  545 VYGPTE-STVFATSYDVHEVEEGAVSIPIGGpisnTAIYIVNAQNKLQ-PIGVAGELCVAGDGLARGYL-NRPDLTAEKF 621
Cdd:PRK06334  331 GYGTTEcSPVITINTVNSPKHESCVGMPIRG----MDVLIVSEETKVPvSSGETGLVLTRGTSLFSGYLgEDFGQGFVEL 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  622 AdnpfapGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLK---LEAIEKATVVVRESANGEK-QLC 697
Cdd:PRK06334  407 G------GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgQNAADHAGPLVVCGLPGEKvRLC 480
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928  698 AYYVADRSLpaNEVRSTL-SQELPAYMLPSYFVQLEQMPLTTNGKVDRRALPA 749
Cdd:PRK06334  481 LFTTFPTSI--SEVNDILkNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
7950-8009 2.74e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 65.28  E-value: 2.74e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  7950 AELARIWQEVLGIGP--ISVKDNFFELGGHSLRATVLSSKVNKELNVNLPLRDIFRFPTVEA 8009
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2843-2914 2.74e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 65.65  E-value: 2.74e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 2843 APRSEEEKVLADVWQAVLG--AERVGATDHFF-ELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTVAQLSKHIR 2914
Cdd:COG0236     1 MPREELEERLAEIIAEVLGvdPEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLE 76
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
405-747 2.90e-12

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 72.39  E-value: 2.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  405 VIYTSGTTGKPKGNLTTHRNIIRVVKNTN-YIDVTGQdKLLQLSSYSFDGSTFdIFGALLNGAKLVLVPKETVLDVAKLA 483
Cdd:PRK07824   40 VVATSGTTGTPKGAMLTAAALTASADATHdRLGGPGQ-WLLALPAHHIAGLQV-LVRSVIAGSEPVELDVSAGFDPTALP 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  484 GLIEKQQISVMFITtaffnvLVDMNPD----------CLRHARAILFGGERVSVSHVRKA--LGhlgpgkIKHV--YGPT 549
Cdd:PRK07824  118 RAVAELGGGRRYTS------LVPMQLAkalddpaataALAELDAVLVGGGPAPAPVLDAAaaAG------INVVrtYGMS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  550 EsTVFATSYDvheveegavsipiGGPISNTAIYIVNaqnklqpigvaGELCVAGDGLARGYLNRPDltaekfaDNPFA-P 628
Cdd:PRK07824  186 E-TSGGCVYD-------------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFAeP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  629 GerMYRTGDLARwLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV-VRESANGEKQLCAYYVADRSLP 707
Cdd:PRK07824  234 G--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFgLPDDRLGQRVVAAVVGDGGPAP 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 386647928  708 A-NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PRK07824  311 TlEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
5029-5381 2.93e-12

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 74.36  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5029 EPHDLAYVIYTSGTTGRPKGVMIEHRSL------VNTAAGYRREyrlDQFpvrLLQLASF-SFDVFVGDIARTLYngGTM 5101
Cdd:PRK08043  363 QPEDAALILFTSGSEGHPKGVVHSHKSLlanveqIKTIADFTPN---DRF---MSALPLFhSFGLTVGLFTPLLT--GAE 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5102 VIcpkddrIDPARLHYWISEEKI-----TIFESTPAliipFMDYVAE--HGLDMSSMVLLITSSDSCSVTDYRVLQERFG 5174
Cdd:PRK08043  435 VF------LYPSPLHYRIVPELVydrncTVLFGTST----FLGNYARfaNPYDFARLRYVVAGAEKLQESTKQLWQDKFG 504
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5175 sqFRIINAYGVTEAAidsslydePLAKLpeagNVPIGkaalnAKFYIV-------DAHLNPVPvGVL--GELCIGGIGVA 5245
Cdd:PRK08043  505 --LRILEGYGVTECA--------PVVSI----NVPMA-----AKPGTVgrilpgmDARLLSVP-GIEqgGRLQLKGPNIM 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5246 RGYL--NRPELTEEKFVDSpfVEGER---LYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREA 5320
Cdd:PRK08043  565 NGYLrvEKPGVLEVPTAEN--ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQH 642
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 5321 VVVVREDA-KGQK-VLcahFTAESELKLSEL----RSSLSQELPgymIPSYFVQLEQLPLTANGKID 5381
Cdd:PRK08043  643 ATAIKSDAsKGEAlVL---FTTDSELTREKLqqyaREHGVPELA---VPRDIRYLKQLPLLGSGKPD 703
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
5030-5385 3.01e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 72.51  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIC-PKDD 5108
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgPAGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5109 RIDPARLHYW--ISEEKITIFESTPALIIPFMDyvAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVT 5186
Cdd:cd05944    81 RNPGLFDNFWklVERYRITSLSTVPTVYAALLQ--VPVNADISSLRFAMSGAAPLPVELRARFEDATGLP--VVEGYGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5187 EAAIDSSLYDEPLAKLPeaGNVPIGKAALNAKFYIVDA---HLNPVPVGVLGELCIGGIGVARGYLNRpELTEEKFVDsp 5263
Cdd:cd05944   157 EATCLVAVNPPDGPKRP--GSVGLRLPYARVRIKVLDGvgrLLRDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVA-- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5264 fvegERLYRTGDLARWMPDGNVDFIGRidnqAK---IR-GYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFT 5339
Cdd:cd05944   232 ----DGWLNTGDLGRLDADGYLFITGR----AKdliIRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQ 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 5340 AESELKLS--ELRSSLSQELPGY-MIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05944   304 LKPGAVVEeeELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
3879-4337 3.43e-12

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 73.23  E-value: 3.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3879 QLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTq 3958
Cdd:cd05939     3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3959 RHLRERVSFAGTFVAVDDEQAYHadgsnlepvvgpNHLAYvIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRV 4038
Cdd:cd05939    82 NLLDPLLTQSSTEPPSQDDVNFR------------DKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4039 vqFASLSFDASCWEIF---KALFFGATLYI----PTSTTILDYPLFE----SYMNEngITATILPPTYAAYLNPDRMpsl 4107
Cdd:cd05939   149 --YDCLPLYHSAGGIMgvgQALLHGSTVVIrkkfSASNFWDDCVKYNctivQYIGE--ICRYLLAQPPSEEEQKHNV--- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4108 kKLITG-GSAASVefvqqWKDKVLYFNA------YGPTE--ASIVTSiwdeasdslgDRKSVPIG-RPLANHRIYVVdsh 4177
Cdd:cd05939   222 -RLAVGnGLRPQI-----WEQFVRRFGIpqigefYGATEgnSSLVNI----------DNHVGACGfNSRILPSVYPI--- 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4178 nRMLPVG-VAGEL-------CI------SGVGLAR-----------GYLNRPElTAEKFVDNPFEPGERMYRTGDLVRWL 4232
Cdd:cd05939   283 -RLIKVDeDTGELirdsdglCIpcqpgePGLLVGKiiqndplrrfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMD 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4233 PDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLARE--DANGQQQLVAYFVAQRELTAAELRATMSQELP 4310
Cdd:cd05939   361 ELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvpGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLP 440
                         490       500
                  ....*....|....*....|....*..
gi 386647928 4311 NYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:cd05939   441 PYARPQFIRLLPEVDKTGTFKLQKTDL 467
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
401-744 3.91e-12

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 73.62  E-value: 3.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  401 HLTYVIYTSGTTGKPKGNLTTH-RNIIRVVKNTNYIDVTGQDKLLqLSSYSFDGSTFDIF--GALLNGAKLVLV------ 471
Cdd:PTZ00237  255 HPLYILYTSGTTGNSKAVVRSNgPHLVGLKYYWRSIIEKDIPTVV-FSHSSIGWVSFHGFlyGSLSLGNTFVMFeggiik 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  472 PKETVLDvakLAGLIEKQQISVMFITTAFFNVLVDMNPDC--------LRHARAILFGGERVSVS---HVRKALghlgpg 540
Cdd:PTZ00237  334 NKHIEDD---LWNTIEKHKVTHTLTLPKTIRYLIKTDPEAtiirskydLSNLKEIWCGGEVIEESipeYIENKL------ 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  541 KIK--HVYGPTESTVfATSYDVHeveegAVSIPI---GGPISNTAIYIVNAQNKLQPIGVAGELCVA---GDGLARGYLN 612
Cdd:PTZ00237  405 KIKssRGYGQTEIGI-TYLYCYG-----HINIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYK 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  613 RPDLTAEKFadNPFaPGerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLK----LE----AIEKAT- 683
Cdd:PTZ00237  479 NDEKFKQLF--SKF-PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKhplvLEccsiGIYDPDc 553
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  684 ------VVVRESANGEKQLcayyvaDRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDR 744
Cdd:PTZ00237  554 ynvpigLLVLKQDQSNQSI------DLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
PLN02479 PLN02479
acetate-CoA ligase
3858-4339 4.00e-12

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 73.34  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3858 GLFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPE 3937
Cdd:PLN02479   24 WFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3938 YPEDRIRYMLEDSGAQALLTQRHLrervsfagtFVAVDDEQAYHAD--GSNLEP----VVG-----PNHLAYVI------ 4000
Cdd:PLN02479  104 LNAPTIAFLLEHSKSEVVMVDQEF---------FTLAEEALKILAEkkKSSFKPplliVIGdptcdPKSLQYALgkgaie 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4001 ---------------------------YTSGTTGKPKGVMVEHHGLCSLKLmfANTLQMTEQDRVVQFASLSF---DASC 4050
Cdd:PLN02479  175 yekfletgdpefawkppadewqsialgYTSGTTASPKGVVLHHRGAYLMAL--SNALIWGMNEGAVYLWTLPMfhcNGWC 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4051 WEIFKALFFGATLYIPTSTTILDYplfeSYMNENGIT------------------ATILPptyaaylnpdrMPSLKKLIT 4112
Cdd:PLN02479  253 FTWTLAALCGTNICLRQVTAKAIY----SAIANYGVThfcaapvvlntivnapksETILP-----------LPRVVHVMT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4113 GGSA--ASVEFVQQWKD-KVLYF----NAYGPTEASIVTSIWDEASDS----LGDRKSVpigRPLANHRIYVVDSHNrML 4181
Cdd:PLN02479  318 AGAAppPSVLFAMSEKGfRVTHTyglsETYGPSTVCAWKPEWDSLPPEeqarLNARQGV---RYIGLEGLDVVDTKT-MK 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4182 PV----GVAGELCISGVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELG 4257
Cdd:PLN02479  394 PVpadgKTMGEIVMRGNMVMKGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSL 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4258 EVETQLAKIDAVQEAIVLAREDANGQQQLVAyFVAQRE--------LTAAELRATMSQELPNYMIPSYFVqLAQMPLTPN 4329
Cdd:PLN02479  467 EVENVVYTHPAVLEASVVARPDERWGESPCA-FVTLKPgvdksdeaALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTAT 544
                         570
                  ....*....|
gi 386647928 4330 GKIDRKALPA 4339
Cdd:PLN02479  545 GKIQKHVLRA 554
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
391-744 4.50e-12

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 73.29  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  391 SNLESVNGPEHLTYVIYTSGTTGKPKGNLTTHRNIIrvVKNTNYIDVTG---QDKLLQLSSYSFDGSTFDIFGALLNGAK 467
Cdd:PLN02860  163 TELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALI--VQSLAKIAIVGygeDDVYLHTAPLCHIGGLSSALAMLMVGAC 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  468 LVLVPK---ETVLDVaklaglIEKQQISVMFITTAFFNVLV-----DMNPDCLRHARAILFGGERVSVSHVRKALGHLGP 539
Cdd:PLN02860  241 HVLLPKfdaKAALQA------IKQHNVTSMITVPAMMADLIsltrkSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPN 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  540 GKIKHVYGPTE---STVFATSYDvHEVEEGAVSIPIGGPISNTAIYivnaqnklQPIGV-AG------ELCVAGDG---- 605
Cdd:PLN02860  315 AKLFSAYGMTEacsSLTFMTLHD-PTLESPKQTLQTVNQTKSSSVH--------QPQGVcVGkpaphvELKIGLDEssrv 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  606 ---LARGylnrPDLTAEKFADNPFAPGERM----YRTGDLArWLPD-GTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLE 677
Cdd:PLN02860  386 griLTRG----PHVMLGYWGQNSETASVLSndgwLDTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHP 460
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  678 AIEKATVV-VRESANGEKQLCAYYV------ADRSLPANEVRSTLSQE----------LPAYMLPSYFVQLE-QMPLTTN 739
Cdd:PLN02860  461 GVASVVVVgVPDSRLTEMVVACVRLrdgwiwSDNEKENAKKNLTLSSEtlrhhcreknLSRFKIPKLFVQWRkPFPLTTT 540

                  ....*
gi 386647928  740 GKVDR 744
Cdd:PLN02860  541 GKIRR 545
PLN02614 PLN02614
long-chain acyl-CoA synthetase
4914-5297 4.61e-12

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 73.52  E-value: 4.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4914 TYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVgALAVWKAGGAY-VPLDPDYPSDRIQFMLEDSAASVLLTQT 4992
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWII-SMEACNAHGLYcVPLYDTLGAGAVEFIISHSEVSIVFVEE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 ----------------------------HLQERAQQWGQTLQAalcLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTG 5044
Cdd:PLN02614  160 kkiselfktcpnsteymktvvsfggvsrEQKEEAETFGLVIYA---WDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5045 RPKGVMIEHRSLVNTAAGYRR------------EYRLDQFPVR----------LLQLASfSFDVFVGDIARTLYNGGTM- 5101
Cdd:PLN02614  237 DPKGVMISNESIVTLIAGVIRllksanaaltvkDVYLSYLPLAhifdrvieecFIQHGA-AIGFWRGDVKLLIEDLGELk 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5102 --VICPKDDRIDpaRLHYWISEE-------KITIFESTPALIIPFMDYVAEHgldmssmvllITSSDSCSVTDYRVLQER 5172
Cdd:PLN02614  316 ptIFCAVPRVLD--RVYSGLQKKlsdggflKKFVFDSAFSYKFGNMKKGQSH----------VEASPLCDKLVFNKVKQG 383
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5173 FGSQFRII------------------------NAYGVTE--AAIDSSLYDEplakLPEAGNVpiGKAALNakfyiVDAHL 5226
Cdd:PLN02614  384 LGGNVRIIlsgaaplashvesflrvvacchvlQGYGLTEscAGTFVSLPDE----LDMLGTV--GPPVPN-----VDIRL 452
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 5227 NPVP--------VGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKI 5297
Cdd:PLN02614  453 ESVPemeydalaSTPRGEICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDRKKNIFKL 524
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
3866-4336 4.81e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 73.24  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3866 RNPDAVAVvfeksQLTYGELNERANRLARTLRDAGVRPDQlVGLMVERSLEMVVGIMAIMKAGGAYIPI-DPEYP--EDR 3942
Cdd:PRK12476   60 HSAAGCAV-----ELTWTQLGVRLRAVGARLQQVAGPGDR-VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAER 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3943 IRYMLEDSGAQALLTQRHLRERV-SF--------AGTFVAVDDEQAyhADGSNLEPV-VGPNHLAYVIYTSGTTGKPKGV 4012
Cdd:PRK12476  134 LDTALRDAEPTVVLTTTAAAEAVeGFlrnlprlrRPRVIAIDAIPD--SAGESFVPVeLDTDDVSHLQYTSGSTRPPVGV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4013 MVEHHGLCSlklmfaNTLQMT----EQDRVVQFAS---LSFDASCWEI-FKALFFG-ATLYIPTSTTILDY----PLFES 4079
Cdd:PRK12476  212 EITHRAVGT------NLVQMIlsidLLDRNTHGVSwlpLYHDMGLSMIgFPAVYGGhSTLMSPTAFVRRPQrwikALSEG 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4080 YMNENGITATilpPTYAAYLNPDR-MP--------SLKKLITGGSAASVefvqqwkDKVLYFNA---------------Y 4135
Cdd:PRK12476  286 SRTGRVVTAA---PNFAYEWAAQRgLPaegddidlSNVVLIIGSEPVSI-------DAVTTFNKafapyglprtafkpsY 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4136 GPTEASI-VTSIWDEASDS--------LGDRKSVPI-------------GRPLANHRIYVVD-SHNRMLPVGVAGELCIS 4192
Cdd:PRK12476  356 GIAEATLfVATIAPDAEPSvvyldreqLGAGRAVRVaadapnavahvscGQVARSQWAVIVDpDTGAELPDGEVGEIWLH 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4193 GVGLARGYLNRPELTAEKF-------------VDNPfEPGERMYRTGDLVRWLpDGNLEYLGRIDHQVKIRGYRIELGEV 4259
Cdd:PRK12476  436 GDNIGRGYWGRPEETERTFgaklqsrlaegshADGA-ADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDI 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4260 ETQLAKID-AVQEAIVLARE-DANGQQQLVayFVAQRELTAAE---------LRATMSQElpnYMIPSY---FVQLAQMP 4325
Cdd:PRK12476  514 EATVAEASpMVRRGYVTAFTvPAEDNERLV--IVAERAAGTSRadpapaidaIRAAVSRR---HGLAVAdvrLVPAGAIP 588
                         570
                  ....*....|.
gi 386647928 4326 LTPNGKIDRKA 4336
Cdd:PRK12476  589 RTTSGKLARRA 599
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
5939-6420 4.84e-12

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 73.28  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5939 QLFEEQAERIPDHLAVTFED---KQLTYGELNERANRLARTLRNA-GVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVP 6014
Cdd:PRK05620   14 RILEYGSTVHGDTTVTTWGGaeqEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6015 IDPDYPEDRIRYMLEDSGAKLLLVQGHLLDR------------------ASFADK-------------LVNLNDDGAYHE 6063
Cdd:PRK05620   94 LNKQLMNDQIVHIINHAEDEVIVADPRLAEQlgeilkecpcvravvfigPSDADSaaahmpegikvysYEALLDGRSTVY 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6064 DGSNLepvngPEHLTYVI-YTSGTTGRPKGVMVEHRNV----VRLVKNTNYVELNEQT--------HILQTGAVVfdast 6130
Cdd:PRK05620  174 DWPEL-----DETTAAAIcYSTGTTGAPKGVVYSHRSLylqsLSLRTTDSLAVTHGESflccvpiyHVLSWGVPL----- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6131 feiwGALLNGGRLyVVRNETiLDAVSLKNAI------QQYGINTMWLTAPLYnqlSQQDSGMFAGLKTLIVGGDVLSvPH 6204
Cdd:PRK05620  244 ----AAFMSGTPL-VFPGPD-LSAPTLAKIIatamprVAHGVPTLWIQLMVH---YLKNPPERMSLQEIYVGGSAVP-PI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6205 INRVLREHAGLSIVNGYGPTENTTFSTTHT----IVGEQKEAVPIGK---PINNSTAYIVDSKLSLLPVGVWGELIVGGD 6277
Cdd:PRK05620  314 LIKAWEERYGVDVVHVWGMTETSPVGTVARppsgVSGEARWAYRVSQgrfPASLEYRIVNDGQVMESTDRNEGEIQVRGN 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6278 GVARGYLNRP----------------ELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGE 6341
Cdd:PRK05620  394 WVTASYYHSPteegggaastfrgedvEDANDRFTADGWL------RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQ 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6342 IEEQLLKVASVKEATVIVREDES-GQKQLCAYFVAE----RELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKID 6416
Cdd:PRK05620  468 LENYIMAAPEVVECAVIGYPDDKwGERPLAVTVLAPgiepTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFD 547

                  ....
gi 386647928 6417 RRAL 6420
Cdd:PRK05620  548 KKDL 551
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2931-3219 5.26e-12

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 72.52  E-value: 5.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2931 LTPIQHWFFepqfaephhfnqsvmLHRRDGF------------------DEAAIRKVLQKLVEHHDALRVVFHksENGYt 2992
Cdd:cd19535     4 LTDVQYAYW---------------IGRQDDQelggvgchaylefdgedlDPDRLERAWNKLIARHPMLRAVFL--DDGT- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2993 awNRAIGEGELYGLEVVDLKGieESAQAVEAKANEIQSS-----IDLEAGPFVKAGLFQCADGDH-------LLivihhg 3060
Cdd:cd19535    66 --QQILPEVPWYGITVHDLRG--LSEEEAEAALEELRERlshrvLDVERGPLFDIRLSLLPEGRTrlhlsidLL------ 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3061 VVDGVSWRILLEDLAIGYEQAvkGEELRFPAKTdaYRTWSEQLAAYAQSPViERELAYW-KRVAQTEVQP-LPkdeqvdv 3138
Cdd:cd19535   136 VADALSLQILLRELAALYEDP--GEPLPPLELS--FRDYLLAEQALRETAY-ERARAYWqERLPTLPPAPqLP------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3139 sLQQDSESIS-IEWTREETE------QLLKGVHRAYNTEMNDILLAALGMAVQKWSGLDRVLVNLEGHGRESIMTDIDit 3211
Cdd:cd19535   204 -LAKDPEEIKePRFTRREHRlsaeqwQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVN-- 280

                  ....*...
gi 386647928 3212 RTVGWFTS 3219
Cdd:cd19535   281 DVVGDFTS 288
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
7663-7929 5.35e-12

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 72.33  E-value: 5.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7663 ILDYPLFESymnenGITAAILPPTYAIYLSPDRL--------PSLKKLIT---GGSAASVEFVQQWK-DKVRYFNAYGPT 7730
Cdd:PRK07445  190 ILPYKRLKS-----GQELPPNPSDFFLSLVPTQLqrllqlrpQWLAQFRTillGGAPAWPSLLEQARqLQLRLAPTYGMT 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7731 E-ASIVTsvwAASPDGLDLRSVPIGRPIANHQIFIVDSQnhmlpvgvAGELCISGAGLARGYLnrPEltaekFVDNPfla 7809
Cdd:PRK07445  265 EtASQIA---TLKPDDFLAGNNSSGQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQ-----ILDSQ--- 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7810 geRMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV-ADRELT 7888
Cdd:PRK07445  324 --GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVpKDPSIS 401
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 386647928 7889 VSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDRNALP 7929
Cdd:PRK07445  402 LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
4913-5299 5.76e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 73.24  E-value: 5.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRaQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPL-DPDYP--SDRIQFMLEDSAASVLL 4989
Cdd:PRK12476   69 LTWTQLGVRLRAVGARLQ-QVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4990 TQTHLQERAQQWGQTLQAA-----LCLDDEAAYAEDASNVANVNEpHDLAYVIYTSGTTGRPKGVMIEHRslvntAAGyr 5064
Cdd:PRK12476  148 TTTAAAEAVEGFLRNLPRLrrprvIAIDAIPDSAGESFVPVELDT-DDVSHLQYTSGSTRPPVGVEITHR-----AVG-- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5065 reyrldqfpVRLLQLAsFSFDVFVGDIART----LYN--GGTMVICP-----KDDRIDPA----RLHYWISEEKI----- 5124
Cdd:PRK12476  220 ---------TNLVQMI-LSIDLLDRNTHGVswlpLYHdmGLSMIGFPavyggHSTLMSPTafvrRPQRWIKALSEgsrtg 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5125 TIFESTPALIipfMDYVAEHGL-------DMSSMVLLItSSDSCSVTDYRVLQERFG----SQFRIINAYGVTEA----- 5188
Cdd:PRK12476  290 RVVTAAPNFA---YEWAAQRGLpaegddiDLSNVVLII-GSEPVSIDAVTTFNKAFApyglPRTAFKPSYGIAEAtlfva 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5189 -----AIDSSLY--DEPL---------AKLPEA-GNVPIGKAALNAKFYIVDAHL-NPVPVGVLGELCIGGIGVARGYLN 5250
Cdd:PRK12476  366 tiapdAEPSVVYldREQLgagravrvaADAPNAvAHVSCGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWG 445
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 5251 RPELTEEKF---VDSPFVEGE---------RLYRTGDLARWMpDGNVDFIGRIDNQAKIRG 5299
Cdd:PRK12476  446 RPEETERTFgakLQSRLAEGShadgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDG 505
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
7471-7842 5.91e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 72.85  E-value: 5.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7471 QLTYRELNERanrlartLRAEGVQADQ------PVGLMIERSLEMIVGAFAIMKAGGAYVPI-DPEYP--EDRIRYMLED 7541
Cdd:PRK12476   68 ELTWTQLGVR-------LRAVGARLQQvagpgdRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7542 SGAQVLLTQRHLQECV-SFDGK--------VIAADD-EQAYGEDGSNLEPVVgpNHLAYVIYTSGTTGKPKGVMVEHHGL 7611
Cdd:PRK12476  141 AEPTVVLTTTAAAEAVeGFLRNlprlrrprVIAIDAiPDSAGESFVPVELDT--DDVSHLQYTSGSTRPPVGVEITHRAV 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7612 CS-LKLMFaetLRITEEDRVVQFAS---LSFDASCWEI-FKALFFG-ATLYIPAkdTILDYP------LFESYMNENGIT 7679
Cdd:PRK12476  219 GTnLVQMI---LSIDLLDRNTHGVSwlpLYHDMGLSMIgFPAVYGGhSTLMSPT--AFVRRPqrwikaLSEGSRTGRVVT 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7680 AAilpPTYAIYLSPDR-LP--------SLKKLITGGSAASVefvqqwkDKVRYFNA---------------YGPTEASIV 7735
Cdd:PRK12476  294 AA---PNFAYEWAAQRgLPaegddidlSNVVLIIGSEPVSI-------DAVTTFNKafapyglprtafkpsYGIAEATLF 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7736 TSVWA--ASPDGLDL--------RSVPI-------------GRPIANHQIFIVD-SQNHMLPVGVAGELCISGAGLARGY 7791
Cdd:PRK12476  364 VATIApdAEPSVVYLdreqlgagRAVRVaadapnavahvscGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGY 443
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 7792 LNRPELTAEKF---VDNPFLAGE---------RMYRTGDLARWLpDGNIEYLGRIDHQVKIRG 7842
Cdd:PRK12476  444 WGRPEETERTFgakLQSRLAEGShadgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDG 505
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
8213-8466 6.48e-12

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 73.56  E-value: 6.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8213 WLQTLAGeLPVIELPTDYERTSTRSFEGAELEFEADEAltqrlnELAARHESTLYMVLLSAYTVLLSKYSGQEDIIVGTp 8292
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8293 vagRTHADVEPIIgmfvntlaIRNYPAGDKTFLSYLEEVKETTLGAFEHQDYPFEELVERLNVKRDASRNPV-FDTMFVl 8371
Cdd:TIGR03443   74 ---SSNKSGRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPlFRLAFQ- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  8372 qntedrgiEADAFSLTPFVFDQTVaaqfDLTLSVAEDDGAIRGSFQYAAKLFKATMIRKMSKDLLAVLEQICGNPDIRLS 8451
Cdd:TIGR03443  142 --------DAPDNQQTTYSTGSTT----DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIG 209
                          250
                   ....*....|....*
gi 386647928  8452 QIQLNEPenDSNDSL 8466
Cdd:TIGR03443  210 KVSLITP--SQKSLL 222
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
5962-6415 6.67e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 72.82  E-value: 6.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5962 TYGELNERANRLARTLRNAGVQPDQMVGLMV---ERSLEM---VVGMIAILKAggayvpIDPDYPEDRIRYMLEDSGAKL 6035
Cdd:PRK07008   41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAyygVSGSGAVCHT------INPRLFPEQIAYIVNHAEDRY 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6036 L--------LVQG------------HLLDRASF-ADKLVNLNDDGAYH-EDGSNLEPVNGPEHLTYVIYTSGTTGRPKGV 6093
Cdd:PRK07008  115 VlfdltflpLVDAlapqcpnvkgwvAMTDAAHLpAGSTPLLCYETLVGaQDGDYDWPRFDENQASSLCYTSGTTGNPKGA 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6094 MVEHRNVVRlvkNTNYVELNEQTHILQTGAVVFDASTFEI--WG----ALLNGGRLyvVRNETILDAVSLKNAIQQ---- 6163
Cdd:PRK07008  195 LYSHRSTVL---HAYGAALPDAMGLSARDAVLPVVPMFHVnaWGlpysAPLTGAKL--VLPGPDLDGKSLYELIEAervt 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6164 --YGINTMWLTapLYNQLsQQDSGMFAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTENTTFSTTHTIVGEQkE 6241
Cdd:PRK07008  270 fsAGVPTVWLG--LLNHM-REAGLRFSTLRRTVIGGSACP-PAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKH-S 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6242 AVPI----------GKPINNSTAYIVDSKLSLLPvgvW-----GELIVGGDGVARGYLNRpelTAEKFVESSFlPgercy 6306
Cdd:PRK07008  345 QLPLdeqrkllekqGRVIYGVDMKIVGDDGRELP---WdgkafGDLQVRGPWVIDRYFRG---DASPLVDGWF-P----- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6307 rTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI-VREDESGQKQLCAyfVAER---ELTIG 6382
Cdd:PRK07008  413 -TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIaCAHPKWDERPLLV--VVKRpgaEVTRE 489
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 6383 ELRAALSQELPNYMIPSHFVPLERMPLTPNGKI 6415
Cdd:PRK07008  490 ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
257-746 8.25e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 72.47  E-value: 8.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  257 PRDTTIHRLFEEQAERRPDAVAVTFEDR---------QLTYGELNERANRLARTLRNAGVQADQlVGLMVERSLEMIVGI 327
Cdd:PRK12476   31 PPGTTLISLIERNIANVGDTVAYRYLDHshsaagcavELTWTQLGVRLRAVGARLQQVAGPGDR-VAILAPQGIDYVAGF 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  328 MGILKAGGAYVPI-DPEYP--EERIRYMLEDSGTQVLLSQGHLQERV-SFSGTWIRLDD------EEAYHEDGSNLESVN 397
Cdd:PRK12476  110 FAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEAVeGFLRNLPRLRRprviaiDAIPDSAGESFVPVE 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  398 -GPEHLTYVIYTSGTTGKPKGNLTTHR----NIIRVVKNTNYIDVTGQDkLLQLSSYSFDGSTFDIFGALLNGAKLVLVP 472
Cdd:PRK12476  190 lDTDDVSHLQYTSGSTRPPVGVEITHRavgtNLVQMILSIDLLDRNTHG-VSWLPLYHDMGLSMIGFPAVYGGHSTLMSP 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  473 KETV---------LDVAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRHArAILFGGERVSVSHVR---KALGHLG-- 538
Cdd:PRK12476  269 TAFVrrpqrwikaLSEGSRTGRVVTAAPNFAYEWAAQRGLPAEGDDIDLSNV-VLIIGSEPVSIDAVTtfnKAFAPYGlp 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  539 PGKIKHVYGPTESTVF-----------ATSYDVHEVEEG-AVSIPIGGP------------ISNTAIYIVNAQNKLQPIG 594
Cdd:PRK12476  348 RTAFKPSYGIAEATLFvatiapdaepsVVYLDREQLGAGrAVRVAADAPnavahvscgqvaRSQWAVIVDPDTGAELPDG 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  595 VAGELCVAGDGLARGYLNRPDLTAEKF-------------ADNPfAPGERMYRTGDLARWLpDGTIEYVGRIDDQVKIRG 661
Cdd:PRK12476  428 EVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshADGA-ADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDG 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  662 FRIELGEIEAhllkleAIEKATVVVRE------SANGEKQLCAYYVADRSL--------PANE-VRSTLSQELPAYMLPS 726
Cdd:PRK12476  506 RNHYPQDIEA------TVAEASPMVRRgyvtafTVPAEDNERLVIVAERAAgtsradpaPAIDaIRAAVSRRHGLAVADV 579
                         570       580
                  ....*....|....*....|
gi 386647928  727 YFVQLEQMPLTTNGKVDRRA 746
Cdd:PRK12476  580 RLVPAGAIPRTTSGKLARRA 599
PLN02614 PLN02614
long-chain acyl-CoA synthetase
1324-1707 1.02e-11

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 72.36  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1324 TYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVgALAVWKAGGAY-VPLDPDYPSDRIQFMLEDSAASVLLTQT 1402
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWII-SMEACNAHGLYcVPLYDTLGAGAVEFIISHSEVSIVFVEE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 ----------------------------HLQERAQQWGQTLQAvlcLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTG 1454
Cdd:PLN02614  160 kkiselfktcpnsteymktvvsfggvsrEQKEEAETFGLVIYA---WDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1455 RPKGVMIEHRSLVNTAAGYrreyrldqfpVRLLQLASFSF---DVFVGDIART-----------LYNGGTMVICPKDDRI 1520
Cdd:PLN02614  237 DPKGVMISNESIVTLIAGV----------IRLLKSANAALtvkDVYLSYLPLAhifdrvieecfIQHGAAIGFWRGDVKL 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1521 dparLHYWISEEKITIFESTPALIIP--------------FMDYVAEHGL-----DMSSMELLITSSDSCSVTDYRVLQE 1581
Cdd:PLN02614  307 ----LIEDLGELKPTIFCAVPRVLDRvysglqkklsdggfLKKFVFDSAFsykfgNMKKGQSHVEASPLCDKLVFNKVKQ 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1582 RFGSQFRII------------------------NAYGVTE--AAIDSSLYDEplakLPEAGNVpiGKAALNakfyiVDAH 1635
Cdd:PLN02614  383 GLGGNVRIIlsgaaplashvesflrvvacchvlQGYGLTEscAGTFVSLPDE----LDMLGTV--GPPVPN-----VDIR 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1636 LNPVP--------VGVLGELCIGGIGVARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKI 1707
Cdd:PLN02614  452 LESVPemeydalaSTPRGEICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDRKKNIFKL 524
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
6074-6338 1.07e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 72.44  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6074 PEHLTYVIYTSGTTGRPKGVMVEHRN----VVRLVKNTNYVELNEQTH--------ILQTGAV---VFDASTFEIWGALL 6138
Cdd:PTZ00342  303 PDFITSIVYTSGTSGKPKGVMLSNKNlyntVVPLCKHSIFKKYNPKTHlsylpishIYERVIAylsFMLGGTINIWSKDI 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6139 N--------------GG------RLYVVRNETILDAVSLKNAIQQygiNTMWLTAPLYN-QLSQQDSGMF---------- 6187
Cdd:PTZ00342  383 NyfskdiynskgnilAGvpkvfnRIYTNIMTEINNLPPLKRFLVK---KILSLRKSNNNgGFSKFLEGIThisskikdkv 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6188 -AGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTEnttfsTTHTIVGEQKE---AVPIGKPINNSTAYIVDS---- 6259
Cdd:PTZ00342  460 nPNLEVILNGGGKLS-PKIAEELSVLLNVNYYQGYGLTE-----TTGPIFVQHADdnnTESIGGPISPNTKYKVRTwety 533
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6260 -KLSLLPVGvwgELIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGDLARWLPDGTLEYKGRIDEQVKI-RGYRI 6337
Cdd:PTZ00342  534 kATDTLPKG---ELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYI 604

                  .
gi 386647928 6338 E 6338
Cdd:PTZ00342  605 E 605
PLN02479 PLN02479
acetate-CoA ligase
2338-2830 1.15e-11

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 71.80  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2338 AADYEAdKTIHQLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLK 2417
Cdd:PLN02479   14 AANYTA-LTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPM 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2418 AGGAYVPIDPEYPEDRISYMLEDSSAQVL--------LAQRRL-----QERVSFAGTVVTV--DDEQayagDGSNLESAV 2482
Cdd:PLN02479   93 AGAVVNCVNIRLNAPTIAFLLEHSKSEVVmvdqefftLAEEALkilaeKKKSSFKPPLLIVigDPTC----DPKSLQYAL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2483 GPNDLAY------------------------IIYTSGTTGKPKGVMVEHHG--LCSLkqmfANTLQINAQDRVVQFASLS 2536
Cdd:PLN02479  169 GKGAIEYekfletgdpefawkppadewqsiaLGYTSGTTASPKGVVLHHRGayLMAL----SNALIWGMNEGAVYLWTLP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2537 -FDASCWEVFQTL--FFGATLYIPTKETILDYQwferYMSDNGITTATLPPtyaVYLN-----PDH-----MPDFKRLIA 2603
Cdd:PLN02479  245 mFHCNGWCFTWTLaaLCGTNICLRQVTAKAIYS----AIANYGVTHFCAAP---VVLNtivnaPKSetilpLPRVVHVMT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2604 AGSASSLELLQQWKDK-VKYFNAYGPTE----DSICTtiWTPstedisQLKSVPiggPIVNHRIY--------------I 2664
Cdd:PLN02479  318 AGAAPPPSVLFAMSEKgFRVTHTYGLSEtygpSTVCA--WKP------EWDSLP---PEEQARLNarqgvryiglegldV 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2665 VDAH-YQPVPV--GVAGELCIAGVGLARGYLNRPDLTAEKFVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIR 2741
Cdd:PLN02479  387 VDTKtMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISG 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2742 GYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYFV-------ADRTMTVGELRGELSGELPGYMIPAHFVqLER 2814
Cdd:PLN02479  460 GENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVPKSVV-FGP 538
                         570
                  ....*....|....*.
gi 386647928 2815 MPLTPNGKIDRKALPA 2830
Cdd:PLN02479  539 LPKTATGKIQKHVLRA 554
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
5407-5466 1.16e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 63.35  E-value: 1.16e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  5407 AKLVSIWQEVLGL--EKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEE 5466
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
2370-2827 1.26e-11

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 72.08  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2370 QLTYRELNERANRLARTLQALGVKTDQpVGLMLERSLEMVVGMFAVLKAGGAYVPI-DPEYP--EDRISYMLEDSSAQVL 2446
Cdd:PRK12476   68 ELTWTQLGVRLRAVGARLQQVAGPGDR-VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2447 LAQRRLQERV-SF--------AGTVVTVDDEQAYAGDGSnLESAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCS-LKQM 2516
Cdd:PRK12476  147 LTTTAAAEAVeGFlrnlprlrRPRVIAIDAIPDSAGESF-VPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTnLVQM 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2517 FantLQINAQDRVVQFAS---LSFDASCWEV-FQTLFFG-ATLYIPTKETILDYQWFeRYMSDNGIT--TATLPPTYAVY 2589
Cdd:PRK12476  226 I---LSIDLLDRNTHGVSwlpLYHDMGLSMIgFPAVYGGhSTLMSPTAFVRRPQRWI-KALSEGSRTgrVVTAAPNFAYE 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2590 LN-----PDHMPDFK----RLIAAGSASSLellqqwkDKVKYFNA---------------YGPTEDSICTTIWTPSTE-- 2643
Cdd:PRK12476  302 WAaqrglPAEGDDIDlsnvVLIIGSEPVSI-------DAVTTFNKafapyglprtafkpsYGIAEATLFVATIAPDAEps 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2644 ----DISQL---KSVPI-------------GGPIVNHRIYIVDAHY-QPVPVGVAGELCIAGVGLARGYLNRPDLTAEKF 2702
Cdd:PRK12476  375 vvylDREQLgagRAVRVaadapnavahvscGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTF 454
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2703 -------------VDNPfEPGERMYRTGDLAKWLpDGTIEYLGRIDHQVKIRGYRIELGEIEeqllkvASVQEA--IV-- 2765
Cdd:PRK12476  455 gaklqsrlaegshADGA-ADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIE------ATVAEAspMVrr 526
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 2766 --IAHDDASGQKQLCAYFVADRTMTVGE---------LRGELSGElpgYMIPAH---FVQLERMPLTPNGKIDRKA 2827
Cdd:PRK12476  527 gyVTAFTVPAEDNERLVIVAERAAGTSRadpapaidaIRAAVSRR---HGLAVAdvrLVPAGAIPRTTSGKLARRA 599
PLN03102 PLN03102
acyl-activating enzyme; Provisional
407-747 1.35e-11

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 71.59  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  407 YTSGTTGKPKGNLTTHRNIIRVVKNTnyidVTGQDK------LLQLSSYSFDGSTFdIFGALLNGAKLVLVPKETVLDVA 480
Cdd:PLN03102  193 YTSGTTADPKGVVISHRGAYLSTLSA----IIGWEMgtcpvyLWTLPMFHCNGWTF-TWGTAARGGTSVCMRHVTAPEIY 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  481 KLaglIEKQQISVMFITTAFFNVLVDMNPDCLRHARA---ILFGGERVSVSHVRKaLGHLGpGKIKHVYGPTEST---VF 554
Cdd:PLN03102  268 KN---IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGpvhVLTGGSPPPAALVKK-VQRLG-FQVMHAYGLTEATgpvLF 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  555 ATSYDVHE--VEEGAVSIPIGGPISNTAIYIVNAQNKLQPIGVA------GELCVAGDGLARGYLNRPDLTAEKFADNpf 626
Cdd:PLN03102  343 CEWQDEWNrlPENQQMELKARQGVSILGLADVDVKNKETQESVPrdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHG-- 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  627 apgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYVADRSL 706
Cdd:PLN03102  421 -----WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGE 495
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928  707 PANEVRSTL------------SQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PLN03102  496 TTKEDRVDKlvtrerdlieycRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
5955-6420 1.61e-11

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 71.31  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5955 TFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAK 6034
Cdd:cd05915    19 TGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6035 LLLVQGHLLDRASFADKLV-----NLNDDGAY--HED-----GSNLEPVNGPEHLTYVI--YTSGTTGRPKGVMVEHRNV 6100
Cdd:cd05915    99 VLLFDPNLLPLVEAIRGELktvqhFVVMDEKApeGYLayeeaLGEEADPVRVPERAACGmaYTTGTTGLPKGVVYSHRAL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6101 ---VRLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYVVR----NETILDAVsLKNAIQQYGintmwLTA 6173
Cdd:cd05915   179 vlhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGprldPASLVELF-DGEGVTFTA-----GVP 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6174 PLYNQLSQQDSGM---FAGLKTLIVGGDvlSVPHINRVLREHAGLSIVNGYGPTENTTFSTT-------HTIVGEQK--- 6240
Cdd:cd05915   253 TVWLALADYLESTghrLKTLRRLVVGGS--AAPRSLIARFERMGVEVRQGYGLTETSPVVVQnfvkshlESLSEEEKltl 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6241 ----------EAVPIGKPINNSTAYivDSKLSLLpvgvwgeLIVGGDGVARGYLNRPELTAEKFVESSFlpgercYRTGD 6310
Cdd:cd05915   331 kaktglpiplVRLRVADEEGRPVPK--DGKALGE-------VQLKGPWITGGYYGNEEATRSALTPDGF------FRTGD 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6311 LARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYF-VAERELTIGELRAALS 6389
Cdd:cd05915   396 IAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvPRGEKPTPEELNEHLL 475
                         490       500       510
                  ....*....|....*....|....*....|..
gi 386647928 6390 QELPNY-MIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05915   476 KAGFAKwQLPDAYVFAEEIPRTSAGKFLKRAL 507
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1817-1876 1.64e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 62.97  E-value: 1.64e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  1817 AKLASIWQEVLGL--EKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEE 1876
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1307-1459 1.75e-11

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 71.06  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 1386
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QfmledsaasVLLTQthlqeraqqwgQTLQAVLCLDDEAAYAE-DASNVANVNEPHDLAY-------VIYTSGTTGRPKG 1458
Cdd:PRK09029   93 E---------ELLPS-----------LTLDFALVLEGENTFSAlTSLHLQLVEGAHAVAWqpqrlatMTLTSGSTGLPKA 152

                  .
gi 386647928 1459 V 1459
Cdd:PRK09029  153 A 153
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1308-1709 1.99e-11

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 71.31  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1308 ERTPEVAAVvyendRLTYRELNERANRLARMLRaQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPL-DPDYP--SD 1384
Cdd:PRK12476   59 SHSAAGCAV-----ELTWTQLGVRLRAVGARLQ-QVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1385 RIQFMLEDSAASVLLTQTHLQERAQQWGQTLQA-----VLCLDDEAAYAEDASNVANVNEpHDLAYVIYTSGTTGRPKGV 1459
Cdd:PRK12476  133 RLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRlrrprVIAIDAIPDSAGESFVPVELDT-DDVSHLQYTSGSTRPPVGV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1460 MIEHRslvntAAGyrreyrldqfpVRLLQLAsFSFDVFVGDIART----LYN--GGTMVICP-----KDDRIDPA----R 1524
Cdd:PRK12476  212 EITHR-----AVG-----------TNLVQMI-LSIDLLDRNTHGVswlpLYHdmGLSMIGFPavyggHSTLMSPTafvrR 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1525 LHYWISEEKI-----TIFESTPALIipfMDYVAEHGL-------DMSSMeLLITSSDSCSVTDYRVLQERFG----SQFR 1588
Cdd:PRK12476  275 PQRWIKALSEgsrtgRVVTAAPNFA---YEWAAQRGLpaegddiDLSNV-VLIIGSEPVSIDAVTTFNKAFApyglPRTA 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1589 IINAYGVTEA----------AIDSSLY--DEPL---------AKLPEA-GNVPIGKAALNAKFYIVDAHL-NPVPVGVLG 1645
Cdd:PRK12476  351 FKPSYGIAEAtlfvatiapdAEPSVVYldREQLgagravrvaADAPNAvAHVSCGQVARSQWAVIVDPDTgAELPDGEVG 430
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1646 ELCIGGIGVARGYLNRPELTEEKF---VDSPFVEGE---------RLYRTGDLARWMpDGNVDFIGRIDNQAKIRG 1709
Cdd:PRK12476  431 EIWLHGDNIGRGYWGRPEETERTFgakLQSRLAEGShadgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDG 505
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
5958-6420 2.17e-11

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 70.53  E-value: 2.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5958 DKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLL 6037
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6038 VQgHLLDRASFADKLVNLNDDGAYHedgsnlepvngpEHLTYvIYTSGTTGRPKGVMVEHRNVVRLVKNTNYvelneqTH 6117
Cdd:cd05939    81 FN-LLDPLLTQSSTEPPSQDDVNFR------------DKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYY------AF 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6118 ILQTGAVVFDA-----STFEIWG---ALLNGGRLyVVRNE-----TILDAVSLKNAIQQYgINTM--WLTAPLYNQLSQQ 6182
Cdd:cd05939   141 GMRPEDVVYDClplyhSAGGIMGvgqALLHGSTV-VIRKKfsasnFWDDCVKYNCTIVQY-IGEIcrYLLAQPPSEEEQK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6183 DSGMFA---GLKTLIVGGDV--LSVPHINRVlrehaglsivngYGPTE-NTTFSTTHTIVGeqkeavPIG-KPINNSTAY 6255
Cdd:cd05939   219 HNVRLAvgnGLRPQIWEQFVrrFGIPQIGEF------------YGATEgNSSLVNIDNHVG------ACGfNSRILPSVY 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6256 IVdsklSLLPVG-VWGELIVGGDGVA------------------------RGYLNRPElTAEKFVESSFLPGERCYRTGD 6310
Cdd:cd05939   281 PI----RLIKVDeDTGELIRDSDGLCipcqpgepgllvgkiiqndplrrfDGYVNEGA-TNKKIARDVFKKGDSAFLSGD 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6311 LARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI---VREDEsGQKQLCAYFVAERELTIGELRAA 6387
Cdd:cd05939   356 VLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYgveVPGVE-GRAGMAAIVDPERKVDLDRFSAV 434
                         490       500       510
                  ....*....|....*....|....*....|...
gi 386647928 6388 LSQELPNYMIPSHFVPLERMPLTPNGKIDRRAL 6420
Cdd:cd05939   435 LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
1318-1718 2.34e-11

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 70.78  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1318 YENDRLTYRELNERANRLARMLRAQ-GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAAS 1396
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1397 VLLTQTHLQERAQQWGQTLQA----------------VLCLDDEAAYAED----ASNVANVNePHDLAYVIYTSGTTGRP 1456
Cdd:cd05938    81 VLVVAPELQEAVEEVLPALRAdgvsvwylshtsntegVISLLDKVDAASDepvpASLRAHVT-IKSPALYIYTSGTTGLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1457 KGVMIEHRSLVNTAA-----GYRREyrlDQFPVRL-LQLASFSFDVFVGDIARtlynGGTMVICPK-------DDridpA 1523
Cdd:cd05938   160 KAARISHLRVLQCSGflslcGVTAD---DVIYITLpLYHSSGFLLGIGGCIEL----GATCVLKPKfsasqfwDD----C 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1524 RLHywiseeKITIFEstpaliipfmdYVAEhgldmsSMELLITSSDSCSVTDYRV---------------LQERFGsQFR 1588
Cdd:cd05938   229 RKH------NVTVIQ-----------YIGE------LLRYLCNQPQSPNDRDHKVrlaignglradvwreFLRRFG-PIR 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1589 IINAYGVTEAAIDSSLYdeplaklpeAGNV-PIGKA-ALNAKFY--------------IVDA--HLNPVPVGVLGELcig 1650
Cdd:cd05938   285 IREFYGSTEGNIGFFNY---------TGKIgAVGRVsYLYKLLFpfelikfdvekeepVRDAqgFCIPVAKGEPGLL--- 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1651 gigVAR--------GYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIE 1718
Cdd:cd05938   353 ---VAKitqqspflGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVA 425
PLN02614 PLN02614
long-chain acyl-CoA synthetase
5962-6341 2.53e-11

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 71.21  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5962 TYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQ-- 6039
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEek 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6040 -------------GHLLDRASF----------ADKL---VNLNDDGAYHEDGSNLE-PVNGPEHLTYVIYTSGTTGRPKG 6092
Cdd:PLN02614  161 kiselfktcpnstEYMKTVVSFggvsreqkeeAETFglvIYAWDEFLKLGEGKQYDlPIKKKSDICTIMYTSGTTGDPKG 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6093 VMVEHRNVV-------RLVKNTN--------YVELNEQTHI---------LQTGAVV----------------FDASTF- 6131
Cdd:PLN02614  241 VMISNESIVtliagviRLLKSANaaltvkdvYLSYLPLAHIfdrvieecfIQHGAAIgfwrgdvklliedlgeLKPTIFc 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6132 -------EIWGAL---LNGGRLYvvrNETILD-AVSLKNAIQQYGiNTMWLTAPLYNQL--SQQDSGMFAGLKTLIVGGD 6198
Cdd:PLN02614  321 avprvldRVYSGLqkkLSDGGFL---KKFVFDsAFSYKFGNMKKG-QSHVEASPLCDKLvfNKVKQGLGGNVRIILSGAA 396
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6199 VLSvPHINRVLREHAGLSIVNGYGPTENTTfSTTHTIVGEQKEAVPIGKPINNstayiVDSKLSLLPVGVW--------G 6270
Cdd:PLN02614  397 PLA-SHVESFLRVVACCHVLQGYGLTESCA-GTFVSLPDELDMLGTVGPPVPN-----VDIRLESVPEMEYdalastprG 469
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 6271 ELIVGGDGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYkgrIDEQVKIrgYRIELGE 6341
Cdd:PLN02614  470 EICIRGKTLFSGYYKREDLTKEVLIDGWL-------HTGDVGEWQPNGSMKI---IDRKKNI--FKLSQGE 528
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
4897-5049 2.61e-11

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 70.29  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4897 AECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 4976
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4977 QfmledsaasVLLTQthlqeraqqwgQTLQAALCLDDEAAYAE-DASNVANVNEPHDLAY-------VIYTSGTTGRPKG 5048
Cdd:PRK09029   93 E---------ELLPS-----------LTLDFALVLEGENTFSAlTSLHLQLVEGAHAVAWqpqrlatMTLTSGSTGLPKA 152

                  .
gi 386647928 5049 V 5049
Cdd:PRK09029  153 A 153
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
7472-7834 2.68e-11

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 70.85  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQR 7551
Cdd:cd05933     9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7552 HLQECvsfdgKVIAADDE----QA---YGEDGSNLEP-------------------------VVGPNHLAYVIYTSGTTG 7599
Cdd:cd05933    89 QKQLQ-----KILQIQDKlphlKAiiqYKEPLKEKEPnlyswdefmelgrsipdeqldaiisSQKPNQCCTLIYTSGTTG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7600 KPKGVMVEHHGLCSLKLMFAETLRITEEDR----VVQFASLSF-DASCWEIFKALFFGATLYIPAKD----TILD----- 7665
Cdd:cd05933   164 MPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHiAAQILDIWLPIKVGGQVYFAQPDalkgTLVKtlrev 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7666 -----------YPLFESYMNENGITAAIL------------------------PPTYAIYL------SPDR----LPSLK 7700
Cdd:cd05933   244 rptafmgvprvWEKIQEKMKAVGAKSGTLkrkiaswakgvgletnlklmggesPSPLFYRLakklvfKKVRkalgLDRCQ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7701 KLITGGSAASVEFVQQWKD-KVRYFNAYGPTEASIVTSVwaASPDGLDLRSVPIGRPIANHQIFIVDSQNHmlpvgvaGE 7779
Cdd:cd05933   324 KFFTGAAPISRETLEFFLSlNIPIMELYGMSETSGPHTI--SNPQAYRLLSCGKALPGCKTKIHNPDADGI-------GE 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 7780 LCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRI 7834
Cdd:cd05933   395 ICFWGRHVFMGYLNMEDKTEEAIDEDGWL------HSGDLGKLDEDGFLYITGRI 443
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
5953-6422 2.72e-11

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 70.62  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5953 AVTFEDKQL---TYGELNERANRLARTLRNagvQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLE 6029
Cdd:PRK06334   35 ATVCWDEQLgklSYNQVRKAVIALATKVSK---YPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACAN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6030 DSGAKlllvqgHLLDRASFADKLVNLNDDGA-------YHEDG----SNLE----------PVN-----------GPEHL 6077
Cdd:PRK06334  112 LVGVT------HVLTSKQLMQHLAQTHGEDAeypfsliYMEEVrkelSFWEkcrigiymsiPFEwlmrwfgvsdkDPEDV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6078 TYVIYTSGTTGRPKGVMVEHRNvvrLVKNT----NYVELNEQThILQTGAVVFDASTFEIWG--ALLNGgrLYVVRNETI 6151
Cdd:PRK06334  186 AVILFTSGTEKLPKGVPLTHAN---LLANQraclKFFSPKEDD-VMMSFLPPFHAYGFNSCTlfPLLSG--VPVVFAYNP 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6152 LDAVSLKNAIQQYGInTMWLTAPLY-----NQLSQQDSGMfAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTEN 6226
Cdd:PRK06334  260 LYPKKIVEMIDEAKV-TFLGSTPVFfdyilKTAKKQESCL-PSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTEC 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6227 TTFSTTHTIVGEQKEAVpIGKPINNSTAYIVdSKLSLLPV--GVWGELIVGGDGVARGYLNRPEltAEKFVEssfLPGER 6304
Cdd:PRK06334  338 SPVITINTVNSPKHESC-VGMPIRGMDVLIV-SEETKVPVssGETGLVLTRGTSLFSGYLGEDF--GQGFVE---LGGET 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6305 CYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEAtvivREDES-------GQK-QLCAYFVAE 6376
Cdd:PRK06334  411 WYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA----DHAGPlvvcglpGEKvRLCLFTTFP 486
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 6377 RelTIGELRAAL-SQELPNYMIPSHFVPLERMPLTPNGKIDRRALPA 6422
Cdd:PRK06334  487 T--SISEVNDILkNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
PRK08162 PRK08162
acyl-CoA synthetase; Validated
3868-4337 3.01e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 70.36  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3868 PDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAY----IPIDPEypedRI 3943
Cdd:PRK08162   32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLntlnTRLDAA----SI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3944 RYMLEDSGAQALLTQRHLRERVSFA---------------------GTFVAVDDEQAYHADGSNLEPVVGPNHLAYVI-- 4000
Cdd:PRK08162  108 AFMLRHGEAKVLIVDTEFAEVAREAlallpgpkplvidvddpeypgGRFIGALDYEAFLASGDPDFAWTLPADEWDAIal 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4001 -YTSGTTGKPKGVmVEHHGLCSLKLMfANTLQMTEQDRVVQFASLS-FDASCWeifkalFFGATLYIPTSTTIL-----D 4073
Cdd:PRK08162  188 nYTSGTTGNPKGV-VYHHRGAYLNAL-SNILAWGMPKHPVYLWTLPmFHCNGW------CFPWTVAARAGTNVClrkvdP 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4074 YPLFESyMNENGIT----ATILpptYAAYLNpdrMPSLKK--------LITGGSAASVEFVQQWKD---KVLYfnAYGPT 4138
Cdd:PRK08162  260 KLIFDL-IREHGVThycgAPIV---LSALIN---APAEWRagidhpvhAMVAGAAPPAAVIAKMEEigfDLTH--VYGLT 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4139 E----ASIVT--SIWDEASDS----LGDRKSVpigRPLANHRIYVVDShNRMLPVG----VAGELCISGVGLARGYLNRP 4204
Cdd:PRK08162  331 EtygpATVCAwqPEWDALPLDeraqLKARQGV---RYPLQEGVTVLDP-DTMQPVPadgeTIGEIMFRGNIVMKGYLKNP 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4205 ELTAEKFVDNPFEpgermyrTGDLVRWLPDGnleYlgridhqVKIR----------GYRIELGEVETQLAKIDAVQEAIV 4274
Cdd:PRK08162  407 KATEEAFAGGWFH-------TGDLAVLHPDG---Y-------IKIKdrskdiiisgGENISSIEVEDVLYRHPAVLVAAV 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 4275 LAREDANGQQQLVAyFVAQRE---LTAAELRATMSQELPNYMIPSYFVqLAQMPLTPNGKIDRKAL 4337
Cdd:PRK08162  470 VAKPDPKWGEVPCA-FVELKDgasATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1288-1795 3.80e-11

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 70.43  E-value: 3.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1288 PAAPDAPENEVFHALFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAV 1367
Cdd:PRK07059   14 PAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1368 WKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTqthLQERAQqwgqTLQAVL---------------------------- 1419
Cdd:PRK07059   94 LRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVV---LENFAT----TVQQVLaktavkhvvvasmgdllgfkghivnfvv 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1420 --------------CLDDEAAYAEDAS---NVANVNePHDLAYVIYTSGTTGRPKGVMIEHRSLV-NTA-------AGYR 1474
Cdd:PRK07059  167 rrvkkmvpawslpgHVRFNDALAEGARqtfKPVKLG-PDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLqmeawlqPAFE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1475 REYRLDQFpvrllqlasfsfdVFVgdIARTLYN--------------GGTMVICPkddriDPARLHYWISE---EKITIF 1537
Cdd:PRK07059  246 KKPRPDQL-------------NFV--CALPLYHifaltvcgllgmrtGGRNILIP-----NPRDIPGFIKElkkYQVHIF 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1538 ESTPALIIPFMDYVAEHGLDMSSmeLLITSSDSCSVTdyRVLQERFGSQFR--IINAYGVTEAAidSSLYDEPLAKLPEA 1615
Cdd:PRK07059  306 PAVNTLYNALLNNPDFDKLDFSK--LIVANGGGMAVQ--RPVAERWLEMTGcpITEGYGLSETS--PVATCNPVDATEFS 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1616 GNvpIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNV 1695
Cdd:PRK07059  380 GT--IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYT 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1696 DFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFT-AESELKLSELRSSLSQELPGYMIPS 1774
Cdd:PRK07059  452 KIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVkKDPALTEEDVKAFCKERLTNYKRPK 531
                         570       580
                  ....*....|....*....|.
gi 386647928 1775 YFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK07059  532 FVEFRTELPKTNVGKILRREL 552
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4359-4418 4.31e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 61.81  E-value: 4.31e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  4359 AKLAHIWQDVLGL--EKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQFPTVEQ 4418
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK05850 PRK05850
acyl-CoA synthetase; Validated
3855-4251 4.33e-11

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 69.97  E-value: 4.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3855 TIHGLFEEQALRNPDAVAVVF---------EKSQLTYGELNERANRLARTLRDAGVRPDQLVGLmVERSLEMVVGIMAIM 3925
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTFidyeqdpagVAETLTWSQLYRRTLNVAEELRRHGSTGDRAVIL-APQGLEYIVAFLGAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3926 KAGGAYIPIDPEYP---EDRIRYMLEDSGAQALLTQR----HLRERVS-----FAGTFVAVD--DEQAyhADGSNLEPVV 3991
Cdd:PRK05850   81 QAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSavvdDVTEYVApqpgqSAPPVIEVDllDLDS--PRGSDARPRD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3992 GPNhLAYVIYTSGTTGKPKGVMVEHHGLcslklmFANTLQmteqdrvvqfaslsfdascweIFKAlFFGATLYIPTS-TT 4070
Cdd:PRK05850  159 LPS-TAYLQYTSGSTRTPAGVMVSHRNV------IANFEQ---------------------LMSD-YFGDTGGVPPPdTT 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4071 ILDY-PLFESYMNENGITATIL---------------------------PPTYAAYLN-----------PDRMPSL---- 4107
Cdd:PRK05850  210 VVSWlPFYHDMGLVLGVCAPILggcpavltspvaflqrparwmqllasnPHAFSAAPNfafelavrktsDDDMAGLdlgg 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4108 -KKLITGGSAASVEFVQQWKDKVLYFN--------AYGPTEAS--IVTSIWDEA-------SDSLGDRKSVP----IGRP 4165
Cdd:PRK05850  290 vLGIISGSERVHPATLKRFADRFAPFNlretairpSYGLAEATvyVATREPGQPpesvrfdYEKLSAGHAKRcetgGGTP 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4166 LANH--------RIyvVDSHNRM-LPVGVAGELCISGVGLARGYLNRPELTAEKF---VDNPFE--PGERMYRTGDLvRW 4231
Cdd:PRK05850  370 LVSYgsprsptvRI--VDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPgtPEGPWLRTGDL-GF 446
                         490       500
                  ....*....|....*....|
gi 386647928 4232 LPDGNLEYLGRIDHQVKIRG 4251
Cdd:PRK05850  447 ISEGELFIVGRIKDLLIVDG 466
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
1324-1721 4.60e-11

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 70.14  E-value: 4.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1324 TYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTH 1403
Cdd:cd17641    13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1404 LQ---------------------ERA-----QQWGQTLQAVLCLDDEAAYAEDASNVANVNE--PHDLAYVIYTSGTTGR 1455
Cdd:cd17641    93 EQvdklleiadripsvryviycdPRGmrkydDPRLISFEDVVALGRALDRRDPGLYEREVAAgkGEDVAVLCTTSGTTGK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1456 PKGVMIEHRSLVNTAAGYRR--EYRLDQFPVRLLQLASFSFDVFVgdIARTLYNGGTmVICPKDDR-------------- 1519
Cdd:cd17641   173 PKLAMLSHGNFLGHCAAYLAadPLGPGDEYVSVLPLPWIGEQMYS--VGQALVCGFI-VNFPEEPEtmmedlreigptfv 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1520 IDPARLhyW---ISEEKITIFESTpaliiPFMDYVAEHGLDmSSMELLITSSDSCSVTD-------------YRVLQERF 1583
Cdd:cd17641   250 LLPPRV--WegiAADVRARMMDAT-----PFKRFMFELGMK-LGLRALDRGKRGRPVSLwlrlaswladallFRPLRDRL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1584 G----------------SQFRIINA--------YGVTEAAIDSSLYDEPLAKlPEAGNVPIGKAAlnakfyivdahlnpV 1639
Cdd:cd17641   322 GfsrlrsaatggaalgpDTFRFFHAigvplkqlYGQTELAGAYTVHRDGDVD-PDTVGVPFPGTE--------------V 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1640 PVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVegerlyRTGDLARWMPDGNVDFIGRIDNQAKI-RGYRIETGEIE 1718
Cdd:cd17641   387 RIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIE 460

                  ...
gi 386647928 1719 TQL 1721
Cdd:cd17641   461 NKL 463
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
2371-2821 4.62e-11

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 70.18  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALG-VKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISY--------MLEDS 2441
Cdd:cd17632    68 ITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPilaeteprLLAVS 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2442 SAQVLLAQ---------RRL-------------------QERVSFAGTVVTVDDEQAYAGDGSNLESAVGPND----LAY 2489
Cdd:cd17632   148 AEHLDLAVeavleggtpPRLvvfdhrpevdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPdddpLAL 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2490 IIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVV-QFASLSFDASCWEVFQTLFFGATLYI------------ 2556
Cdd:cd17632   228 LIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITlNFMPMSHIAGRISLYGTLARGGTAYFaaasdmstlfdd 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2557 -----PTKETILDYQW---FERYMSD------NGITTATLPPTYAVYLNPDHMPdfKRLIAA--GSASSLELLQQWKDK- 2619
Cdd:cd17632   308 lalvrPTELFLVPRVCdmlFQRYQAEldrrsvAGADAETLAERVKAELRERVLG--GRLLAAvcGSAPLSAEMKAFMESl 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2620 --VKYFNAYGPTEDSICT---TIWTPSTEDiSQLKSVPIGGPIVNHRiyivdahyqPVPvgvAGELCIAGVGLARGYLNR 2694
Cdd:cd17632   386 ldLDLHDGYGSTEAGAVIldgVIVRPPVLD-YKLVDVPELGYFRTDR---------PHP---RGELLVKTDTLFPGYYKR 452
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2695 PDLTAEKFVDNPFepgermYRTGD-LAKWLPDgTIEYLGRIDHQVKI-RGYRIELGEIEEQLLKVASVQEAIVIAhddAS 2772
Cdd:cd17632   453 PEVTAEVFDEDGF------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYG---NS 522
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2773 GQKQLCAYFV----ADRTMTVGELRGEL---------SGELPGYMIPAHFVqLERMPLTP-NG 2821
Cdd:cd17632   523 ERAYLLAVVVptqdALAGEDTARLRAALaeslqriarEAGLQSYEIPRDFL-IETEPFTIaNG 584
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
3881-4332 5.30e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 69.74  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3881 TYGELNERANRLARTLRDAGVRPDQLVGLMV---ERSLEMVVGIMAimkAGGAYIPIDPEYPEDRIRYMLEDSGAQAL-- 3955
Cdd:PRK07008   41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSG---SGAVCHTINPRLFPEQIAYIVNHAEDRYVlf 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3956 -LTQRHLRERVsfAGT------FVAVDDE----------QAYHA-----DGSNLEPVVGPNHLAYVIYTSGTTGKPKGVM 4013
Cdd:PRK07008  118 dLTFLPLVDAL--APQcpnvkgWVAMTDAahlpagstplLCYETlvgaqDGDYDWPRFDENQASSLCYTSGTTGNPKGAL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4014 VEHHG--LCSLKLMFANTLQMTEQDRVVQFASLsFDASCWEI-FKALFFGATLYIPTSTtiLD----YPLFESymneNGI 4086
Cdd:PRK07008  196 YSHRStvLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLpYSAPLTGAKLVLPGPD--LDgkslYELIEA----ERV 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4087 TATILPPT----YAAYLNPD--RMPSLKKLITGGSAASVEFVQQWKDK--VLYFNAYGPTEAS----IVTSIWDEASDSL 4154
Cdd:PRK07008  269 TFSAGVPTvwlgLLNHMREAglRFSTLRRTVIGGSACPPAMIRTFEDEygVEVIHAWGMTEMSplgtLCKLKWKHSQLPL 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4155 GDRKSVPI--GRPLANHRIYVVDSHNRMLPV-GVA-GELCISGVGLARGYLNRpelTAEKFVDNPFEpgermyrTGDLVR 4230
Cdd:PRK07008  349 DEQRKLLEkqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRG---DASPLVDGWFP-------TGDVAT 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4231 WLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLA----REDangQQQLVAyfVAQR---ELTAAELRA 4303
Cdd:PRK07008  419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIAcahpKWD---ERPLLV--VVKRpgaEVTREELLA 493
                         490       500
                  ....*....|....*....|....*....
gi 386647928 4304 TMSQELPNYMIPSYFVQLAQMPLTPNGKI 4332
Cdd:PRK07008  494 FYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
7754-7928 5.61e-11

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 68.53  E-value: 5.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7754 GRPIANHQIFIVDsqnhmlpvgvaGELCISGAGLARGYLNRPeltaekfvDNPFLAGERMYRTGDLARwLPDGNIEYLGR 7833
Cdd:PRK07824  195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV--------DPDPFAEPGWFRTDDLGA-LDDGVLTVLGR 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7834 IDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDAN-GQQQLCAYFVADREL-TVSELRGTLSQELPGYMIPSYFVQ 7911
Cdd:PRK07824  255 ADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVAAVVGDGGPApTLEALRAHVARTLDRTAAPRELHV 334
                         170
                  ....*....|....*..
gi 386647928 7912 LEQMPLTPNGKIDRNAL 7928
Cdd:PRK07824  335 VDELPRRGIGKVDRRAL 351
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
2678-2828 6.36e-11

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 68.53  E-value: 6.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2678 GELCIAGVGLARGYLNRPDltaekfvDNPF-EPGerMYRTGDLAKwLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLK 2756
Cdd:PRK07824  208 GRIALGGPTLAKGYRNPVD-------PDPFaEPG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALAT 277
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2757 VASVQEAIVIA-HDDASGQKQLCAYFVADR-TMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PRK07824  278 HPAVADCAVFGlPDDRLGQRVVAAVVGDGGpAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
1324-1792 9.86e-11

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 68.67  E-value: 9.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1324 TYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVgalAVWKAG-GAYVPLDPDYPSDriqfmledsaasvlltQT 1402
Cdd:cd05908    17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLY---LFWACLlGGMIAVPVSIGSN----------------EE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1403 HLQERAQQWGQTLQAVLCLDDEaayaedasnVANVNePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQf 1482
Cdd:cd05908    78 HKLKLNKVWNTLKNPYLITEEE---------VLCEL-ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKT- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1483 PVRLLQLASFSFDVfvGDIA---RTLYNGGTMVICPKDDRI-DPARLHYWISEEKITIFeSTP----ALIIPFMDYVAEH 1554
Cdd:cd05908   147 KDRILSWMPLTHDM--GLIAfhlAPLIAGMNQYLMPTRLFIrRPILWLKKASEHKATIV-SSPnfgyKYFLKTLKPEKAN 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1555 GLDMSSMELLITSSDSCSVTDYRVLQERFgSQFR-----IINAYGVTEAAIDSSL--YDEPLaKLPEAGN---------- 1617
Cdd:cd05908   224 DWDLSSIRMILNGAEPIDYELCHEFLDHM-SKYGlkrnaILPVYGLAEASVGASLpkAQSPF-KTITLGRrhvthgepep 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1618 ------------VPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVegerlyRTGD 1685
Cdd:cd05908   302 evdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGD 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1686 LArWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVV----REDAKGQKVLCAYFTAESELKLSELRS 1761
Cdd:cd05908   376 LG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvnNSNTRNEEIFCFIEHRKSEDDFYPLGK 454
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 1762 SLSQEL---PGYMIpSYFVQLEQLPLTANGKIDR 1792
Cdd:cd05908   455 KIKKHLnkrGGWQI-NEVLPIRRIPKTTSGKVKR 487
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
3864-4334 1.19e-10

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 68.64  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3864 ALRNPDAVAVVFEK-----SQLTYGELNERANRLARTLRDAGvrPDQLVGLMVERSLEMVVGIMAIMKAGGAyIPIDPey 3938
Cdd:PRK05851   11 AMTASGRDLVVLDResglwRRHPWPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAA-VSILP-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 peDRIRYMLEDSGAQALLTQ-------------RHLrERVSFAGTFVAV-DDEQAYHADGSNLEPVVGPNHLAYVIYTSG 4004
Cdd:PRK05851   86 --GPVRGADDGRWADATLTRfagigvrtvlshgSHL-ERLRAVDSSVTVhDLATAAHTNRSASLTPPDSGGPAVLQGTAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4005 TTGKPKGVMVEHHG-LCSLKLMFANTLQMTEQDRVVQFASLSFDASCWEIFKALFFGATLYIPTSTTILDYPL-FESYMN 4082
Cdd:PRK05851  163 STGTPRTAILSPGAvLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFSASPFrWLSWLS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4083 ENGITATILPP-------TYAAYLNPDRMPSLKKLITGGSAASVEFVQQWKDKVLYFN--------AYGPTEASIVTSI- 4146
Cdd:PRK05851  243 DSRATLTAAPNfaynligKYARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFGfdagaaapSYGLAESTCAVTVp 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4147 -------WDEASDSLGD--RKSVPIGRPLANHRIYVVDSHNrmlPVGVA----GELCISGVGLARGYLNrpeltaekfvD 4213
Cdd:PRK05851  323 vpgiglrVDEVTTDDGSgaRRHAVLGNPIPGMEVRISPGDG---AAGVAgreiGEIEIRGASMMSGYLG----------Q 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4214 NPFEPGErMYRTGDLvRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLA--REDANGQQQLV--AY 4289
Cdd:PRK05851  390 APIDPDD-WFPTGDL-GYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvgTGEGSARPGLViaAE 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 4290 FVAQRELTAaelRATMSQELPNY--MIPSYFVQLA--QMPLTPNGKIDR 4334
Cdd:PRK05851  468 FRGPDEAGA---RSEVVQRVASEcgVVPSDVVFVApgSLPRTSSGKLRR 513
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
4908-5308 1.46e-10

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 68.47  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4908 YENDRLTYRELNERANRLARTLRAQ-GVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAAS 4986
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4987 VLLTQTHLQERAQQWGQTLQA----------------ALCLDDEAAYAED----ASNVANVNePHDLAYVIYTSGTTGRP 5046
Cdd:cd05938    81 VLVVAPELQEAVEEVLPALRAdgvsvwylshtsntegVISLLDKVDAASDepvpASLRAHVT-IKSPALYIYTSGTTGLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5047 KGVMIEHRSLVNTAA-----GYRREyrlDQFPVRL-LQLASFSFDVFVGDIARtlynGGTMVICPK-------DDridpA 5113
Cdd:cd05938   160 KAARISHLRVLQCSGflslcGVTAD---DVIYITLpLYHSSGFLLGIGGCIEL----GATCVLKPKfsasqfwDD----C 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5114 RLHywiseeKITIFEstpaliipfmdYVAEhgldmsSMVLLITSSDSCSVTDYRV---------------LQERFGsQFR 5178
Cdd:cd05938   229 RKH------NVTVIQ-----------YIGE------LLRYLCNQPQSPNDRDHKVrlaignglradvwreFLRRFG-PIR 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5179 IINAYGVTEAAIDSSLYdeplaklpeAGNV-PIGKA-ALNAKFY--------------IVDA--HLNPVPVGVLGELcig 5240
Cdd:cd05938   285 IREFYGSTEGNIGFFNY---------TGKIgAVGRVsYLYKLLFpfelikfdvekeepVRDAqgFCIPVAKGEPGLL--- 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 5241 gigVAR--------GYLNRPELTEEKFVDSPFVEGERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIE 5308
Cdd:cd05938   353 ---VAKitqqspflGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVA 425
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
1439-1797 1.61e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 68.30  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1439 EPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpKDD 1518
Cdd:PRK06334  181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVF--AYN 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1519 RIDPARLHYWISEEKITIFESTPAliipFMDYV----AEHGLDMSSMELLITSSDSCSVTDYRVLQERFgSQFRIINAYG 1594
Cdd:PRK06334  259 PLYPKKIVEMIDEAKVTFLGSTPV----FFDYIlktaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTF-PHIQLRQGYG 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1595 VTEAAIDSSLYDEPLAKLPEAGNVPIgkAALNAKFYIVDAHLnPVPVGVLGELCIGGIGVARGYLnrpeltEEKFVDSpF 1674
Cdd:PRK06334  334 TTECSPVITINTVNSPKHESCVGMPI--RGMDVLIVSEETKV-PVSSGETGLVLTRGTSLFSGYL------GEDFGQG-F 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1675 VE--GERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRE---DAKGQKV-LCAYF 1748
Cdd:PRK06334  404 VElgGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADHAGPLvvcGLPGEKVrLCLFT 483
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 1749 TAESElkLSELRSSL-SQELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 1797
Cdd:PRK06334  484 TFPTS--ISEVNDILkNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
7473-7869 1.68e-10

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 68.22  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7473 TYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQVLLTQRh 7552
Cdd:cd17641    13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7553 lQECVS--------------------------FDGKVIAADDEQAYGEDGSNLEPVVG--------PNHLAYVIYTSGTT 7598
Cdd:cd17641    92 -EEQVDklleiadripsvryviycdprgmrkyDDPRLISFEDVVALGRALDRRDPGLYerevaagkGEDVAVLCTTSGTT 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7599 GKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLSfdascW---EIF---KALFFGATLYIPAKDT---------- 7662
Cdd:cd17641   171 GKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLP-----WigeQMYsvgQALVCGFIVNFPEEPEtmmedlreig 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7663 ---------------------ILDYPLFESYMNENGITAAI----------LPPT---------YAIYLSP--DRL--PS 7698
Cdd:cd17641   246 ptfvllpprvwegiaadvrarMMDATPFKRFMFELGMKLGLraldrgkrgrPVSLwlrlaswlaDALLFRPlrDRLgfSR 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7699 LKKLITGGSAASvefvqqwKDKVRYFNA--------YGPTEASIVTSVwaaSPDGlDLRSVPIGRPIANHQIFIVDsqnh 7770
Cdd:cd17641   326 LRSAATGGAALG-------PDTFRFFHAigvplkqlYGQTELAGAYTV---HRDG-DVDPDTVGVPFPGTEVRIDE---- 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7771 mlpvgvAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGRI-DHQVKIRGYRIELGE 7849
Cdd:cd17641   391 ------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQF 458
                         490       500
                  ....*....|....*....|
gi 386647928 7850 IEEQLLKIASVQETIVIARG 7869
Cdd:cd17641   459 IENKLKFSPYIAEAVVLGAG 478
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
4914-5065 1.72e-10

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 68.22  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4914 TYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQTH 4993
Cdd:cd17641    13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4994 LQ---------------------ERA-----QQWGQTLQAALCLDDEAAYAEDASNVANVNE--PHDLAYVIYTSGTTGR 5045
Cdd:cd17641    93 EQvdklleiadripsvryviycdPRGmrkydDPRLISFEDVVALGRALDRRDPGLYEREVAAgkGEDVAVLCTTSGTTGK 172
                         170       180
                  ....*....|....*....|
gi 386647928 5046 PKGVMIEHRSLVNTAAGYRR 5065
Cdd:cd17641   173 PKLAMLSHGNFLGHCAAYLA 192
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
2365-2825 1.84e-10

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 67.90  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2365 VFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDpeYpedRISymLEDSSAQ 2444
Cdd:PLN02860   27 ISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN--Y---RWS--FEEAKSA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2445 VLLAQ--------------RRLQ------------------ERVSFAGTVVTVDDEQAYAGDGSNLESAVGPNDLAYIIY 2492
Cdd:PLN02860  100 MLLVRpvmlvtdetcsswyEELQndrlpslmwqvflespssSVFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVLICF 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2493 TSGTTGKPKGVMVEHHGLcsLKQMFANTLQI--NAQDRVVQFASLSFDASCWEVFQTLFFGAT-LYIPTKETILDYQwfe 2569
Cdd:PLN02860  180 TSGTTGRPKGVTISHSAL--IVQSLAKIAIVgyGEDDVYLHTAPLCHIGGLSSALAMLMVGAChVLLPKFDAKAALQ--- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2570 rYMSDNGITT-ATLPPTYAVYLNPDHM-------PDFKRLIAAGSASSLELLQQWKD---KVKYFNAYGPTEdsICT--- 2635
Cdd:PLN02860  255 -AIKQHNVTSmITVPAMMADLISLTRKsmtwkvfPSVRKILNGGGSLSSRLLPDAKKlfpNAKLFSAYGMTE--ACSslt 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2636 --TIWTPSTEDISQ-LKSVPIGGPIVNHriyivdaHYQPVPVGVAG---ELCIA-------GVGLARGylnrPDLTAEKF 2702
Cdd:PLN02860  332 fmTLHDPTLESPKQtLQTVNQTKSSSVH-------QPQGVCVGKPAphvELKIGldessrvGRILTRG----PHVMLGYW 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2703 VDNPFEPGERM----YRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIA----------- 2767
Cdd:PLN02860  401 GQNSETASVLSndgwLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGvpdsrltemvv 480
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2768 ---------------HDDASGQKQLCAYFVADRTMTVGelrgelsgeLPGYMIPAHFVQLER-MPLTPNGKIDR 2825
Cdd:PLN02860  481 acvrlrdgwiwsdneKENAKKNLTLSSETLRHHCREKN---------LSRFKIPKLFVQWRKpFPLTTTGKIRR 545
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
7583-7925 2.06e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 68.23  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7583 VGPNHLAYVIYTSGTTGKPKGVmVEHHGLCSLKLMFAETLRITEEDRVVQFASLSFDascWEIFKALFFGATLY------ 7656
Cdd:PTZ00237  251 VESSHPLYILYTSGTTGNSKAV-VRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIG---WVSFHGFLYGSLSLgntfvm 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7657 ----IPAKDTILDYpLFESYMNENGITAAILPPT--YAIYLSPD--------RLPSLKKLITGGSA--ASV-EFVQQwKD 7719
Cdd:PTZ00237  327 feggIIKNKHIEDD-LWNTIEKHKVTHTLTLPKTirYLIKTDPEatiirskyDLSNLKEIWCGGEVieESIpEYIEN-KL 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7720 KVRYFNAYGPTEASIvTSVWAASPDGLDLRSVPIGRPIANHQIFIVDSQNhmLPVGVAGELCIS---GAGLARGYLNRPE 7796
Cdd:PTZ00237  405 KIKSSRGYGQTEIGI-TYLYCYGHINIPYNATGVPSIFIKPSILSEDGKE--LNVNEIGEVAFKlpmPPSFATTFYKNDE 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7797 LTAEKFVDNPflageRMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQ 7876
Cdd:PTZ00237  482 KFKQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNV 556
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7877 LCAYFVADRELTVS---------ELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKIDR 7925
Cdd:PTZ00237  557 PIGLLVLKQDQSNQsidlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
5930-6419 2.23e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 67.83  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5930 KYPSDKTIHQLFEEQAERIPDHLAVTFED---------KQLTYGELNERANRLARTLRNAGvQPDQMVGLMVERSLEMVV 6000
Cdd:PRK07769   16 RFPPNTNLVRHVERWAKVRGDKLAYRFLDfsterdgvaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6001 GMIAILKAGGAYVPI-DPDYP--EDRIRYMLEDSGAKLLLVQGHLLD--RASFADKLVN-----LNDDGAYHEDGSNLEP 6070
Cdd:PRK07769   95 AFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEgvRKFFRARPAKerprvIAVDAVPDEVGATWVP 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6071 VNgPEHLT--YVIYTSGTTGRPKGVMVEHRNV-VRLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLyvvr 6147
Cdd:PRK07769  175 PE-ANEDTiaYLQYTSGSTRIPAGVQITHLNLpTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYI---- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6148 neTILDAVSLknaIQQYGintMWLtaplyNQLSQQDSGM---------FA-------GL-------------KTLIVGGD 6198
Cdd:PRK07769  250 --TFMSPAAF---VRRPG---RWI-----RELARKPGGTggtfsaapnFAfehaaarGLpkdgeppldlsnvKGLLNGSE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6199 VLSVPHINRVLREHA--GL---SIVNGYGPTENTTF-STT------------------HTIV---GEQKEAVP---IGKP 6248
Cdd:PRK07769  317 PVSPASMRKFNEAFApyGLpptAIKPSYGMAEATLFvSTTpmdeeptviyvdrdelnaGRFVevpADAPNAVAqvsAGKV 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6249 INNSTAYIVD-SKLSLLPVGVWGELIVGGDGVARGYLNRPELTAEKF-------VESSFLPG----ERCYRTGDLARWLp 6316
Cdd:PRK07769  397 GVSEWAVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrLSESHAEGapddALWVRTGDYGVYF- 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6317 DGTLEYKGRIDEQVKIRGYRIELGEIEeqllkvASVKEATVIVR------------------------------EDESgq 6366
Cdd:PRK07769  476 DGELYITGRVKDLVIIDGRNHYPQDLE------YTAQEATKALRtgyvaafsvpanqlpqvvfddshaglkfdpEDTS-- 547
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6367 KQLCayFVAER---------ELTIGELRAALSQelpnymipSH--------FVPLERMPLTPNGKIDRRA 6419
Cdd:PRK07769  548 EQLV--IVAERapgahkldpQPIADDIRAAIAV--------RHgvtvrdvlLVPAGSIPRTSSGKIARRA 607
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6554-6832 2.23e-10

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 67.34  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6554 DEAALRQVLQKLAEHHDALRTVFrKSENGYAAwnRAIGEGELYSLEVADFRDVKSAE--QAVEAKANEiqsSIDLEVGPL 6631
Cdd:cd20484    37 DVEKFKQACQFVLEQHPILKSVI-EEEDGVPF--QKIEPSKPLSFQEEDISSLKESEiiAYLREKAKE---PFVLENGPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6632 FKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEEVRL---PAKTDSFRTWSEQLAAYAQSpamENE 6707
Cdd:cd20484   111 MRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLassPASYYDFVAWEQDMLAGAEG---EEH 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6708 RAYW-EQIAQT-AVAPLPKD--KQSDRSLQQDSESITIqwsrkeTEQLLKKVH---RAYNTEMNDILLTALGMAVQKWSG 6780
Cdd:cd20484   188 RAYWkQQLSGTlPILELPADrpRSSAPSFEGQTYTRRL------PSELSNQIKsfaRSQSINLSTVFLGIFKLLLHRYTG 261
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 6781 LDRLLVNLEGHGR-----ESImtdiditrtVGWFTSKYPVLLQMEPGRSLSTRIKKV 6832
Cdd:cd20484   262 QEDIIVGMPTMGRpeerfDSL---------IGYFINMLPIRSRILGEETFSDFIRKL 309
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
2962-3121 2.30e-10

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 67.06  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2962 DEAAIRKVLQKLVEHHDALRVVFHKSENGYTAWNRAIGEGELyGLEVVDLkgieESAQAVEAKANEIQSSIDLEAGPFVK 3041
Cdd:cd19540    37 DVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARP-DLTVVDV----TEDELAARLAEAARRGFDLTAELPLR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3042 AGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEElrfPAktdayrtWSE---QLAAYA---------- 3107
Cdd:cd19540   112 ARLFRLGPDEHvLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA---PD-------WAPlpvQYADYAlwqrellgde 181
                         170
                  ....*....|....*.
gi 386647928 3108 --QSPVIERELAYWKR 3121
Cdd:cd19540   182 ddPDSLAARQLAYWRE 197
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
7460-7923 2.53e-10

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 67.68  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7460 PEKAAVVF----ENTQLTYRELNERANRLARTLRAEGVQA-DQPVGLMiERSLEMIVGAFAIMKAGGAYVPIDPEY---- 7530
Cdd:cd05943    83 DDPAAIYAaedgERTEVTWAELRRRVARLAAALRALGVKPgDRVAGYL-PNIPEAVVAMLATASIGAIWSSCSPDFgvpg 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7531 ---------PE-----DRIRY--MLEDSGAQVLLTQRHL----------------QECVSFDGKVIAADDEQAYGEDGSn 7578
Cdd:cd05943   162 vldrfgqiePKvlfavDAYTYngKRHDVREKVAELVKGLpsllavvvvpytvaagQPDLSKIAKALTLEDFLATGAAGE- 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7579 LEPV-VGPNHLAYVIYTSGTTGKPK-------GVMVEH---HGLCSlklmfaetlRITEEDRVVQFASLSFDASCWEIfK 7647
Cdd:cd05943   241 LEFEpLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHlkeHILHC---------DLRPGDRLFYYTTCGWMMWNWLV-S 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7648 ALFFGAT--LY-----IPAKDTILDYplfesyMNENGIT-----AAILPPTYAIYLSPDR---LPSLKKLITGGSAASVE 7712
Cdd:cd05943   311 GLAVGATivLYdgspfYPDTNALWDL------ADEEGITvfgtsAKYLDALEKAGLKPAEthdLSSLRTILSTGSPLKPE 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7713 ----FVQQWKDKVRYFNAYGPTE-------ASIVTSVWA----ASPDGLDLRSV-PIGRPIanhqifivdsqnhmlpVGV 7776
Cdd:cd05943   385 sfdyVYDHIKPDVLLASISGGTDiiscfvgGNPLLPVYRgeiqCRGLGMAVEAFdEEGKPV----------------WGE 448
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7777 AGELCISGAGLAR--GYLNRPEltAEKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQL 7854
Cdd:cd05943   449 KGELVCTKPFPSMpvGFWNDPD--GSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVV 526
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 7855 LKIASVQETIVIARGDANGQQQLcAYFVADR---ELT---VSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGKI 7923
Cdd:cd05943   527 EKIPEVEDSLVVGQEWKDGDERV-ILFVKLRegvELDdelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
6540-6836 2.92e-10

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 66.95  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6540 HFNQAfMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGYA-AWNRAIGEGELYSLEVADFRDVKSAEQAVEAKAN 6618
Cdd:cd19547    24 YFNQN-VLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPlQYVRDDLAPPWALLDWSGEDPDRRAELLERLLAD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6619 EIQSSIDLEVGPLFKAGLFQCADGDHLLLVIHHGVV-DGVSWRILLEDVALGYEQAAKGEEVRL-PAKtdSFRTWSEQLA 6696
Cdd:cd19547   103 DRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILlDGWCLSLIWGDVFRVYEELAHGREPQLsPCR--PYRDYVRWIR 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6697 AYAqSPAMENERAYWEQIAQTAVAPL---PKDKQS--DRSLQQDSESITiqwsrketeQLLKKVHRAYNTEMNDILLTAL 6771
Cdd:cd19547   181 ART-AQSEESERFWREYLRDLTPSPFstaPADREGefDTVVHEFPEQLT---------RLVNEAARGYGVTTNAISQAAW 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6772 GMAVQKWSGLDRLLVNLEGHGRESIMTDIDItrTVGWFTSKYPVLLQMEPGRSLSTRIKKVKEDL 6836
Cdd:cd19547   251 SMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
PLN03102 PLN03102
acyl-activating enzyme; Provisional
2355-2828 2.99e-10

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 67.35  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRI 2434
Cdd:PLN03102   24 SECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 SYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAY---------------AGDGSNLESAV-----GPNDLAYII--- 2491
Cdd:PLN03102  104 AAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNlpvifiheidfpkrpSSEELDYECLIqrgepTPSLVARMFriq 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2492 ---------YTSGTTGKPKGVMVEHHG--LCSLKQMFANTLQINAqdrVVQFASLSFDASCWevfqTLFFGATLYIPTKE 2560
Cdd:PLN03102  184 dehdpislnYTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCP---VYLWTLPMFHCNGW----TFTWGTAARGGTSV 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2561 TILDYQWFERY--MSDNGITTATLPPTYAVYL------NPDHMPDFKRLIAAGSASSLELLQQWKD-KVKYFNAYGPTED 2631
Cdd:PLN03102  257 CMRHVTAPEIYknIEMHNVTHMCCVPTVFNILlkgnslDLSPRSGPVHVLTGGSPPPAALVKKVQRlGFQVMHAYGLTEA 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2632 S--ICTTIWTPSTEDISQLKSVPIGGP--IVNHRIYIVDAH----YQPVPVG--VAGELCIAGVGLARGYLNRPDLTAEK 2701
Cdd:PLN03102  337 TgpVLFCEWQDEWNRLPENQQMELKARqgVSILGLADVDVKnketQESVPRDgkTMGEIVIKGSSIMKGYLKNPKATSEA 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2702 FVDNpfepgerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYF 2781
Cdd:PLN03102  417 FKHG-------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2782 VADRTMTVGELR--------GEL----SGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PLN03102  490 VLEKGETTKEDRvdklvtreRDLieycRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
2369-2790 3.03e-10

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 67.45  E-value: 3.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2369 QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLA 2448
Cdd:cd17641    10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2449 QRR--------LQERVSFAGTVVTVDD--------------EQAYA----------GDGSNLESAVGPNDLAYIIYTSGT 2496
Cdd:cd17641    90 EDEeqvdklleIADRIPSVRYVIYCDPrgmrkyddprlisfEDVVAlgraldrrdpGLYEREVAAGKGEDVAVLCTTSGT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2497 TGKPKGVMVEHHGLCSlkqMFANTLQINAQ---DRVVQFASLSfdascW------EVFQTLFFGATLYIPTKET------ 2561
Cdd:cd17641   170 TGKPKLAMLSHGNFLG---HCAAYLAADPLgpgDEYVSVLPLP-----WigeqmySVGQALVCGFIVNFPEEPEtmmedl 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2562 -------------------------ILDYQWFERYMSDNGITTA----------TLPPT---------YAVYLNP--DHM 2595
Cdd:cd17641   242 reigptfvllpprvwegiaadvrarMMDATPFKRFMFELGMKLGlraldrgkrgRPVSLwlrlaswlaDALLFRPlrDRL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2596 pDFKRL-IAAGSASSLEllqqwKDKVKYFNA--------YGPTEDSICTTIwtpstEDISQLKSVPIGGPIVNHRIYIVD 2666
Cdd:cd17641   322 -GFSRLrSAATGGAALG-----PDTFRFFHAigvplkqlYGQTELAGAYTV-----HRDGDVDPDTVGVPFPGTEVRIDE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2667 ahyqpvpvgvAGELCIAGVGLARGYLNRPDLTAEKFVDNPFepgermYRTGDLAKWLPDGTIEYLGRI-DHQVKIRGYRI 2745
Cdd:cd17641   391 ----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRF 454
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 2746 ELGEIEEQLLKVASVQEAIVIAHDdasgqKQLCAYFVADRTMTVG 2790
Cdd:cd17641   455 SPQFIENKLKFSPYIAEAVVLGAG-----RPYLTAFICIDYAIVG 494
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
6552-6678 3.10e-10

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 66.68  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6552 RFDEAALRQVLQKLAEHHDALRTVFRKSENGYAAWNRAIGEGELySLEVadfRDVkSAEQAVEAKANEIQSSIDLEVGPL 6631
Cdd:cd19540    35 ALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARP-DLTV---VDV-TEDELAARLAEAARRGFDLTAELP 109
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 6632 FKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQAAKGEE 6678
Cdd:cd19540   110 LRARLFRLGPDEHvLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA 157
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
6341-6414 3.20e-10

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 59.87  E-value: 3.20e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  6341 EIEEQLLKVASVKEATVIVREDESGQKQLCAYFV--AERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGK 6414
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK07867 PRK07867
acyl-CoA synthetase; Validated
259-749 3.21e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 67.01  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  259 DTTIHRLFEEQAErrPDAVAVTFEDRQLTYGELNERANRLARTLRN-AGVQADQLVGLMVERSLEMIVGIMGILKAGGAY 337
Cdd:PRK07867    4 APTVAELLLPLAE--DDDRGLYFEDSFTSWREHIRGSAARAAALRArLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  338 VPIDPEYPEERIRYMLEDSGTQVLLSQGHLQERVSFSGTWIRL--------DDEEAYHEDGSNLESVNGPEHLTYVIYTS 409
Cdd:PRK07867   82 VGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVinvdspawADELAAHRDAEPPFRVADPDDLFMLIFTS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  410 GTTGKPKGNLTTHRNI----IRVVKNTNYidvtGQDKLLQLSSYSFDGSTFdIFG---ALLNGAKLVLVPKetvldvakl 482
Cdd:PRK07867  162 GTSGDPKAVRCTHRKVasagVMLAQRFGL----GPDDVCYVSMPLFHSNAV-MAGwavALAAGASIALRRK--------- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  483 agliekqqisvmFITTAFFnvlvdmnPDCLRharailFGGerVSVSHVRKALGHL-----GPGK----IKHVYG----PT 549
Cdd:PRK07867  228 ------------FSASGFL-------PDVRR------YGA--TYANYVGKPLSYVlatpeRPDDadnpLRIVYGnegaPG 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  550 ESTVFATSYDVHEVE-----EGAVSI---------PIGGPISNTAIY-----------IVNAQNKLQPIGVAGELC-VAG 603
Cdd:PRK07867  281 DIARFARRFGCVVVDgfgstEGGVAItrtpdtppgALGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAG 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  604 DGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKAT 683
Cdd:PRK07867  361 PGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVA 433
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  684 VV-VRESANGEKQLCAYYVAD-RSLPANEVRSTLSQ--ELPAYMLPSYFVQLEQMPLTTNGKVDRRALPA 749
Cdd:PRK07867  434 VYaVPDPVVGDQVMAALVLAPgAKFDPDAFAEFLAAqpDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
4878-5385 3.39e-10

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 67.35  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4878 PAAPDAPENEAFHALFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAV 4957
Cdd:PRK07059   14 PAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4958 WKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTqthLQERAQqwgqTLQAAL---------------------------- 5009
Cdd:PRK07059   94 LRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVV---LENFAT----TVQQVLaktavkhvvvasmgdllgfkghivnfvv 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5010 --------------CLDDEAAYAEDAS---NVANVNePHDLAYVIYTSGTTGRPKGVMIEHRSLV-NTA-------AGYR 5064
Cdd:PRK07059  167 rrvkkmvpawslpgHVRFNDALAEGARqtfKPVKLG-PDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLqmeawlqPAFE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5065 REYRLDQFpvrllqlasfsfdVFVgdIARTLYN--------------GGTMVICPkddriDPARLHYWISE---EKITIF 5127
Cdd:PRK07059  246 KKPRPDQL-------------NFV--CALPLYHifaltvcgllgmrtGGRNILIP-----NPRDIPGFIKElkkYQVHIF 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5128 ESTPALIIPFMDYVAEHGLDMSSmvLLITSSDSCSVTdyRVLQERFGSQFR--IINAYGVTEAAidSSLYDEPLAKLPEA 5205
Cdd:PRK07059  306 PAVNTLYNALLNNPDFDKLDFSK--LIVANGGGMAVQ--RPVAERWLEMTGcpITEGYGLSETS--PVATCNPVDATEFS 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5206 GNvpIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGDLARWMPDGNV 5285
Cdd:PRK07059  380 GT--IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYT 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5286 DFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAhFTAESELKLSE--LRSSLSQELPGYMIP 5363
Cdd:PRK07059  452 KIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKL-FVVKKDPALTEedVKAFCKERLTNYKRP 530
                         570       580
                  ....*....|....*....|..
gi 386647928 5364 SYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK07059  531 KFVEFRTELPKTNVGKILRREL 552
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
4914-5382 3.39e-10

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 67.13  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4914 TYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVgalAVWKAG-GAYVPLDPDYPSDriqfmledsaasvlltQT 4992
Cdd:cd05908    17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLY---LFWACLlGGMIAVPVSIGSN----------------EE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4993 HLQERAQQWgQTLQAALCLDDEAAYAEDasnvanvnePHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQf 5072
Cdd:cd05908    78 HKLKLNKVW-NTLKNPYLITEEEVLCEL---------ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKT- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5073 PVRLLQLASFSFDVfvGDIA---RTLYNGGTMVICPKDDRI-DPARLHYWISEEKITIFeSTP----ALIIPFMDYVAEH 5144
Cdd:cd05908   147 KDRILSWMPLTHDM--GLIAfhlAPLIAGMNQYLMPTRLFIrRPILWLKKASEHKATIV-SSPnfgyKYFLKTLKPEKAN 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5145 GLDMSSMVLLITSSDSCSVTDYRVLQERFgSQFR-----IINAYGVTEAAIDSSL--YDEPLaKLPEAGN---------- 5207
Cdd:cd05908   224 DWDLSSIRMILNGAEPIDYELCHEFLDHM-SKYGlkrnaILPVYGLAEASVGASLpkAQSPF-KTITLGRrhvthgepep 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5208 ------------VPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSPFVegerlyRTGD 5275
Cdd:cd05908   302 evdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGD 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5276 LArWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVV----REDAKGQKVLCAHFTAESELKLSELRS 5351
Cdd:cd05908   376 LG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvnNSNTRNEEIFCFIEHRKSEDDFYPLGK 454
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 5352 SLSQEL---PGYMIpSYFVQLEQLPLTANGKIDR 5382
Cdd:cd05908   455 KIKKHLnkrGGWQI-NEVLPIRRIPKTTSGKVKR 487
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
6442-6500 3.77e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 59.11  E-value: 3.77e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  6442 KALAAVWQAVLG--AERVGVTDHFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTLAQ 6500
Cdd:pfam00550    1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PRK08162 PRK08162
acyl-CoA synthetase; Validated
267-747 3.79e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 66.89  E-value: 3.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  267 EEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPE 346
Cdd:PRK08162   25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  347 ERIRYMLEDSGTQVLLSQGHLQERVS-----FSGTWIRL-DDEEAYHEDGSNLESVN-------GPEHLTYVI------- 406
Cdd:PRK08162  105 ASIAFMLRHGEAKVLIVDTEFAEVARealalLPGPKPLViDVDDPEYPGGRFIGALDyeaflasGDPDFAWTLpadewda 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  407 ----YTSGTTGKPKGNLTTHR--------NIIrvvkntnyidVTGQDK----LLQLSSYSFDGSTFDIFGALLNGAKLVL 470
Cdd:PRK08162  185 ialnYTSGTTGNPKGVVYHHRgaylnalsNIL----------AWGMPKhpvyLWTLPMFHCNGWCFPWTVAARAGTNVCL 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  471 --VPKETVLDvaklagLIEKQQISVMFITTAFFNVLVDMnPDCLRHARAilfggERVSV--------SHVRKALGHLGPg 540
Cdd:PRK08162  255 rkVDPKLIFD------LIREHGVTHYCGAPIVLSALINA-PAEWRAGID-----HPVHAmvagaappAAVIAKMEEIGF- 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  541 KIKHVYGPTE----STVFATSYDVHE--VEEGA-------VSIPiggpiSNTAIYIVNAQNkLQPIG----VAGELCVAG 603
Cdd:PRK08162  322 DLTHVYGLTEtygpATVCAWQPEWDAlpLDERAqlkarqgVRYP-----LQEGVTVLDPDT-MQPVPadgeTIGEIMFRG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  604 DGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKAT 683
Cdd:PRK08162  396 NIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAA 468
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928  684 VVVRESAN-GEKQlCAyYVADR---SLPANEVRSTLSQELPAYMLPSYFVqLEQMPLTTNGKVDRRAL 747
Cdd:PRK08162  469 VVAKPDPKwGEVP-CA-FVELKdgaSATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVL 533
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
7583-7930 4.03e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 66.76  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7583 VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASlSFDA---SCWEIF------------- 7646
Cdd:PRK06334  180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLP-PFHAygfNSCTLFpllsgvpvvfayn 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7647 --------------KALFFGATlyipakdtildyPLFESYMnengITAAilpptyaiYLSPDRLPSLKKLITGGSA---A 7709
Cdd:PRK06334  259 plypkkivemideaKVTFLGST------------PVFFDYI----LKTA--------KKQESCLPSLRFVVIGGDAfkdS 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7710 SVEFVQQWKDKVRYFNAYGPTEASIVTSVWAA-SPDgldlRSVPIGRPIANHQIFIVDSQNHM-LPVGVAGELCISGAGL 7787
Cdd:PRK06334  315 LYQEALKTFPHIQLRQGYGTTECSPVITINTVnSPK----HESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSL 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7788 ARGYLNRPEltAEKFVDnpfLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLK---IASVQETI 7864
Cdd:PRK06334  391 FSGYLGEDF--GQGFVE---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgQNAADHAG 465
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 7865 -VIARGDANGQQQLCAYFVAdrELTVSELRGTL-SQELPGYMIPSYFVQLEQMPLTPNGKIDRNALPA 7930
Cdd:PRK06334  466 pLVVCGLPGEKVRLCLFTTF--PTSISEVNDILkNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1307-1795 4.48e-10

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 66.63  E-value: 4.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1307 AERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDri 1386
Cdd:cd05929     2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRA-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 qfmlEDSAASVLLTQTHLQERAQQWGqtlqavlCLDDEAAYAE-----DASNVANVNEPHDLayvIYTSGTTGRPKGVM- 1460
Cdd:cd05929    80 ----EACAIIEIKAAALVCGLFTGGG-------ALDGLEDYEAaeggsPETPIEDEAAGWKM---LYSGGTTGRPKGIKr 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1461 --------IEHRSLVNTAAGYRREYRLdQFPVRLLQLASFSFdvfvgdIARTLYNGGTMVICPKddrIDPARLHYWISEE 1532
Cdd:cd05929   146 glpggppdNDTLMAAALGFGPGADSVY-LSPAPLYHAAPFRW------SMTALFMGGTLVLMEK---FDPEEFLRLIERY 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1533 KITIFESTPAL---IIPFMDYVaEHGLDMSSMELLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEA----AIDSSLY 1605
Cdd:cd05929   216 RVTFAQFVPTMfvrLLKLPEAV-RNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGP--IIWEYYGGTEGqgltIINGEEW 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1606 deplakLPEAGNVpiGKAALnAKFYIVDAHLNPVPVGVLGELCIGGiGVARGYLNRPELTEEKFvdspfveGERLYRT-G 1684
Cdd:cd05929   293 ------LTHPGSV--GRAVL-GKVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAAR-------NEGGWSTlG 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1685 DLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAYFTAES----ELKLSEL 1759
Cdd:cd05929   356 DVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEElGQRVHAVVQPAPGadagTALAEEL 435
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 1760 RSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05929   436 IAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
270-685 4.53e-10

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 66.43  E-value: 4.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERI 349
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  350 RYMLEDSGTQVLLSqghLQERVSFSG-TWIRLDDEEAYHEDGSNlesvngPEHLTYVIYTSGTTGKPKGNLTTHR----N 424
Cdd:PRK09029   93 EELLPSLTLDFALV---LEGENTFSAlTSLHLQLVEGAHAVAWQ------PQRLATMTLTSGSTGLPKAAVHTAQahlaS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  425 IIRVVkntNYIDVTGQDK-LLQLSSYSFDGSTFdIFGALLNGAKLVLVPKETvLDVAkLAGliekqqisvmfITTAffnV 503
Cdd:PRK09029  164 AEGVL---SLMPFTAQDSwLLSLPLFHVSGQGI-VWRWLYAGATLVVRDKQP-LEQA-LAG-----------CTHA---S 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  504 LV----------DMNPDCLRHaraILFGGERVSVSHVRKALGH-----LGpgkikhvYGPTE--STVFATSYDvheveeg 566
Cdd:PRK09029  224 LVptqlwrlldnRSEPLSLKA---VLLGGAAIPVELTEQAEQQgircwCG-------YGLTEmaSTVCAKRAD------- 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  567 avSIP-IGGPISNTAIYIVNaqnklqpigvaGELCVAGDGLARGYLNRPDLTaekfadnPFAPGERMYRTGDLARWLpDG 645
Cdd:PRK09029  287 --GLAgVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NG 345
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 386647928  646 TIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVV 685
Cdd:PRK09029  346 ELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV 385
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
270-417 4.54e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 66.64  E-value: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  270 AERRPD--AVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEE 347
Cdd:PRK13391    7 AQTTPDkpAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  348 RIRYMLEDSGTQVLLSQG--------------HLQERVSFSGT-----WIRLDDEEAYHEDGSNLESVNGpehlTYVIYT 408
Cdd:PRK13391   87 EAAYIVDDSGARALITSAakldvarallkqcpGVRHRLVLDGDgelegFVGYAEAVAGLPATPIADESLG----TDMLYS 162

                  ....*....
gi 386647928  409 SGTTGKPKG 417
Cdd:PRK13391  163 SGTTGRPKG 171
PLN02479 PLN02479
acetate-CoA ligase
596-754 4.74e-10

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 66.79  E-value: 4.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  596 AGELCVAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLK 675
Cdd:PLN02479  402 MGEIVMRGNMVMKGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYT 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  676 LEAIEKATVVVRESANGEKQLCAYYV-------ADRSLPANEVRSTLSQELPAYMLPSYFVqLEQMPLTTNGKVDRRALP 748
Cdd:PLN02479  475 HPAVLEASVVARPDERWGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVLR 553

                  ....*.
gi 386647928  749 APEESM 754
Cdd:PLN02479  554 AKAKEM 559
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
2369-2734 4.91e-10

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 66.61  E-value: 4.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2369 QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLA 2448
Cdd:cd05933     7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2449 Q--------RRLQERVSFAGTVVTVDDEQAYAGDG-------------------SNLESAVGPNDLAYIIYTSGTTGKPK 2501
Cdd:cd05933    87 EnqkqlqkiLQIQDKLPHLKAIIQYKEPLKEKEPNlyswdefmelgrsipdeqlDAIISSQKPNQCCTLIYTSGTTGMPK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2502 GVMVEHHGLCSLKQMFANTLQINA----QDRVVQFASLSF-DASCWEVFQTLFFGATLYIPTKE----TILD-------- 2564
Cdd:cd05933   167 GVMLSHDNITWTAKAASQHMDLRPatvgQESVVSYLPLSHiAAQILDIWLPIKVGGQVYFAQPDalkgTLVKtlrevrpt 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2565 --------YQWFERYMSDNGITTATLPPTYAVY-------------LNPDHMPDFKRL---------------------I 2602
Cdd:cd05933   247 afmgvprvWEKIQEKMKAVGAKSGTLKRKIASWakgvgletnlklmGGESPSPLFYRLakklvfkkvrkalgldrcqkfF 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2603 AAGSASSLELLQQWKD-KVKYFNAYGPTEDSICTTIwtpSTEDISQLKSVPIGGPIVNHRIYIVDAHYQpvpvgvaGELC 2681
Cdd:cd05933   327 TGAAPISRETLEFFLSlNIPIMELYGMSETSGPHTI---SNPQAYRLLSCGKALPGCKTKIHNPDADGI-------GEIC 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 2682 IAGVGLARGYLNRPDLTAEKfVDNpfepgERMYRTGDLAKWLPDGTIEYLGRI 2734
Cdd:cd05933   397 FWGRHVFMGYLNMEDKTEEA-IDE-----DGWLHSGDLGKLDEDGFLYITGRI 443
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2850-2908 5.05e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 58.73  E-value: 5.05e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  2850 KVLADVWQAVLG--AERVGATDHFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTVAQ 2908
Cdd:pfam00550    1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
3993-4333 5.17e-10

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 67.04  E-value: 5.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3993 PNHLAYVIYTSGTTGKPKGVMVEHHGLcslklmFANTLQM------TEQDRVVqfaslsfdaSCWEIFKAlfFGAT--LY 4064
Cdd:PRK08043  364 PEDAALILFTSGSEGHPKGVVHSHKSL------LANVEQIktiadfTPNDRFM---------SALPLFHS--FGLTvgLF 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4065 IP--TSTTILDYP-------LFESYMNENGI----TATILpPTYAAYLNPDRMPSLKKLITGGSAASVEFVQQWKDK--V 4129
Cdd:PRK08043  427 TPllTGAEVFLYPsplhyriVPELVYDRNCTvlfgTSTFL-GNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKfgL 505
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4130 LYFNAYGPTEASIVTSIwdeasdslgdrkSVP-------IGRPLANhriyvVDShnRMLPV-GVA--GELCISGVGLARG 4199
Cdd:PRK08043  506 RILEGYGVTECAPVVSI------------NVPmaakpgtVGRILPG-----MDA--RLLSVpGIEqgGRLQLKGPNIMNG 566
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4200 YL--NRP---ELTAEKFVDNPFEPGerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVEtQLA-KIDAVQEAI 4273
Cdd:PRK08043  567 YLrvEKPgvlEVPTAENARGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE-QLAlGVSPDKQHA 643
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 4274 VLAREDANGQQQLVaYFVAQRELTAAEL-RATMSQELPNYMIPSYFVQLAQMPLTPNGKID 4333
Cdd:PRK08043  644 TAIKSDASKGEALV-LFTTDSELTREKLqQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
4258-4331 5.85e-10

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 59.10  E-value: 5.85e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  4258 EVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV--AQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGK 4331
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
5029-5387 6.30e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 66.38  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5029 EPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVIcpKDD 5108
Cdd:PRK06334  181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVF--AYN 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5109 RIDPARLHYWISEEKITIFESTPAliipFMDYV----AEHGLDMSSMVLLITSSDSCSVTDYRVLQERFgSQFRIINAYG 5184
Cdd:PRK06334  259 PLYPKKIVEMIDEAKVTFLGSTPV----FFDYIlktaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTF-PHIQLRQGYG 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5185 VTEAAIDSSLYDEPLAKLPEAGNVPIgkAALNAKFYIVDAHLnPVPVGVLGELCIGGIGVARGYLnrpeltEEKFVDSpF 5264
Cdd:PRK06334  334 TTECSPVITINTVNSPKHESCVGMPI--RGMDVLIVSEETKV-PVSSGETGLVLTRGTSLFSGYL------GEDFGQG-F 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5265 VE--GERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRE---DAKGQKVLCAHFT 5339
Cdd:PRK06334  404 VElgGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADHAGPLvvcGLPGEKVRLCLFT 483
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 5340 AESElKLSELRSSL-SQELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 5387
Cdd:PRK06334  484 TFPT-SISEVNDILkNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
6527-6742 6.33e-10

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 65.74  E-value: 6.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6527 QR--WFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFrkSENGyaawnrAIGEGEL-----YSLE 6599
Cdd:cd20483     8 QRrlWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAY--FEGD------DFGEQQVlddpsFHLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6600 VADFRDVKSAEQAVEAKANEIQSS-IDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQ-AAKG 6676
Cdd:cd20483    80 VIDLSEAADPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFaLVLASHHIAWDRGSSKSIFEQFTALYDAlRAGR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 6677 EEVRLPAKTDS---FRTWSEQLaayAQSPAMENERAYWEQI---AQTAVAPLPKDKqSDRSLQQDSESITIQ 6742
Cdd:cd20483   160 DLATVPPPPVQyidFTLWHNAL---LQSPLVQPLLDFWKEKlegIPDASKLLPFAK-AERPPVKDYERSTVE 227
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
258-757 6.77e-10

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 66.34  E-value: 6.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  258 RDTTIHRLFEEQAErrpdavavtfedrQLTYGELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGA 336
Cdd:PRK05620   24 GDTTVTTWGGAEQE-------------QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  337 YVPIDPEYPEERIRYMLEDSGTQVLLSQGHLQER-------------VSFSGTwiRLDDEEAYHEDGS----NLES-VNG 398
Cdd:PRK05620   91 FNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQlgeilkecpcvraVVFIGP--SDADSAAAHMPEGikvySYEAlLDG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  399 ----------PEHLTYVI-YTSGTTGKPKGNLTTHRNII---RVVKNTNYIDVT-GQDKLLQLSSYSFDgSTFDIFGALL 463
Cdd:PRK05620  169 rstvydwpelDETTAAAIcYSTGTTGAPKGVVYSHRSLYlqsLSLRTTDSLAVThGESFLCCVPIYHVL-SWGVPLAAFM 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  464 NGAKLVLvPKETVlDVAKLAGLIEKQQISVMF-ITTAFFNVLVDM--NPDCLRHARAILFGGERVSVSHVRKALGHLGPG 540
Cdd:PRK05620  248 SGTPLVF-PGPDL-SAPTLAKIIATAMPRVAHgVPTLWIQLMVHYlkNPPERMSLQEIYVGGSAVPPILIKAWEERYGVD 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  541 KIkHVYGPTESTVFAT-----------SYDVHEVEEGAVSIPIGGPISNTAiYIVNAQNKLQpigvaGELCVAGDGLARG 609
Cdd:PRK05620  326 VV-HVWGMTETSPVGTvarppsgvsgeARWAYRVSQGRFPASLEYRIVNDG-QVMESTDRNE-----GEIQVRGNWVTAS 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  610 YLNRP----DLTAEKFADNPFAPGERMY------RTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAI 679
Cdd:PRK05620  399 YYHSPteegGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  680 EKATVV-VRESANGEKQLCAYYVADRSLP----ANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRR--------- 745
Cdd:PRK05620  479 VECAVIgYPDDKWGERPLAVTVLAPGIEPtretAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKdlrqhladg 558
                         570
                  ....*....|....*..
gi 386647928  746 -----ALPAPEESMETG 757
Cdd:PRK05620  559 dfeiiKLKGPGESGESD 575
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
4135-4338 7.11e-10

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 65.79  E-value: 7.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4135 YGPTE-ASIVTSIWDEasDSL-GDRKSvpiGRPLANHRIYVVDSHnrmlpvgvAGELCISGVGLARGYLnrPEltaekFV 4212
Cdd:PRK07445  261 YGMTEtASQIATLKPD--DFLaGNNSS---GQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQ-----IL 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4213 DNPfepgeRMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV- 4291
Cdd:PRK07445  321 DSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVp 395
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 4292 AQRELTAAELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKALP 4338
Cdd:PRK07445  396 KDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
6074-6346 7.25e-10

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 66.29  E-value: 7.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6074 PEHLTYVIYTSGTTGRPKGVMVEHRNVV-----------RLVKNTNYVELNEQTHILQTGA--VVFDASTFEIWGALLN- 6139
Cdd:PLN02387  249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVatvagvmtvvpKLGKNDVYLAYLPLAHILELAAesVMAAVGAAIGYGSPLTl 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6140 -----------GGRLYVVRNE------TILDAVS---LKNAIQQYG----------------INTMWLTA-----PLYNQ 6178
Cdd:PLN02387  329 tdtsnkikkgtKGDASALKPTlmtavpAILDRVRdgvRKKVDAKGGlakklfdiaykrrlaaIEGSWFGAwglekLLWDA 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6179 LS-QQDSGMFAG-LKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTEN---TTFST-THTIVGEqkeavpIGKPINNS 6252
Cdd:PLN02387  409 LVfKKIRAVLGGrIRFMLSGGAPLS-GDTQRFINICLGAPIGQGYGLTETcagATFSEwDDTSVGR------VGPPLPCC 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6253 taYIvdsKLSLLPVGVW---------GELIVGGDGVARGYLNRPELTAEKF-VESSflpGERCYRTGDLARWLPDGTLEY 6322
Cdd:PLN02387  482 --YV---KLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYkVDER---GMRWFYTGDIGQFHPDGCLEI 553
                         330       340
                  ....*....|....*....|....*
gi 386647928 6323 KGRIDEQVKIR-GYRIELGEIEEQL 6346
Cdd:PLN02387  554 IDRKKDIVKLQhGEYVSLGKVEAAL 578
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
2367-2763 8.94e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 65.91  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2367 EGQQLTYRELNERANRLARTLQALGVKTDQpVGLMLERSLEMVVGMFAVLKAGGAYVPI-DPEYP--EDRISYMLEDSSA 2443
Cdd:PRK07769   52 VARDLTWSQFGARNRAVGARLQQVTKPGDR-VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTP 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2444 QVLLAQRRLQERVS--FAGT-------VVTVD---DEQAyagdgsnlESAVGP----NDLAYIIYTSGTTGKPKGVMVEH 2507
Cdd:PRK07769  131 SAILTTTDSAEGVRkfFRARpakerprVIAVDavpDEVG--------ATWVPPeaneDTIAYLQYTSGSTRIPAGVQITH 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2508 HGLCS-LKQMFaNTLQINAQDRVVQFASLSFDASCWEVFQTLFFGA--TLYIPTKETILDYQWFeRYM---SDNGITTAT 2581
Cdd:PRK07769  203 LNLPTnVLQVI-DALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHyiTFMSPAAFVRRPGRWI-RELarkPGGTGGTFS 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2582 LPPTYAVylnpDH---------------MPDFKRLIAAG---SASSLEllqqwkdkvKYFNAYGP--------------T 2629
Cdd:PRK07769  281 AAPNFAF----EHaaarglpkdgeppldLSNVKGLLNGSepvSPASMR---------KFNEAFAPyglpptaikpsygmA 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2630 EDS--ICTTIWTPSTE----DISQLKS-----VPIGGP-----------IVNHRIYIVDAHY-QPVPVGVAGELCIAGVG 2686
Cdd:PRK07769  348 EATlfVSTTPMDEEPTviyvDRDELNAgrfveVPADAPnavaqvsagkvGVSEWAVIVDPETaSELPDGQIGEIWLHGNN 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2687 LARGYLNRPDLTAEKF---VDNPF--------EPGERMYRTGDLAKWLpDGTIEYLGRIDHQVKIRGYRIELGEIEeqll 2755
Cdd:PRK07769  428 IGTGYWGKPEETAATFqniLKSRLseshaegaPDDALWVRTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLE---- 502

                  ....*...
gi 386647928 2756 kvASVQEA 2763
Cdd:PRK07769  503 --YTAQEA 508
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
1322-1795 1.05e-09

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 65.54  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILA---DRSADLLVGALAVwkaGGAYVPLDP-----------DYPSDRIQ 1387
Cdd:PRK06018   39 RTTYAQIHDRALKVSQALDRDGIKLGDRVATIAwntWRHLEAWYGIMGI---GAICHTVNPrlfpeqiawiiNHAEDRVV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1388 F-------MLEDSAASVLLTQTH--LQERAQQWGQTLQAVLCLDDEAAYAEDASNVANVNEpHDLAYVIYTSGTTGRPKG 1458
Cdd:PRK06018  116 ItdltfvpILEKIADKLPSVERYvvLTDAAHMPQTTLKNAVAYEEWIAEADGDFAWKTFDE-NTAAGMCYTSGTTGDPKG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1459 VMIEHRS------LVNTAAGYRREYRLDQFPVRLLqlasfsFDVFVGDIARTLYNGGTMVICPkDDRIDPARLHYWISEE 1532
Cdd:PRK06018  195 VLYSHRSnvlhalMANNGDALGTSAADTMLPVVPL------FHANSWGIAFSAPSMGTKLVMP-GAKLDGASVYELLDTE 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1533 KITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQErFGSQfrIINAYGVTEAAIDSSL--YDEPLA 1610
Cdd:PRK06018  268 KVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFED-MGVE--VRHAWGMTEMSPLGTLaaLKPPFS 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1611 KLPEAGNVPI----GKAALNAKFYIVDAHLNPVPVG--VLGELCIGGIGVARGYLNrpelteekfVDSPFVEGERLYRTG 1684
Cdd:PRK06018  345 KLPGDARLDVlqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYR---------VDGEILDDDGFFDTG 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1685 DLArwmpdgNVDFIG--RIDNQAK--IR--GYRIETGEIETQllkAEGVREAVVVVredakgqkVLCAYFTAESE----- 1753
Cdd:PRK06018  416 DVA------TIDAYGymRITDRSKdvIKsgGEWISSIDLENL---AVGHPKVAEAA--------VIGVYHPKWDErplli 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 1754 LKLSELRSSLSQELPGYM--------IPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK06018  479 VQLKPGETATREEILKYMdgkiakwwMPDDVAFVDAIPHTATGKILKTAL 528
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1312-1795 1.16e-09

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 65.14  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1312 EVAAVV-----YENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 1386
Cdd:cd05915     9 GRKEVVsrlhtGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1387 QFMLEDSAASVLLTQTHLQERAQQWGQTLQAVLCLDDEAAYAEDASNVANVNEPH----------DLAYVIYTSGTTGRP 1456
Cdd:cd05915    89 AYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEeadpvrvperAACGMAYTTGTTGLP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1457 KGVMIEHRS--LVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGgtMVICPKDDRIDPARLHYwISEEKI 1534
Cdd:cd05915   169 KGVVYSHRAlvLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGA--KQVLPGPRLDPASLVEL-FDGEGV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1535 TIFESTPaliiPFMDYVA--EHGLDMSSMELLITSSDSCSVTDYRVLQERFGSqFRIINAYGVTE--AAIDSSLYDEPLA 1610
Cdd:cd05915   246 TFTAGVP----TVWLALAdyLESTGHRLKTLRRLVVGGSAAPRSLIARFERMG-VEVRQGYGLTEtsPVVVQNFVKSHLE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1611 KLPEAGNVPI-GKAALNAKFYIVDAhLNPVPVGV------LGELCIGGIGVARGYLNRPELTEEkfvdSPFVEGerLYRT 1683
Cdd:cd05915   321 SLSEEEKLTLkAKTGLPIPLVRLRV-ADEEGRPVpkdgkaLGEVQLKGPWITGGYYGNEEATRS----ALTPDG--FFRT 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1684 GDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFT-AESELKLSELRSS 1762
Cdd:cd05915   394 GDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVpRGEKPTPEELNEH 473
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 1763 LSQELPGY-MIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05915   474 LLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRAL 507
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
2360-2828 1.21e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 65.55  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2360 DHPAVVFEG------QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI----DPEY 2429
Cdd:PRK00174   82 DKVAIIWEGddpgdsRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEA 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2430 PEDRIsymlEDSSAQVLL---AQRR------LQERV----SFAGTVVTV--------------------DDEQAYAGDGS 2476
Cdd:PRK00174  162 LADRI----IDAGAKLVItadEGVRggkpipLKANVdealANCPSVEKVivvrrtggdvdwvegrdlwwHELVAGASDEC 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2477 NLEsAVGPNDLAYIIYTSGTTGKPKGV-------MVehhglcslkqmfantlqinaqdrvvqFASLS----FDAS----- 2540
Cdd:PRK00174  238 EPE-PMDAEDPLFILYTSGSTGKPKGVlhttggyLV--------------------------YAAMTmkyvFDYKdgdvy 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2541 -C-----W------EVFQTLFFGAT--LYiptkETILDY----QWF---ERYmsdnGIT---TAtlpPTyAVylnpdhmp 2596
Cdd:PRK00174  291 wCtadvgWvtghsyIVYGPLANGATtlMF----EGVPNYpdpgRFWeviDKH----KVTifyTA---PT-AI-------- 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2597 dfkR-LIAAGSA-------SSLELL-----------QQWkdkvkYFNAYGPTEDSICTTIWtpSTED----ISQLKSV-- 2651
Cdd:PRK00174  351 ---RaLMKEGDEhpkkydlSSLRLLgsvgepinpeaWEW-----YYKVVGGERCPIVDTWW--QTETggimITPLPGAtp 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2652 --------PIGGPIVNhriyIVDAHYQPVPVGVAGELCIAGV--GLARGYLNRPdltaEKFVDNPFEPGERMYRTGDLAK 2721
Cdd:PRK00174  421 lkpgsatrPLPGIQPA----VVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGAR 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2722 WLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVI-AHDDASGQkQLCAYFV--ADRTMT---VGELRGE 2795
Cdd:PRK00174  493 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVgRPDDIKGQ-GIYAFVTlkGGEEPSdelRKELRNW 571
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 386647928 2796 LSGELPGYMIPA--HFVqlERMPLTPNGKIDRKAL 2828
Cdd:PRK00174  572 VRKEIGPIAKPDviQFA--PGLPKTRSGKIMRRIL 604
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
5958-6417 1.48e-09

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 65.21  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5958 DKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDpdYpedriRYMLEDSGAKLLL 6037
Cdd:PLN02860   30 NRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN--Y-----RWSFEEAKSAMLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6038 VQGHLL-----------------------------DRASFADKLVN-LNDDGAYHEDG--SNLEPVNGPEHLTYVIYTSG 6085
Cdd:PLN02860  103 VRPVMLvtdetcsswyeelqndrlpslmwqvflesPSSSVFIFLNSfLTTEMLKQRALgtTELDYAWAPDDAVLICFTSG 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6086 TTGRPKGVMVEHRN-VVRLVKNTNYVELNEQTHILQTGAVVfdastfEIWG-----ALLNGGRLYVVRNEtiLDAVSLKN 6159
Cdd:PLN02860  183 TTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLC------HIGGlssalAMLMVGACHVLLPK--FDAKAALQ 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6160 AIQQYGINTMwLTAPL-------YNQLSQQDSGmFAGLKTLIVGGDVLSVPHINRVLREHAGLSIVNGYGPTE---NTTF 6229
Cdd:PLN02860  255 AIKQHNVTSM-ITVPAmmadlisLTRKSMTWKV-FPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacsSLTF 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6230 STTH------------------TIVGEQKEAVPIGKPinnstAYIVDSKLSLLPVGVWGELIVGGDGVARGYLNRPELTA 6291
Cdd:PLN02860  333 MTLHdptlespkqtlqtvnqtkSSSVHQPQGVCVGKP-----APHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6292 EKFVESSFLPgercyrTGDLArWLPD-GTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVI------------ 6358
Cdd:PLN02860  408 SVLSNDGWLD------TGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVgvpdsrltemvv 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6359 --VREDESGQKQLCAYFVAERELTIGE--LRAALS-QELPNYMIPSHFVPLER-MPLTPNGKIDR 6417
Cdd:PLN02860  481 acVRLRDGWIWSDNEKENAKKNLTLSSetLRHHCReKNLSRFKIPKLFVQWRKpFPLTTTGKIRR 545
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
1315-1797 2.03e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 64.66  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1315 AVVYENDRLTYRE-LNERANR--LARMLRAQGVKPNqlVGILADRSADLLVGALAVWKAGGAYVPLDP---------DYP 1382
Cdd:PRK13388   19 AVRYGDRTWTWREvLAEAAARaaALIALADPDRPLH--VGVLLGNTPEMLFWLAAAALGGYVLVGLNTtrrgaalaaDIR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLEDSAASVLLTqthlqeraqqwGQTLQAVLCLD-DEAAYAEdASNVANVNEPH------DLAYVIYTSGTTGR 1455
Cdd:PRK13388   97 RADCQLLVTDAEHRPLLD-----------GLDLPGVRVLDvDTPAYAE-LVAAAGALTPHrevdamDPFMLIFTSGTTGA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1456 PKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPK-------DDridparlhyw 1528
Cdd:PRK13388  165 PKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKfsasgflDD---------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1529 iseekITIFESTpaliipFMDYVAEH-GLDMSSME--------LLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEAA 1599
Cdd:PRK13388  235 -----VRRYGAT------YFNYVGKPlAYILATPErpddadnpLRVAFGNEASPRDIAEFSRRFGCQ--VEDGYGSSEGA 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1600 IdsSLYDEPLAklPEAGnvpIGKAALNAKfyIVDAH-LNPVPVGVL-------------GELC-IGGIGVARGYLNRPEL 1664
Cdd:PRK13388  302 V--IVVREPGT--PPGS---IGRGAPGVA--IYNPEtLTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPEA 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1665 TEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKV 1743
Cdd:PRK13388  373 TAERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERvGDQV 445
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 1744 LCAYFTAE-SELKLSELRSSLS--QELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 1797
Cdd:PRK13388  446 MAALVLRDgATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
6076-6417 2.05e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 64.76  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTYVIYTSGTTGRPKGVMVEH-RNVVRLVKNTNYVELNEQTHILQTGAVVFDASTFEIWGALLNGGRLYV------VRN 6148
Cdd:PTZ00237  255 HPLYILYTSGTTGNSKAVVRSNgPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVmfeggiIKN 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6149 ETILDavSLKNAIQQYGINTMWLTAPLYNQLSQQDSGM--------FAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNG 6220
Cdd:PTZ00237  335 KHIED--DLWNTIEKHKVTHTLTLPKTIRYLIKTDPEAtiirskydLSNLKEIWCGGEVIE-ESIPEYIENKLKIKSSRG 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6221 YGPTEN---TTFSTTHtivgeqkeavpIGKPIN---NSTAYIVDSKLS----LLPVGVWGELIVG---GDGVARGYLNRP 6287
Cdd:PTZ00237  412 YGQTEIgitYLYCYGH-----------INIPYNatgVPSIFIKPSILSedgkELNVNEIGEVAFKlpmPPSFATTFYKND 480
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6288 ELTAEKFveSSFlPGErcYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQK 6367
Cdd:PTZ00237  481 EKFKQLF--SKF-PGY--YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYN 555
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 6368 QLCAYFVAERELTI---------GELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDR 6417
Cdd:PTZ00237  556 VPIGLLVLKQDQSNqsidlnklkNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
5-210 2.15e-09

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 63.94  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    5 AFERETAFWNKIFEGEEnpPTALPYSK-AQKQAPALVRRMSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTS 83
Cdd:cd19539   187 RAAELLDFWRRRLRGAE--PTALPTDRpRPAGFPYPGADLRFELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTG 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   84 SSSILVGMPVVTKPN-ENRRPVN---QLVILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQYADGVP- 158
Cdd:cd19539   265 QTDIVVGTPVAGRNHpRFESTVGffvNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAELPVDRDAGRHp 344
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  159 -------VVNTL-------VALKQLHITDYRQSAVSDVLFEFELDKDEVRLHLTYNGNLYTESFIA 210
Cdd:cd19539   345 lvqivfqVTNAPagelelaGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQ 410
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
5961-6415 2.24e-09

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 64.60  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQP-DQMVGLMvERSLEMVVGMIAILKAGGAYVPIDPDY-------------P------ 6020
Cdd:cd05943    99 VTWAELRRRVARLAAALRALGVKPgDRVAGYL-PNIPEAVVAMLATASIGAIWSSCSPDFgvpgvldrfgqiePkvlfav 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6021 ------------EDRIRYMLED--SGAKLLLV----QGHLLDrASFADKLVNLNDDGAYHEDGS-NLEPVNgPEHLTYVI 6081
Cdd:cd05943   178 daytyngkrhdvREKVAELVKGlpSLLAVVVVpytvAAGQPD-LSKIAKALTLEDFLATGAAGElEFEPLP-FDHPLYIL 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6082 YTSGTTGRPK-------GVMVEHrnvvrlvkntnyveLNEqtHILQT----GAVVFDAST--FEIW----GALLNGGR-- 6142
Cdd:cd05943   256 YSSGTTGLPKcivhgagGTLLQH--------------LKE--HILHCdlrpGDRLFYYTTcgWMMWnwlvSGLAVGATiv 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6143 LY----VVRNETILDAVSLKNAIQQYGINTMWLTAPLYNQLSQQDSGMFAGLKTLIVGGDVL---SVPHINRVLREHAGL 6215
Cdd:cd05943   320 LYdgspFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLkpeSFDYVYDHIKPDVLL 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6216 SIVNGyGPTENTTFSTTHTIV----GE-QK----EAVPI----GKPINNSTAYIVDSK-LSLLPVGVWGElivgGDGvar 6281
Cdd:cd05943   400 ASISG-GTDIISCFVGGNPLLpvyrGEiQCrglgMAVEAfdeeGKPVWGEKGELVCTKpFPSMPVGFWND----PDG--- 471
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6282 gylnrpeltaEKFVESSF--LPGerCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIV 6359
Cdd:cd05943   472 ----------SRYRAAYFakYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVG 539
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 6360 REDESGQKQLcAYFVAER---ELTiGELRAALSQELPNYMIPSHfVPLE-----RMPLTPNGKI 6415
Cdd:cd05943   540 QEWKDGDERV-ILFVKLRegvELD-DELRKRIRSTIRSALSPRH-VPAKiiavpDIPRTLSGKK 600
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1645-1795 2.60e-09

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 63.53  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1645 GELCIGGIGVARGYLNRPElteekfvDSPFVEgERLYRTGDLARwMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKA 1724
Cdd:PRK07824  208 GRIALGGPTLAKGYRNPVD-------PDPFAE-PGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATH 278
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 1725 EGVREAVVVVREDAK-GQKVLCAYFTAESELK-LSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK07824  279 PAVADCAVFGLPDDRlGQRVVAAVVGDGGPAPtLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
266-741 2.97e-09

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 64.21  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  266 FEEQAERR---PDAVAV----TFEDRQLTYGELNERANRLARTLRNAGVQA-DQLVGLMvERSLEMIVGIMGILKAGGAY 337
Cdd:cd05943    72 YAENLLRHadaDDPAAIyaaeDGERTEVTWAELRRRVARLAAALRALGVKPgDRVAGYL-PNIPEAVVAMLATASIGAIW 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  338 ----------------VPIDP--------------EYP-EERIRYMLED--SGTQVLL---SQGHLQERVSFSGTWIRLD 381
Cdd:cd05943   151 sscspdfgvpgvldrfGQIEPkvlfavdaytyngkRHDvREKVAELVKGlpSLLAVVVvpyTVAAGQPDLSKIAKALTLE 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  382 DEEAYHEDGS-NLESVNgPEHLTYVIYTSGTTGKPKGNLTTHRNIIRVVKntnyidvtgqdKLLQLSSYSFDGSTFDIF- 459
Cdd:cd05943   231 DFLATGAAGElEFEPLP-FDHPLYILYSSGTTGLPKCIVHGAGGTLLQHL-----------KEHILHCDLRPGDRLFYYt 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  460 -----------GALLNGAKLVL------VPKETVLdvaklAGLIEKQQISVMFITTAFFNVLvdmnpdclrhARAILFGG 522
Cdd:cd05943   299 tcgwmmwnwlvSGLAVGATIVLydgspfYPDTNAL-----WDLADEEGITVFGTSAKYLDAL----------EKAGLKPA 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  523 ERVSVSHVRkalghlgpgkikhVYGPTESTVFATSYD-VHE-----VEEGAVS---------------IPIG-GPIS--- 577
Cdd:cd05943   364 ETHDLSSLR-------------TILSTGSPLKPESFDyVYDhikpdVLLASISggtdiiscfvggnplLPVYrGEIQcrg 430
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  578 -NTAIYIVNAQNKlQPIGVAGEL-CVAG-DGLARGYLNRPDltAEKFADNPFA--PGerMYRTGDLARWLPDGTIEYVGR 652
Cdd:cd05943   431 lGMAVEAFDEEGK-PVWGEKGELvCTKPfPSMPVGFWNDPD--GSRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGR 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  653 IDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVRESANGEKQLCAYYV------ADRSLpANEVRSTLSQELPAYMLPS 726
Cdd:cd05943   506 SDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKlregveLDDEL-RKRIRSTIRSALSPRHVPA 584
                         570
                  ....*....|....*
gi 386647928  727 YFVQLEQMPLTTNGK 741
Cdd:cd05943   585 KIIAVPDIPRTLSGK 599
PLN02614 PLN02614
long-chain acyl-CoA synthetase
287-684 3.55e-09

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 64.27  E-value: 3.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  287 TYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGiMGILKAGGAY-VPIDPEYPEERIRYMLEDSGTQVLL--- 362
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIIS-MEACNAHGLYcVPLYDTLGAGAVEFIISHSEVSIVFvee 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  363 ------------SQGHLQERVSFSGTwIRLDDEEA---------YHE-----DGSNLE-SVNGPEHLTYVIYTSGTTGKP 415
Cdd:PLN02614  160 kkiselfktcpnSTEYMKTVVSFGGV-SREQKEEAetfglviyaWDEflklgEGKQYDlPIKKKSDICTIMYTSGTTGDP 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  416 KGNLTTHRNI-------IRVVKNTNYiDVTGQDKLLQLS--SYSFDGSTFDIF-------GALLNGAKLVL--------- 470
Cdd:PLN02614  239 KGVMISNESIvtliagvIRLLKSANA-ALTVKDVYLSYLplAHIFDRVIEECFiqhgaaiGFWRGDVKLLIedlgelkpt 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  471 ----VPKetVLDVA------KLA--GLIEKQQISVMFiTTAFFNVL-----VDMNPDCLR------------HARAILFG 521
Cdd:PLN02614  318 ifcaVPR--VLDRVysglqkKLSdgGFLKKFVFDSAF-SYKFGNMKkgqshVEASPLCDKlvfnkvkqglggNVRIILSG 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  522 GERVSvSHVRKALGHLGPGKIKHVYGPTEST--VFATSYDvhevEEGAVSIpIGGPISNTAIYIVNA-QNKLQPIGVA-- 596
Cdd:PLN02614  395 AAPLA-SHVESFLRVVACCHVLQGYGLTESCagTFVSLPD----ELDMLGT-VGPPVPNVDIRLESVpEMEYDALASTpr 468
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  597 GELCVAGDGLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRIDDQVKI-RGFRIELGEIEAHLLK 675
Cdd:PLN02614  469 GEICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIYGE 541

                  ....*....
gi 386647928  676 LEAIEKATV 684
Cdd:PLN02614  542 VQAVDSVWV 550
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
5961-6360 4.15e-09

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 63.92  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQG 6040
Cdd:cd05933     9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6041 H-LLDRAS-FADKLVNLNDDGAYHEDGSNLEP------------VNGPEH-------------LTYVIYTSGTTGRPKGV 6093
Cdd:cd05933    89 QkQLQKILqIQDKLPHLKAIIQYKEPLKEKEPnlyswdefmelgRSIPDEqldaiissqkpnqCCTLIYTSGTTGMPKGV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6094 MVEHRNVVRLVKN-TNYVELNEQTHiLQTGAVVF------DASTFEIWGALLNGGRLYVVRnetiLDAV--SLKNAIQQ- 6163
Cdd:cd05933   169 MLSHDNITWTAKAaSQHMDLRPATV-GQESVVSYlplshiAAQILDIWLPIKVGGQVYFAQ----PDALkgTLVKTLREv 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6164 -----YGINTMW-----------------------------LTAPLYNQLSQQDSGMFAGL-KTLIVGG--DVLSVPHIN 6206
Cdd:cd05933   244 rptafMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgLETNLKLMGGESPSPLFYRLaKKLVFKKvrKALGLDRCQ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6207 RVLREHAGLS-------------IVNGYGPTENttfSTTHTivgeqkeavpigkpINNSTAYIVDSKLSLLPvGVW---- 6269
Cdd:cd05933   324 KFFTGAAPISretlefflslnipIMELYGMSET---SGPHT--------------ISNPQAYRLLSCGKALP-GCKtkih 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6270 -------GELIVGGDGVARGYLNRPELTAEKFVESSFLpgercyRTGDLARWLPDGTLEYKGRIDEQVKIRGyrielGE- 6341
Cdd:cd05933   386 npdadgiGEICFWGRHVFMGYLNMEDKTEEAIDEDGWL------HSGDLGKLDEDGFLYITGRIKELIITAG-----GEn 454
                         490       500
                  ....*....|....*....|....
gi 386647928 6342 -----IEEqllkvaSVKEATVIVR 6360
Cdd:cd05933   455 vppvpIED------AVKKELPIIS 472
PLN02614 PLN02614
long-chain acyl-CoA synthetase
3881-4274 4.17e-09

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 63.89  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3881 TYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALLTQ-- 3958
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEek 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3959 -------------RHLRERVSFAGtfvaVDDEQAYHAD-----------------GSNLE-PVVGPNHLAYVIYTSGTTG 4007
Cdd:PLN02614  161 kiselfktcpnstEYMKTVVSFGG----VSREQKEEAEtfglviyawdeflklgeGKQYDlPIKKKSDICTIMYTSGTTG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4008 KPKGVMVEHHGLCSL-----KLMFANTLQMTEQDRVVQFASLS--FDASCWEIF--------------KALFFGATLYIP 4066
Cdd:PLN02614  237 DPKGVMISNESIVTLiagviRLLKSANAALTVKDVYLSYLPLAhiFDRVIEECFiqhgaaigfwrgdvKLLIEDLGELKP 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4067 T----STTILD--YPLFESYMNENGITATILPPTYAAY-------------LNP--DRMPSLK---------KLITGGSA 4116
Cdd:PLN02614  317 TifcaVPRVLDrvYSGLQKKLSDGGFLKKFVFDSAFSYkfgnmkkgqshveASPlcDKLVFNKvkqglggnvRIILSGAA 396
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4117 ASVEFVQQWKDKVLYFN---AYGPTE--ASIVTSIWDEAsDSLGDrksvpIGRPLANHRI---YVVDSHNRMLPVGVAGE 4188
Cdd:PLN02614  397 PLASHVESFLRVVACCHvlqGYGLTEscAGTFVSLPDEL-DMLGT-----VGPPVPNVDIrleSVPEMEYDALASTPRGE 470
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4189 LCISGVGLARGYLNRPELTAEKFVDNpfepgerMYRTGDLVRWLPDGNLEYLGRIDHQVKI-RGYRIELGEVETQLAKID 4267
Cdd:PLN02614  471 ICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQ 543

                  ....*..
gi 386647928 4268 AVQEAIV 4274
Cdd:PLN02614  544 AVDSVWV 550
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2960-3121 4.37e-09

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 63.10  E-value: 4.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2960 GFDEAAIRKVLQKLVEHHDALRVVFHKSENGYTAWNRAigEGELYgLEVVDLKGIEES--AQAVEAKANEiqsSIDLEAG 3037
Cdd:cd20484    35 KLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEP--SKPLS-FQEEDISSLKESeiIAYLREKAKE---PFVLENG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3038 PFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEELRFPAKTDAYR---TWSEQLAAYAQSpviE 3113
Cdd:cd20484   109 PLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYdfvAWEQDMLAGAEG---E 185

                  ....*...
gi 386647928 3114 RELAYWKR 3121
Cdd:cd20484   186 EHRAYWKQ 193
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1439-1795 4.77e-09

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 63.53  E-value: 4.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1439 EPHDLAYVIYTSGTTGRPKGVMIEHRSLV------NTAAG----YRREyrldqFPVRLLQLasfsFDVFvgdiART---- 1504
Cdd:PRK08974  204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLanleqaKAAYGpllhPGKE-----LVVTALPL----YHIF----ALTvncl 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1505 --LYNGGTMVIC--PKDdridparLHYWISEEKITIFESTPALIIPFMDYVAE---HGLDMSSMELLITSSDSCSvtdyR 1577
Cdd:PRK08974  271 lfIELGGQNLLItnPRD-------IPGFVKELKKYPFTAITGVNTLFNALLNNeefQELDFSSLKLSVGGGMAVQ----Q 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1578 VLQERFGS--QFRIINAYGVTEAA--IDSSLYDepLAKLpeagNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIG 1653
Cdd:PRK08974  340 AVAERWVKltGQYLLEGYGLTECSplVSVNPYD--LDYY----SGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQ 413
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1654 VARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQL-LKAEGVREAVV 1732
Cdd:PRK08974  414 VMLGYWQRPEATDEVIKDG-------WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVmLHPKVLEVAAV 486
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 1733 VVREDAKGQKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PRK08974  487 GVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK09192 PRK09192
fatty acyl-AMP ligase;
5960-6098 4.87e-09

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 63.49  E-value: 4.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5960 QLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYP-------EDRIRYMLEDSG 6032
Cdd:PRK09192   49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQ 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 6033 AKLLLVQGHLLDRASFADKLVNLNDDGAyHEDGSNLE------PVNGPEHLTYVIYTSGTTGRPKGVMVEHR 6098
Cdd:PRK09192  129 PAAIITPDELLPWVNEATHGNPLLHVLS-HAWFKALPeadvalPRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
4905-5387 4.98e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 63.51  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4905 AVVYENDRLTYRE-LNERANR--LARTLRAQGVKPNqlVGILADRSADLLVGALAVWKAGGAYVPLDP---------DYP 4972
Cdd:PRK13388   19 AVRYGDRTWTWREvLAEAAARaaALIALADPDRPLH--VGVLLGNTPEMLFWLAAAALGGYVLVGLNTtrrgaalaaDIR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLEDSAASVLLTqthlqeraqqwGQTLQAALCLD-DEAAYAEdASNVANVNEPH------DLAYVIYTSGTTGR 5045
Cdd:PRK13388   97 RADCQLLVTDAEHRPLLD-----------GLDLPGVRVLDvDTPAYAE-LVAAAGALTPHrevdamDPFMLIFTSGTTGA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5046 PKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPK-------DDridparlhyw 5118
Cdd:PRK13388  165 PKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKfsasgflDD---------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5119 iseekITIFESTpaliipFMDYV----------AEHGlDMSSMVLLITSSDSCSVTDYRVLQERFGSQfrIINAYGVTEA 5188
Cdd:PRK13388  235 -----VRRYGAT------YFNYVgkplayilatPERP-DDADNPLRVAFGNEASPRDIAEFSRRFGCQ--VEDGYGSSEG 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5189 AIdsSLYDEPLAklPEAGnvpIGKAALNAKfyIVDAH-LNPVPVGVL-------------GELC-IGGIGVARGYLNRPE 5253
Cdd:PRK13388  301 AV--IVVREPGT--PPGS---IGRGAPGVA--IYNPEtLTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPE 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5254 LTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQK 5332
Cdd:PRK13388  372 ATAERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERvGDQ 444
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928 5333 VLCAHFTAE-SELKLSELRSSLS--QELPGYMIPSYFVQLEQLPLTANGKIDRKALPA 5387
Cdd:PRK13388  445 VMAALVLRDgATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
6270-6421 5.14e-09

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 63.09  E-value: 5.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6270 GELIVGGDGVARGYLnrPEltaekfvessFLPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKV 6349
Cdd:PRK07445  302 GNITIQAQSLALGYY--PQ----------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 6350 ASVKEATVI-VREDESGQKQLCAYFVAERELTIGELRAALSQELPNYMIPSHFVPLERMPLTPNGKIDRRALP 6421
Cdd:PRK07445  370 GLVQDVCVLgLPDPHWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
4907-5282 5.16e-09

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 63.24  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4907 VYENDRLTYRELNERANRLARTLRA-QGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPL------------------ 4967
Cdd:cd17632    62 LPRFETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLqagasaaqlapilaetep 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4968 -----DPDYPSDRIQFMLEDSAASVLLTQTHLQE----RAQQWGQTLQAA-----LCLDDEAAYAEDASNVAN--VNEPH 5031
Cdd:cd17632   142 rllavSAEHLDLAVEAVLEGGTPPRLVVFDHRPEvdahRAALESARERLAavgipVTTLTLIAVRGRDLPPAPlfRPEPD 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5032 D--LAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDr 5109
Cdd:cd17632   222 DdpLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASD- 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5110 idparlhywISeekiTIFES------TPALIIP------FMDYVAEhgLDMSSMVLLITSSDSCSVTDY---RVLQERFG 5174
Cdd:cd17632   301 ---------MS----TLFDDlalvrpTELFLVPrvcdmlFQRYQAE--LDRRSVAGADAETLAERVKAElreRVLGGRLL 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5175 S--------------------QFRIINAYGVTEAA---IDSSLYDEP-----LAKLPEAGnvpigkaalnakFYIVDahl 5226
Cdd:cd17632   366 AavcgsaplsaemkafmesllDLDLHDGYGSTEAGaviLDGVIVRPPvldykLVDVPELG------------YFRTD--- 430
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 5227 NPVPvgvLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlYRTGD-LARWMPD 5282
Cdd:cd17632   431 RPHP---RGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDvMAELGPD 478
PRK05857 PRK05857
fatty acid--CoA ligase;
4895-5397 5.26e-09

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 63.10  E-value: 5.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4895 KQAECTPEAAAVVYEN--DRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 4972
Cdd:PRK05857   22 EQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4973 SDRIQFMLE--DSAASVLLTQTHLQERAQQWGQTLQAALCLDDEAAYAEDASN------VANVNEPHD--LAyVIYTSGT 5042
Cdd:PRK05857  102 IAAIERFCQitDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSldaaslAGNADQGSEdpLA-MIFTSGT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5043 TGRPKGVMIEHRSLVNTAAGYRRE---------YRLDQFPVRLLQLASFSFdvfvgdIARTLYNGGTMVICPKDDridpA 5113
Cdd:PRK05857  181 TGEPKAVLLANRTFFAVPDILQKEglnwvtwvvGETTYSPLPATHIGGLWW------ILTCLMHGGLCVTGGENT----T 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5114 RLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQerfGSQFRIINAYGVTE---AAI 5190
Cdd:PRK05857  251 SLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIE---ATGVRTAQVYGLSEtgcTAL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5191 DSSLYDEPLAKLpEAGNVpiGKAALNAKFYIVDAH------LNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpf 5264
Cdd:PRK05857  328 CLPTDDGSIVKI-EAGAV--GRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG-- 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5265 vegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFTAESEL 5344
Cdd:PRK05857  403 -----WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEL 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5345 KLS---ELRSSLS----QELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASMQTGME 5397
Cdd:PRK05857  478 DESaarALKHTIAarfrRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVV 537
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
281-684 5.61e-09

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 63.08  E-value: 5.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  281 FEDRQLTYGELNERANRLARTLRN-AGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQ 359
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  360 VLLSQGHLQERV--------------------SFSGTWIRLDDEEAYHEDGSNLESVNGPEHLT----YvIYTSGTTGKP 415
Cdd:cd05938    81 VLVVAPELQEAVeevlpalradgvsvwylshtSNTEGVISLLDKVDAASDEPVPASLRAHVTIKspalY-IYTSGTTGLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  416 KGNLTTHRNIIRVVKNTNYIDVTGQDKL-LQLSSYSFDGSTFDIFGALLNGAKLVLVPKetvldvaklagliekqqisvm 494
Cdd:cd05938   160 KAARISHLRVLQCSGFLSLCGVTADDVIyITLPLYHSSGFLLGIGGCIELGATCVLKPK--------------------- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  495 FITTAFFNvlvdmnpDCLRH-ARAILFGGE-----------RVSVSH-VRKALGH-------------LGPGKIKHVYGP 548
Cdd:cd05938   219 FSASQFWD-------DCRKHnVTVIQYIGEllrylcnqpqsPNDRDHkVRLAIGNglradvwreflrrFGPIRIREFYGS 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  549 TESTVFATSYDVHeveegavsipIGgpisntAIYIVNAQNKL--------------QPIGVAGELCV------AGDGLAR 608
Cdd:cd05938   292 TEGNIGFFNYTGK----------IG------AVGRVSYLYKLlfpfelikfdvekeEPVRDAQGFCIpvakgePGLLVAK 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  609 --------GYLNRPDLTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIE 680
Cdd:cd05938   356 itqqspflGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQ 435

                  ....
gi 386647928  681 KATV 684
Cdd:cd05938   436 EVNV 439
PRK07867 PRK07867
acyl-CoA synthetase; Validated
5932-6422 5.74e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 63.16  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5932 PSDKTIHQLFEEQAEriPDHLAVTFEDKQLTYGELNERANRLARTLRnAGVQPDQ--MVGLMVERSLEMVVGMIAILKAG 6009
Cdd:PRK07867    2 SSAPTVAELLLPLAE--DDDRGLYFEDSFTSWREHIRGSAARAAALR-ARLDPTRppHVGVLLDNTPEFSLLLGAAALSG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6010 GAYVPIDPDYPEDRIRYMLEDSGAKLLLV---QGHLLDRASFADKLVNLN-----DDGAYHEDGSNLEPVNGPEHLTYVI 6081
Cdd:PRK07867   79 IVPVGLNPTRRGAALARDIAHADCQLVLTesaHAELLDGLDPGVRVINVDspawaDELAAHRDAEPPFRVADPDDLFMLI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6082 YTSGTTGRPKGVMVEHRNV----VRLVK-------NTNYVELNeqthILQTGAVVFDastfeiWGALLNGGRLYVVRNEt 6150
Cdd:PRK07867  159 FTSGTSGDPKAVRCTHRKVasagVMLAQrfglgpdDVCYVSMP----LFHSNAVMAG------WAVALAAGASIALRRK- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6151 iLDAVSLKNAIQQYGINTM-WLTAPLYNQLSQQDSGMFAGLKTLIVGGDVLSVPHINRvLREHAGLSIVNGYGPTEnTTF 6229
Cdd:PRK07867  228 -FSASGFLPDVRRYGATYAnYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIAR-FARRFGCVVVDGFGSTE-GGV 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6230 STTHTivgeqkEAVP---IGKPINNSTAYIVDSkLSLLPVGVW------------GELI-VGGDGVARGYLNRPELTAEK 6293
Cdd:PRK07867  305 AITRT------PDTPpgaLGPLPPGVAIVDPDT-GTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAER 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6294 FVESSflpgercYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYF 6373
Cdd:PRK07867  378 MRGGV-------YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAAL 450
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386647928 6374 VAER--ELTIGELRAALSQ--ELPNYMIPSHFVPLERMPLTPNGKIDRRALPA 6422
Cdd:PRK07867  451 VLAPgaKFDPDAFAEFLAAqpDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
4912-5380 5.74e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 63.19  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4912 RLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI---------QFMLED 4982
Cdd:PRK07008   39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIayivnhaedRYVLFD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4983 SAASVLLTQTHLQ-ERAQQWGQTLQAA---------LCLDDEAAyAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIE 5052
Cdd:PRK07008  119 LTFLPLVDALAPQcPNVKGWVAMTDAAhlpagstplLCYETLVG-AQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5053 HRSLV--NTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLyNGGTMVICPKDdrIDPARLHYWISEEKITIFEST 5130
Cdd:PRK07008  198 HRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPGPD--LDGKSLYELIEAERVTFSAGV 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5131 PALIIPFMDYVAEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAA---IDSSLYDEPLAkLPEAGN 5207
Cdd:PRK07008  275 PTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYG--VEVIHAWGMTEMSplgTLCKLKWKHSQ-LPLDEQ 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5208 VPI----GKAALNAKFYIVDAHLNPVPV-GV-LGELCIGGIGVARGYLNRPelteekfvDSPFVEGerLYRTGDLARWMP 5281
Cdd:PRK07008  352 RKLlekqGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGD--------ASPLVDG--WFPTGDVATIDA 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5282 DGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVreavvvvredAKGQKVLCAH------------FTAESELKLSEL 5349
Cdd:PRK07008  422 DGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAV----------AEAACIACAHpkwderpllvvvKRPGAEVTREEL 491
                         490       500       510
                  ....*....|....*....|....*....|.
gi 386647928 5350 RSSLSQELPGYMIPSYFVQLEQLPLTANGKI 5380
Cdd:PRK07008  492 LAFYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
2366-2508 5.81e-09

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 63.08  E-value: 5.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2366 FEGQQLTYRELNERANRLARTL-QALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQ 2444
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2445 VLLAQRRLQERV--------------------SFAGTVVTVDDEQAYAGDGS---NLESAVGPNDLAYIIYTSGTTGKPK 2501
Cdd:cd05938    81 VLVVAPELQEAVeevlpalradgvsvwylshtSNTEGVISLLDKVDAASDEPvpaSLRAHVTIKSPALYIYTSGTTGLPK 160

                  ....*..
gi 386647928 2502 GVMVEHH 2508
Cdd:cd05938   161 AARISHL 167
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
284-655 6.58e-09

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 63.21  E-value: 6.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  284 RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSGTQVLLS 363
Cdd:cd17641    10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  364 Q------------------------------GHLQERVSFSGTWIRLDDEEAYHEDGSNLESVNG--PEHLTYVIYTSGT 411
Cdd:cd17641    90 EdeeqvdklleiadripsvryviycdprgmrKYDDPRLISFEDVVALGRALDRRDPGLYEREVAAgkGEDVAVLCTTSGT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  412 TGKPKGNLTTHRNIIRvvKNTNYIDVTGQ---DKLLQLSSYSFDGSTFDIFGALLNGAKLVLVPKE--TVLDVAKLAG-- 484
Cdd:cd17641   170 TGKPKLAMLSHGNFLG--HCAAYLAADPLgpgDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEpeTMMEDLREIGpt 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  485 -------LIEKQQISVM-----------FITTAFFNVLVDMNPDCLRH-------------ARAILFGG--ERVSVSHVR 531
Cdd:cd17641   248 fvllpprVWEGIAADVRarmmdatpfkrFMFELGMKLGLRALDRGKRGrpvslwlrlaswlADALLFRPlrDRLGFSRLR 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  532 KAL---GHLGPG----------KIKHVYGPTESTVFATSYDVHEVEEGAVsipiGGPISNTAIYIVNAqnklqpigvaGE 598
Cdd:cd17641   328 SAAtggAALGPDtfrffhaigvPLKQLYGQTELAGAYTVHRDGDVDPDTV----GVPFPGTEVRIDEV----------GE 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  599 LCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDD 655
Cdd:cd17641   394 ILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKD 444
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
4911-5385 7.00e-09

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 62.78  E-value: 7.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4911 DRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDriqfmlEDSAASVLLT 4990
Cdd:cd05929    16 RLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRA------EACAIIEIKA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4991 QTHLQERAQQWGqtlqaalCLDDEAAYAE-----DASNVANVNEPHDLayvIYTSGTTGRPKGVM---------IEHRSL 5056
Cdd:cd05929    90 AALVCGLFTGGG-------ALDGLEDYEAaeggsPETPIEDEAAGWKM---LYSGGTTGRPKGIKrglpggppdNDTLMA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5057 VNTAAGYRREYRLdQFPVRLLQLASFSFdvfvgdIARTLYNGGTMVICPKddrIDPARLHYWISEEKITIFESTPAL--- 5133
Cdd:cd05929   160 AALGFGPGADSVY-LSPAPLYHAAPFRW------SMTALFMGGTLVLMEK---FDPEEFLRLIERYRVTFAQFVPTMfvr 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5134 IIPFMDYVaEHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSqfRIINAYGVTEA----AIDSSLYdeplakLPEAGNVp 5209
Cdd:cd05929   230 LLKLPEAV-RNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGP--IIWEYYGGTEGqgltIINGEEW------LTHPGSV- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5210 iGKAALnAKFYIVDAHLNPVPVGVLGELCIGGiGVARGYLNRPELTEEKFvdspfveGERLYRT-GDLARWMPDGNVDFI 5288
Cdd:cd05929   300 -GRAVL-GKVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAAR-------NEGGWSTlGDVGYLDEDGYLYLT 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5289 GRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAK-GQKVLCAHFTAES----ELKLSELRSSLSQELPGYMIP 5363
Cdd:cd05929   370 DRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEElGQRVHAVVQPAPGadagTALAEELIAFLRDRLSRYKCP 449
                         490       500
                  ....*....|....*....|..
gi 386647928 5364 SYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05929   450 RSIEFVAELPRDDTGKLYRRLL 471
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
4902-5385 7.40e-09

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 62.83  E-value: 7.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4902 EAAAVV-----YENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRI 4976
Cdd:cd05915     9 GRKEVVsrlhtGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4977 QFMLEDSAASVLLTQTHLQERAQQWGQTLQAALCLDDEAAYAEDASNVANVNEPH----------DLAYVIYTSGTTGRP 5046
Cdd:cd05915    89 AYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEeadpvrvperAACGMAYTTGTTGLP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5047 KGVMIEHRS--LVNTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLYNGgtMVICPKDDRIDPARLHYwISEEKI 5124
Cdd:cd05915   169 KGVVYSHRAlvLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGA--KQVLPGPRLDPASLVEL-FDGEGV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5125 TIFESTPaliiPFMDYVA--EHGLDMSSMVLLITSSDSCSVTDYRVLQERFGSqFRIINAYGVTE--AAIDSSLYDEPLA 5200
Cdd:cd05915   246 TFTAGVP----TVWLALAdyLESTGHRLKTLRRLVVGGSAAPRSLIARFERMG-VEVRQGYGLTEtsPVVVQNFVKSHLE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5201 KLPEAGNVPI-GKAALNAKFYIVDAhLNPVPVGV------LGELCIGGIGVARGYLNRPELTEEkfvdSPFVEGerLYRT 5273
Cdd:cd05915   321 SLSEEEKLTLkAKTGLPIPLVRLRV-ADEEGRPVpkdgkaLGEVQLKGPWITGGYYGNEEATRS----ALTPDG--FFRT 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5274 GDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAHFT-AESELKLSELRSS 5352
Cdd:cd05915   394 GDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVpRGEKPTPEELNEH 473
                         490       500       510
                  ....*....|....*....|....*....|....
gi 386647928 5353 LSQELPGY-MIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05915   474 LLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRAL 507
PLN02654 PLN02654
acetate-CoA ligase
1320-1795 7.62e-09

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 62.99  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1320 NDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL 1399
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1400 TQT---------HLQE-------RAQQWGQTLQAVLCLDDEAAYAEDASN------------VANVNEPHDLAYV----- 1446
Cdd:PLN02654  198 TCNavkrgpktiNLKDivdaaldESAKNGVSVGICLTYENQLAMKREDTKwqegrdvwwqdvVPNYPTKCEVEWVdaedp 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1447 ---IYTSGTTGRPKGVMiehrslvNTAAGYRReYRLDQFpvrllqlaSFSFDVFVGDIA-----------------RTLY 1506
Cdd:PLN02654  278 lflLYTSGSTGKPKGVL-------HTTGGYMV-YTATTF--------KYAFDYKPTDVYwctadcgwitghsyvtyGPML 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1507 NGGTMVI---CPkdDRIDPARLHYWISEEKITIFESTPALIIPFM----DYVAEHglDMSSMELLITSSDSCSVTDYRVL 1579
Cdd:PLN02654  342 NGATVLVfegAP--NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgdEYVTRH--SRKSLRVLGSVGEPINPSAWRWF 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1580 QERFG-SQFRIINAYGVTEAAidsslyDEPLAKLPEAGNVPIGKAALnaKFY-----IVDAHLNPVPVGVLGELCI---- 1649
Cdd:PLN02654  418 FNVVGdSRCPISDTWWQTETG------GFMITPLPGAWPQKPGSATF--PFFgvqpvIVDEKGKEIEGECSGYLCVkksw 489
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1650 -GGIGVARGYLNRPELTEEKfvdsPFvegERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLK-AEGV 1727
Cdd:PLN02654  490 pGAFRTLYGDHERYETTYFK----PF---AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVShPQCA 562
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 1728 REAVVVVREDAKGQKVLCAYFTAESELKLSELRSSL----SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PLN02654  563 EAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
7594-7900 8.65e-09

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 62.09  E-value: 8.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7594 TSGTTGKPKGVMVEHHGLCSLKLMFAETLR---ITEEDRVVQFAS-------LSFDASCWEIfkalffGATLyIPA---- 7659
Cdd:COG1541    91 SSGTTGKPTVVGYTRKDLDRWAELFARSLRaagVRPGDRVQNAFGyglftggLGLHYGAERL------GATV-IPAgggn 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7660 KDTILDYplfesyMNENGITAAILPPTYAIYL---------SPDRLpSLKKLITGGSAASVEFVQQWKDK--VRYFNAYG 7728
Cdd:COG1541   164 TERQLRL------MQDFGPTVLVGTPSYLLYLaevaeeegiDPRDL-SLKKGIFGGEPWSEEMRKEIEERwgIKAYDIYG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7729 PTEASivTSVWAASP--DGLDLRsvpigrpiANHQIF-IVDSQNHM-LPVGVAGELCISGaglargylnrpeLTAEKFvd 7804
Cdd:COG1541   237 LTEVG--PGVAYECEaqDGLHIW--------EDHFLVeIIDPETGEpVPEGEEGELVVTT------------LTKEAM-- 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7805 nPFLageRmYRTGDLARWLPDGN--------IEY-LGRIDHQVKIRGYRIELGEIEEQLLKIASVQE--TIVIARgdANG 7873
Cdd:COG1541   293 -PLI---R-YRTGDLTRLLPEPCpcgrthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPeyQIVVDR--EGG 365
                         330       340
                  ....*....|....*....|....*..
gi 386647928 7874 QQQLCAYFVADRELTVSELRGTLSQEL 7900
Cdd:COG1541   366 LDELTVRVELAPGASLEALAEAIAAAL 392
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
1322-1790 1.04e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 62.42  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1322 RLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVL--- 1398
Cdd:PRK07008   39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVlfd 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1399 LTQTHLQERAQQWGQTLQAVLCLDDEAAYAEDASNVANVN---EPHDLAY------------VIYTSGTTGRPKGVMIEH 1463
Cdd:PRK07008  119 LTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTPLLCYEtlvGAQDGDYdwprfdenqassLCYTSGTTGNPKGALYSH 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1464 RSLV--NTAAGYRREYRLDQFPVRLLQLASFSFDVFVGDIARTLyNGGTMVICPKDdrIDPARLHYWISEEKITIFESTP 1541
Cdd:PRK07008  199 RSTVlhAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPGPD--LDGKSLYELIEAERVTFSAGVP 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1542 ALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQERFGsqFRIINAYGVTEAA---IDSSLYDEPLAkLPEAGNV 1618
Cdd:PRK07008  276 TVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYG--VEVIHAWGMTEMSplgTLCKLKWKHSQ-LPLDEQR 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1619 PI----GKAALNAKFYIVDAHLNPVPV-GV-LGELCIGGIGVARGYLNRPelteekfvDSPFVEGerLYRTGDLARWMPD 1692
Cdd:PRK07008  353 KLlekqGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGD--------ASPLVDG--WFPTGDVATIDAD 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1693 GNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQK--VLCAYFTAESELKLSELRSSLSQELPGY 1770
Cdd:PRK07008  423 GFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDErpLLVVVKRPGAEVTREELLAFYEGKVAKW 502
                         490       500
                  ....*....|....*....|
gi 386647928 1771 MIPSYFVQLEQLPLTANGKI 1790
Cdd:PRK07008  503 WIPDDVVFVDAIPHTATGKL 522
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
1323-1721 1.12e-08

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 62.44  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML-EDSAASVLLTQ 1401
Cdd:PLN02387  107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLnETEVTTVICDS 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 THLQERAQQWGQ--TLQAVLCLDDEAAYAEDA------------SNV----------ANVNEPHDLAYVIYTSGTTGRPK 1457
Cdd:PLN02387  187 KQLKKLIDISSQleTVKRVIYMDDEGVDSDSSlsgssnwtvssfSEVeklgkenpvdPDLPSPNDIAVIMYTSGSTGLPK 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1458 GVMIEHRSLVNTAAGYR--------REYRLDQFPV-RLLQLASFSFDVFVGdiARTLYnGGTMVICPKDDRI------Dp 1522
Cdd:PLN02387  267 GVMMTHGNIVATVAGVMtvvpklgkNDVYLAYLPLaHILELAAESVMAAVG--AAIGY-GSPLTLTDTSNKIkkgtkgD- 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1523 arlhywISEEKITIFESTPALIIPFMDYV-----AEHGL-----DMSSMELLITSSDSC-----------SVTDYRVLQE 1581
Cdd:PLN02387  343 ------ASALKPTLMTAVPAILDRVRDGVrkkvdAKGGLakklfDIAYKRRLAAIEGSWfgawglekllwDALVFKKIRA 416
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1582 RFGSQFR------------------------IINAYGVTE--AAIDSSLYDEP---------------LAKLPEAGnvpi 1620
Cdd:PLN02387  417 VLGGRIRfmlsggaplsgdtqrfiniclgapIGQGYGLTEtcAGATFSEWDDTsvgrvgpplpccyvkLVSWEEGG---- 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1621 gkaalnakFYIVDAhlnPVPvgvLGELCIGGIGVARGYLNRPELTEEKF-VDSpfvEGERLYRTGDLARWMPDGNVDFIG 1699
Cdd:PLN02387  493 --------YLISDK---PMP---RGEIVIGGPSVTLGYFKNQEKTDEVYkVDE---RGMRWFYTGDIGQFHPDGCLEIID 555
                         490       500
                  ....*....|....*....|...
gi 386647928 1700 RIDNQAKIR-GYRIETGEIETQL 1721
Cdd:PLN02387  556 RKKDIVKLQhGEYVSLGKVEAAL 578
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
2371-2733 1.15e-08

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 62.55  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2371 LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPI-DP----------EYPEDRISYMLE 2439
Cdd:PLN02861   78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLyDTlganavefiiNHAEVSIAFVQE 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2440 DSSAQVLLAQRR----LQERVSFaGTVVTVDDEQA------------YAGDGSnLESAVGP---NDLAYIIYTSGTTGKP 2500
Cdd:PLN02861  158 SKISSILSCLPKcssnLKTIVSF-GDVSSEQKEEAeelgvscfsweeFSLMGS-LDCELPPkqkTDICTIMYTSGTTGEP 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2501 KGVMVEHH----GLCSLKQMFANTLQINAQ--------------DRVVQFASLSFDASC--WE----------------- 2543
Cdd:PLN02861  236 KGVILTNRaiiaEVLSTDHLLKVTDRVATEedsyfsylplahvyDQVIETYCISKGASIgfWQgdirylmedvqalkpti 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2544 ------VFQTLFFGATLYIPT----KETILDYQW-------------------FERYMSDNgiTTATLPPTYAVYLN--- 2591
Cdd:PLN02861  316 fcgvprVYDRIYTGIMQKISSggmlRKKLFDFAYnyklgnlrkglkqeeasprLDRLVFDK--IKEGLGGRVRLLLSgaa 393
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2592 --PDHMPDFKRLIaagSASSLEllqqwkdkvkyfNAYGPTED------------SICTTIWTPSTEDISQLKSVPIGGpi 2657
Cdd:PLN02861  394 plPRHVEEFLRVT---SCSVLS------------QGYGLTEScggcftsianvfSMVGTVGVPMTTIEARLESVPEMG-- 456
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 2658 vnhriyiVDAhYQPVPvgvAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEpgermyrTGDLAKWLPDGTIEYLGR 2733
Cdd:PLN02861  457 -------YDA-LSDVP---RGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGDIGEWQPNGAMKIIDR 514
PRK05857 PRK05857
fatty acid--CoA ligase;
1305-1807 1.19e-08

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 62.33  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1305 KQAERTPEVAAVVYEN--DRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYP 1382
Cdd:PRK05857   22 EQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1383 SDRIQFMLE--DSAASVLLTQTHLQERAQQWGQTLQAVLCLDDEAAYAEDASN------VANVNEPHD--LAyVIYTSGT 1452
Cdd:PRK05857  102 IAAIERFCQitDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSldaaslAGNADQGSEdpLA-MIFTSGT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1453 TGRPKGVMIEHRSLVNTAAGYRRE---------YRLDQFPVRLLQLASFSFdvfvgdIARTLYNGGTMVICPKDDridpA 1523
Cdd:PRK05857  181 TGEPKAVLLANRTFFAVPDILQKEglnwvtwvvGETTYSPLPATHIGGLWW------ILTCLMHGGLCVTGGENT----T 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1524 RLHYWISEEKITIFESTPALIIPFMDYVAEHGLDMSSMELLITSSDSCSVTDYRVLQerfGSQFRIINAYGVTE---AAI 1600
Cdd:PRK05857  251 SLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIE---ATGVRTAQVYGLSEtgcTAL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1601 DSSLYDEPLAKLpEAGNVpiGKAALNAKFYIVDAH------LNPVPVGVLGELCIGGIGVARGYLNRPELTEEKFVDSpf 1674
Cdd:PRK05857  328 CLPTDDGSIVKI-EAGAV--GRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG-- 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1675 vegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVREDAKGQKVLCAYFTAESEL 1754
Cdd:PRK05857  403 -----WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEL 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1755 KLS---ELRSSLS----QELPGYMIPSYFVQLEQLPLTANGKIDRKALPAPDASMQTGME 1807
Cdd:PRK05857  478 DESaarALKHTIAarfrRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVV 537
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1291-1790 1.21e-08

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 62.29  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1291 PDAPENEVFHALFEKqaerTPEVAAVVY-----ENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGAL 1365
Cdd:cd05943    66 PGARLNYAENLLRHA----DADDPAAIYaaedgERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAML 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1366 AVWKAGGAYVPLDPDYPS----DRiqfmLEDSAASVLLT--------QTH-----LQERAQQWGQTLQAVLCLDDEAAYA 1428
Cdd:cd05943   142 ATASIGAIWSSCSPDFGVpgvlDR----FGQIEPKVLFAvdaytyngKRHdvrekVAELVKGLPSLLAVVVVPYTVAAGQ 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1429 EDASNVANVNEPHDLA-------------------YVIYTSGTTGRPK-------GVMIEHRslvntaagyrREYRLdqf 1482
Cdd:cd05943   218 PDLSKIAKALTLEDFLatgaagelefeplpfdhplYILYSSGTTGLPKcivhgagGTLLQHL----------KEHIL--- 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1483 pvrllqlasfSFDVFVGDI---------------ARTLYNGGTMVI---CPKddRIDPARLHYWISEEKITIFESTPALI 1544
Cdd:cd05943   285 ----------HCDLRPGDRlfyyttcgwmmwnwlVSGLAVGATIVLydgSPF--YPDTNALWDLADEEGITVFGTSAKYL 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1545 ipfmDYVAEHGL------DMSSMELLITSSDSCSVTDYRVLQERFGSQFRIINAYGVTEaaidsslydepLAKLPEAGN- 1617
Cdd:cd05943   353 ----DALEKAGLkpaethDLSSLRTILSTGSPLKPESFDYVYDHIKPDVLLASISGGTD-----------IISCFVGGNp 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1618 -VPIGKAALNAKFY-----IVDAHLNPVpVGVLGEL-CIGGI-GVARGYLNRPEltEEKFVDSPFVEGERLYRTGDLARW 1689
Cdd:cd05943   418 lLPVYRGEIQCRGLgmaveAFDEEGKPV-WGEKGELvCTKPFpSMPVGFWNDPD--GSRYRAAYFAKYPGVWAHGDWIEI 494
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1690 MPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEG-VREAVVVVREDAKGQKVLC-------AYFTAESELKL-SELR 1760
Cdd:cd05943   495 TPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEvEDSLVVGQEWKDGDERVILfvklregVELDDELRKRIrSTIR 574
                         570       580       590
                  ....*....|....*....|....*....|
gi 386647928 1761 SSLSqelPGYmIPSYFVQLEQLPLTANGKI 1790
Cdd:cd05943   575 SALS---PRH-VPAKIIAVPDIPRTLSGKK 600
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
4881-5380 1.51e-08

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 61.90  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4881 PDAPENEAFHALFEKQAectPEAAAVVY----ENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALA 4956
Cdd:cd05943    66 PGARLNYAENLLRHADA---DDPAAIYAaedgERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4957 VWKAGGAYVPLDPDYPS----DRiqfmLEDSAASVLLT--------QTH-----LQERAQQWGQTLQAALCLDDEAAYAE 5019
Cdd:cd05943   143 TASIGAIWSSCSPDFGVpgvlDR----FGQIEPKVLFAvdaytyngKRHdvrekVAELVKGLPSLLAVVVVPYTVAAGQP 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5020 DASNVANVNEPHDLA-------------------YVIYTSGTTGRPK-------GVMIEHRslvntaagyrREYRLdqfp 5073
Cdd:cd05943   219 DLSKIAKALTLEDFLatgaagelefeplpfdhplYILYSSGTTGLPKcivhgagGTLLQHL----------KEHIL---- 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5074 vrllqlasfSFDVFVGDI---------------ARTLYNGGTMVI---CPKddRIDPARLHYWISEEKITIFESTPALIi 5135
Cdd:cd05943   285 ---------HCDLRPGDRlfyyttcgwmmwnwlVSGLAVGATIVLydgSPF--YPDTNALWDLADEEGITVFGTSAKYL- 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5136 pfmDYVAEHGL------DMSSM-VLLITSSdSCSVTDYRVLQERFGSQFRIINAYGVTEaaidsslydepLAKLPEAGN- 5207
Cdd:cd05943   353 ---DALEKAGLkpaethDLSSLrTILSTGS-PLKPESFDYVYDHIKPDVLLASISGGTD-----------IISCFVGGNp 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5208 -VPIGKAALNAKFY-----IVDAHLNPVpVGVLGEL-CIGGI-GVARGYLNRPEltEEKFVDSPFVEGERLYRTGDLARW 5279
Cdd:cd05943   418 lLPVYRGEIQCRGLgmaveAFDEEGKPV-WGEKGELvCTKPFpSMPVGFWNDPD--GSRYRAAYFAKYPGVWAHGDWIEI 494
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5280 MPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEG-VREAVVVVREDAKGQKVLC-------AHFTAESELKL-SELR 5350
Cdd:cd05943   495 TPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEvEDSLVVGQEWKDGDERVILfvklregVELDDELRKRIrSTIR 574
                         570       580       590
                  ....*....|....*....|....*....|
gi 386647928 5351 SSLSqelPGYmIPSYFVQLEQLPLTANGKI 5380
Cdd:cd05943   575 SALS---PRH-VPAKIIAVPDIPRTLSGKK 600
PRK03584 PRK03584
acetoacetate--CoA ligase;
2359-2823 1.67e-08

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 61.73  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2359 PDHPAVVFEG-----QQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFA------------------- 2414
Cdd:PRK03584   98 DDRPAIIFRGedgprRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLAtaslgaiwsscspdfgvqg 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2415 -----------VLKA------GGAYVPIDPEYPE--DRIsymleDSSAQVLLAQrRLQERVSFAGTVVTVDDEQAYA-GD 2474
Cdd:PRK03584  178 vldrfgqiepkVLIAvdgyryGGKAFDRRAKVAElrAAL-----PSLEHVVVVP-YLGPAAAAAALPGALLWEDFLApAE 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2475 GSNLE-SAVGPNDLAYIIYTSGTTGKPK-------GVMVEH---HGL-CSLKqmfantlqinAQDRVVQFaslsfdASC- 2541
Cdd:PRK03584  252 AAELEfEPVPFDHPLWILYSSGTTGLPKcivhghgGILLEHlkeLGLhCDLG----------PGDRFFWY------TTCg 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2542 -----WEVfQTLFFGATLYI----PTKETiLDYQWfeRYMSDNGIttaTLPPTYAVYLN--------PDHMPDFKRLIAA 2604
Cdd:PRK03584  316 wmmwnWLV-SGLLVGATLVLydgsPFYPD-PNVLW--DLAAEEGV---TVFGTSAKYLDacekaglvPGETHDLSALRTI 388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2605 GSASSlELL--------QQWKDKVKYFNAYGPTEdsICT--TIWTPstedisqLKSVPIG---GPIVNHRIYIVDAHYQP 2671
Cdd:PRK03584  389 GSTGS-PLPpegfdwvyEHVKADVWLASISGGTD--ICScfVGGNP-------LLPVYRGeiqCRGLGMAVEAWDEDGRP 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2672 VpVGVAGELCIAG------VGLargyLNRPDltAEKFVDNPFE--PGerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGY 2743
Cdd:PRK03584  459 V-VGEVGELVCTKpfpsmpLGF----WNDPD--GSRYRDAYFDtfPG--VWRHGDWIEITEHGGVVIYGRSDATLNRGGV 529
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2744 RIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLcAYFVADRTMTV----------GELRGELSgelPGYmIPAHFVQLE 2813
Cdd:PRK03584  530 RIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRM-PLFVVLAEGVTlddalrarirTTIRTNLS---PRH-VPDKIIAVP 604
                         570
                  ....*....|
gi 386647928 2814 RMPLTPNGKI 2823
Cdd:PRK03584  605 DIPRTLSGKK 614
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
5961-6341 1.72e-08

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 61.78  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5961 LTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLLVQ- 6039
Cdd:PLN02861   78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQe 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6040 --------------GHLLDRASFADKLVNLNDDG--------AYHEDGS--NLEPVNGPEHLT---YVIYTSGTTGRPKG 6092
Cdd:PLN02861  158 skissilsclpkcsSNLKTIVSFGDVSSEQKEEAeelgvscfSWEEFSLmgSLDCELPPKQKTdicTIMYTSGTTGEPKG 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6093 VMVEHRNVV-------RLVKNTNYVELNEQTHI-LQTGAVVFD----------ASTFEIWGA----LLNG---------- 6140
Cdd:PLN02861  238 VILTNRAIIaevlstdHLLKVTDRVATEEDSYFsYLPLAHVYDqvietyciskGASIGFWQGdiryLMEDvqalkptifc 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6141 ------GRLYVVRNETILDAVSLKNAIQQYGIN----------TMWLTAPLYNQL--SQQDSGMFAGLKTLIVGGDVLSv 6202
Cdd:PLN02861  318 gvprvyDRIYTGIMQKISSGGMLRKKLFDFAYNyklgnlrkglKQEEASPRLDRLvfDKIKEGLGGRVRLLLSGAAPLP- 396
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6203 PHINRVLREHAGLSIVNGYGPTENTTFSTThTIVGEQKEAVPIGKPINNSTAYIVD------SKLSLLPVGvwgELIVGG 6276
Cdd:PLN02861  397 RHVEEFLRVTSCSVLSQGYGLTESCGGCFT-SIANVFSMVGTVGVPMTTIEARLESvpemgyDALSDVPRG---EICLRG 472
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 6277 DGVARGYLNRPELTAEKFVESSFlpgercyRTGDLARWLPDGTLEYkgrIDEQVKIrgYRIELGE 6341
Cdd:PLN02861  473 NTLFSGYHKRQDLTEEVLIDGWF-------HTGDIGEWQPNGAMKI---IDRKKNI--FKLSQGE 525
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
5029-5385 1.94e-08

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 61.61  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5029 EPHDLAYVIYTSGTTGRPKGVMIEHRSLV------NTAAG----YRREyrldqFPVRLLQLasfsFDVFvgdiART---- 5094
Cdd:PRK08974  204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLanleqaKAAYGpllhPGKE-----LVVTALPL----YHIF----ALTvncl 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5095 --LYNGGTMVIC--PKDdridparLHYWISEEKITIFESTPALIIPFMDYVAE---HGLDMSSMVLLITSSDSCSvtdyR 5167
Cdd:PRK08974  271 lfIELGGQNLLItnPRD-------IPGFVKELKKYPFTAITGVNTLFNALLNNeefQELDFSSLKLSVGGGMAVQ----Q 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5168 VLQERFGS--QFRIINAYGVTEAA--IDSSLYDepLAKLpeagNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIGGIG 5243
Cdd:PRK08974  340 AVAERWVKltGQYLLEGYGLTECSplVSVNPYD--LDYY----SGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQ 413
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5244 VARGYLNRPELTEEKFVDSpfvegerLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQL-LKAEGVREAVV 5322
Cdd:PRK08974  414 VMLGYWQRPEATDEVIKDG-------WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVmLHPKVLEVAAV 486
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 5323 VVREDAKGQKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK08974  487 GVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
5235-5385 2.28e-08

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 60.44  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5235 GELCIGGIGVARGYLNRPElteekfvDSPFVEgERLYRTGDLARwMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKA 5314
Cdd:PRK07824  208 GRIALGGPTLAKGYRNPVD-------PDPFAE-PGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATH 278
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 5315 EGVREAVVVVREDAK-GQKVLCAHFTAESELK-LSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PRK07824  279 PAVADCAVFGLPDDRlGQRVVAAVVGDGGPAPtLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
7849-7922 2.35e-08

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 54.47  E-value: 2.35e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  7849 EIEEQLLKIASVQETIVIARGDANGQQQLCAYFV--ADRELTVSELRGTLSQELPGYMIPSYFVQLEQMPLTPNGK 7922
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
2484-2824 2.54e-08

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 61.26  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2484 PNDLAYIIYTSGTTGKPKGVMVEHhglcslKQMFANTLQI------NAQDRVVQFASLsFDASCWEV--FQTLFFGATLY 2555
Cdd:PRK08043  364 PEDAALILFTSGSEGHPKGVVHSH------KSLLANVEQIktiadfTPNDRFMSALPL-FHSFGLTVglFTPLLTGAEVF 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2556 I-PTKetiLDYQWFERYMSDNGIT----TATLPPTYAVYLNPdhmPDFKRL---IAAGSASSLELLQQWKDK--VKYFNA 2625
Cdd:PRK08043  437 LyPSP---LHYRIVPELVYDRNCTvlfgTSTFLGNYARFANP---YDFARLryvVAGAEKLQESTKQLWQDKfgLRILEG 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2626 YGPTEDSICTTIWTPSTEDISQLKSVPIGgpivnhriyiVDAHYQPVPvGVA--GELCIAGVGLARGYL--NRPDLTAEK 2701
Cdd:PRK08043  511 YGVTECAPVVSINVPMAAKPGTVGRILPG----------MDARLLSVP-GIEqgGRLQLKGPNIMNGYLrvEKPGVLEVP 579
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2702 FVDNP---FEPGerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELgEIEEQLLKVASV--QEAIVIAHDDASGQKQ 2776
Cdd:PRK08043  580 TAENArgeMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSL-EMVEQLALGVSPdkQHATAIKSDASKGEAL 656
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 386647928 2777 LcaYFVADRTMTVGELRGEL--SGeLPGYMIPAHFVQLERMPLTPNGKID 2824
Cdd:PRK08043  657 V--LFTTDSELTREKLQQYAreHG-VPELAVPRDIRYLKQLPLLGSGKPD 703
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
5-227 2.56e-08

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 60.46  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    5 AFERETAFWNKIFEGEenPPTALPYSKAQKQAPALVRR---MSTALSKEVSERIiqMSKGAPLPAYMILLTGVqsLLYKY 81
Cdd:cd19533   184 RFERDRAFWTEQFEDL--PEPVSLARRAPGRSLAFLRRtaeLPPELTRTLLEAA--EAHGASWPSFFIALVAA--YLHRL 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   82 TSSSSILVGMPVVTKPNENRR----PVNQLVILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMteRLELQYADGV 157
Cdd:cd19533   258 TGANDVVLGVPVMGRLGAAARqtpgMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYRYEDL--RRDLGLTGEL 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  158 -----PVVNTLVALKQLHITDYR----------QSAVSDVLFEFElDKDEVRLHLTYNGNLYTESFIAQAVDHLNRLFSV 222
Cdd:cd19533   336 hplfgPTVNYMPFDYGLDFGGVVglthnlssgpTNDLSIFVYDRD-DESGLRIDFDANPALYSGEDLARHQERLLRLLEE 414

                  ....*
gi 386647928  223 VLFQP 227
Cdd:cd19533   415 AAADP 419
prpE PRK10524
propionyl-CoA synthetase; Provisional
6076-6422 2.59e-08

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 61.12  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6076 HLTYVIYTSGTTGRPKGVmveHRNV----VRLVKNTNyvelneqtHIL--QTGAVVFDAS--------TFEIWGALLNGg 6141
Cdd:PRK10524  234 EPSYILYTSGTTGKPKGV---QRDTggyaVALATSMD--------TIFggKAGETFFCASdigwvvghSYIVYAPLLAG- 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6142 rlyvvrNETIL--------DAVSLKNAIQQYGINTMWlTAP-----LYNQ----LSQQDsgmFAGLKTLIVGGDVLSVPh 6204
Cdd:PRK10524  302 ------MATIMyeglptrpDAGIWWRIVEKYKVNRMF-SAPtairvLKKQdpalLRKHD---LSSLRALFLAGEPLDEP- 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6205 INRVLREHAGLSIVNGYGPTEnttfsTTHTIVGEQK--EAVPI-----GKP--------INNSTAYIV--DSKLSL---- 6263
Cdd:PRK10524  371 TASWISEALGVPVIDNYWQTE-----TGWPILAIARgvEDRPTrlgspGVPmygynvklLNEVTGEPCgpNEKGVLvieg 445
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6264 -LPVG----VWGElivggDgvargylnrpeltaEKFVESSF-LPGERCYRTGDLARWLPDGTLEYKGRIDEQVKIRGYRI 6337
Cdd:PRK10524  446 pLPPGcmqtVWGD-----D--------------DRFVKTYWsLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRL 506
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6338 ELGEIEEQLLKVASVKEATVIVREDE-SGQKQLC------AYFVAERELTI---GELRAALSQELPNYMIPSHFVPLERM 6407
Cdd:PRK10524  507 GTREIEESISSHPAVAEVAVVGVKDAlKGQVAVAfvvpkdSDSLADREARLaleKEIMALVDSQLGAVARPARVWFVSAL 586
                         410
                  ....*....|....*
gi 386647928 6408 PLTPNGKIDRRALPA 6422
Cdd:PRK10524  587 PKTRSGKLLRRAIQA 601
PLN02654 PLN02654
acetate-CoA ligase
4910-5385 2.94e-08

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 61.07  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4910 NDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL 4989
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4990 TQT---------HLQE-------RAQQWGQTLQAALCLDDEAAYAEDASN------------VANVNEPHDLAYV----- 5036
Cdd:PLN02654  198 TCNavkrgpktiNLKDivdaaldESAKNGVSVGICLTYENQLAMKREDTKwqegrdvwwqdvVPNYPTKCEVEWVdaedp 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5037 ---IYTSGTTGRPKGVMiehrslvNTAAGYRReYRLDQFpvrllqlaSFSFDVFVGDIA-----------------RTLY 5096
Cdd:PLN02654  278 lflLYTSGSTGKPKGVL-------HTTGGYMV-YTATTF--------KYAFDYKPTDVYwctadcgwitghsyvtyGPML 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5097 NGGTMVI---CPkdDRIDPARLHYWISEEKITIFESTPALIIPFM----DYVAEHglDMSSMVLLITSSDSCSVTDYRVL 5169
Cdd:PLN02654  342 NGATVLVfegAP--NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgdEYVTRH--SRKSLRVLGSVGEPINPSAWRWF 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5170 QERFG-SQFRIINAYGVTEAAidsslyDEPLAKLPEAGNVPIGKAALnaKFY-----IVDAHLNPVPVGVLGELCI---- 5239
Cdd:PLN02654  418 FNVVGdSRCPISDTWWQTETG------GFMITPLPGAWPQKPGSATF--PFFgvqpvIVDEKGKEIEGECSGYLCVkksw 489
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5240 -GGIGVARGYLNRPELTEEKfvdsPFvegERLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLK-AEGV 5317
Cdd:PLN02654  490 pGAFRTLYGDHERYETTYFK----PF---AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVShPQCA 562
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928 5318 REAVVVVREDAKGQKVLCAHFTAESELKLSELRSSL----SQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PLN02654  563 EAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
24-219 3.37e-08

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 60.41  E-value: 3.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   24 PTALPYSKAQKQAPALVRRMstaLSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSSSSILVGMPVVTKPNENRRP 103
Cdd:cd20484   205 PADRPRSSAPSFEGQTYTRR---LPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDS 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  104 -----VNQLVIlREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLEL-QYADGVPVVNTLVALKQ-LHITDYR- 175
Cdd:cd20484   282 ligyfINMLPI-RSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNIpRSQANSPVFQVAFFYQNfLQSTSLQq 360
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386647928  176 -QSAVSDVL-------------FEFELD----KDEVRLHLTYNGNLYTESFIAQAVDHLNRL 219
Cdd:cd20484   361 fLAEYQDVLsiefvegihqegeYELVLEvyeqEDRFTLNIKYNPDLFDASTIERMMEHYVKL 422
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
5950-6420 3.69e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 60.54  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5950 DHLAVTFE------DKQLTYGELNERANRLARTLRNAGVQPDQMVGL---MVErslEMVVGMIAILKAGGAYVPI----D 6016
Cdd:PRK00174   82 DKVAIIWEgddpgdSRKITYRELHREVCRFANALKSLGVKKGDRVAIympMIP---EAAVAMLACARIGAVHSVVfggfS 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6017 PDYPEDRIrymlEDSGAKLLLVqghlldrasfAD------KLVNL--NDDGA---------------------------- 6060
Cdd:PRK00174  159 AEALADRI----IDAGAKLVIT----------ADegvrggKPIPLkaNVDEAlancpsvekvivvrrtggdvdwvegrdl 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6061 -YHE--DGSNL----EPVNGpEHLTYVIYTSGTTGRPKGVMveHrnvvrlvkNT-NYVelneqTHILQTGAVVFDASTFE 6132
Cdd:PRK00174  225 wWHElvAGASDecepEPMDA-EDPLFILYTSGSTGKPKGVL--H--------TTgGYL-----VYAAMTMKYVFDYKDGD 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6133 I--------W---------GALLNGGrlyvvrneTIL---------DAVSLKNAIQQYGINTMWlTAP-----Lynqlsq 6181
Cdd:PRK00174  289 VywctadvgWvtghsyivyGPLANGA--------TTLmfegvpnypDPGRFWEVIDKHKVTIFY-TAPtairaL------ 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6182 qdsgMFAG--------LKTL-IVGgdvlSV--PhIN----RVLREHAG---LSIVNGYGPTENTTFSTTHtIVGeqkeAV 6243
Cdd:PRK00174  354 ----MKEGdehpkkydLSSLrLLG----SVgeP-INpeawEWYYKVVGgerCPIVDTWWQTETGGIMITP-LPG----AT 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6244 PIgKPINNST------AYIVDSKLSLLPVGVWGELIVGGD--GVARGYLNRPEltaeKFVESSF--LPGErcYRTGDLAR 6313
Cdd:PRK00174  420 PL-KPGSATRplpgiqPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHE----RFVKTYFstFKGM--YFTGDGAR 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6314 WLPDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDE-SGQkQLCAYFV------AERELtIGELRA 6386
Cdd:PRK00174  493 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDiKGQ-GIYAFVTlkggeePSDEL-RKELRN 570
                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 386647928 6387 ALSQELPNYMIPS--HFVPleRMPLTPNGKIDRRAL 6420
Cdd:PRK00174  571 WVRKEIGPIAKPDviQFAP--GLPKTRSGKIMRRIL 604
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
2749-2822 3.84e-08

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 53.70  E-value: 3.84e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928  2749 EIEEQLLKVASVQEAIVIA-HDDASGQKqLCAYFV--ADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGK 2822
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGvPDELKGEA-PVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
3991-4337 4.72e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 60.53  E-value: 4.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3991 VGPNHLAYVIYTSGTTGKPKGVmVEHHGLCSLKLMFANTLQMTEQDRVVQFASLSFDascWEIFKALFFGATLY------ 4064
Cdd:PTZ00237  251 VESSHPLYILYTSGTTGNSKAV-VRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIG---WVSFHGFLYGSLSLgntfvm 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4065 ----IPTSTTILDYplFESYMNENGITATILPPTYAAYLN---PD--------RMPSLKKLITGGSA--ASV-EFVQQwK 4126
Cdd:PTZ00237  327 feggIIKNKHIEDD--LWNTIEKHKVTHTLTLPKTIRYLIktdPEatiirskyDLSNLKEIWCGGEVieESIpEYIEN-K 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4127 DKVLYFNAYGPTEASIvTSIWDEASdslgdrKSVPI---GRPLANHRIYVVDSHNRMLPVGVAGELCIS---GVGLARGY 4200
Cdd:PTZ00237  404 LKIKSSRGYGQTEIGI-TYLYCYGH------INIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTF 476
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4201 LNRPELTAEKFvdNPFePGerMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAKIDAVQEAIVLAREDA 4280
Cdd:PTZ00237  477 YKNDEKFKQLF--SKF-PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDP 551
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 4281 NGQQQLVAYFVAQRELTAA---------ELRATMSQELPNYMIPSYFVQLAQMPLTPNGKIDRKAL 4337
Cdd:PTZ00237  552 DCYNVPIGLLVLKQDQSNQsidlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
2360-2828 5.56e-08

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 59.75  E-value: 5.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2360 DHPAVVFEGQ-----QLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRI 2434
Cdd:cd05915     9 GRKEVVSRLHtgevhRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2435 SYMLEDSSAQVLLAQRRL----QERVSFAGTVVTVDDEQAYAGDGSNLESAVGPN----------DLAYIIYTSGTTGKP 2500
Cdd:cd05915    89 AYILNHAEDKVLLFDPNLlplvEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEeadpvrvperAACGMAYTTGTTGLP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2501 KGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLS-FDASCWEVFQTLFFGATLYIPTKETILDYQWFERYMSDNGITT 2579
Cdd:cd05915   169 KGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVVPmFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2580 ATLPPTYAVYLNP-----DHMPDFKRLIAAGSASSLELLQQWK-DKVKYFNAYGPTE----DSICttIWTPSTEDISQLK 2649
Cdd:cd05915   249 AGVPTVWLALADYlestgHRLKTLRRLVVGGSAAPRSLIARFErMGVEVRQGYGLTEtspvVVQN--FVKSHLESLSEEE 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2650 SVPIGG-PIVNHRIYIVDAhYQPVPVGVAGE------LCIAGVGLARGYLNRPDLTAEkfvdNPFEPGerMYRTGDLAKW 2722
Cdd:cd05915   327 KLTLKAkTGLPIPLVRLRV-ADEEGRPVPKDgkalgeVQLKGPWITGGYYGNEEATRS----ALTPDG--FFRTGDIAVW 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2723 LPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQLCAYF----VADRTMTVGELRGELSG 2798
Cdd:cd05915   400 DEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvprgEKPTPEELNEHLLKAGF 479
                         490       500       510
                  ....*....|....*....|....*....|
gi 386647928 2799 ELPgyMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:cd05915   480 AKW--QLPDAYVFAEEIPRTSAGKFLKRAL 507
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
290-747 6.04e-08

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 59.79  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  290 ELNERANRLARTLRNA-GVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSG----------- 357
Cdd:cd05928    46 ELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKakcivtsdela 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  358 --------------TQVLLSQGHLQERVSFSGTWIRLDDEEAYHEDGSNlesvngpEHLTyVIYTSGTTGKPKGNLTTHR 423
Cdd:cd05928   126 pevdsvasecpslkTKLLVSEKSRDGWLNFKELLNEASTEHHCVETGSQ-------EPMA-IYFTSGTTGSPKMAEHSHS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  424 NI-IRVVKNTNY-IDVTGQDKLLQLSSYSFDGSTF-DIFGALLNGAkLVLVPKETVLDVAKLAGLIEKQQISVMFITTAF 500
Cdd:cd05928   198 SLgLGLKVNGRYwLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGA-CVFVHHLPRFDPLVILKTLSSYPITTFCGAPTV 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  501 FNVLV--DMNPDCLRHARAILFGGERVSvSHVRKALGHLGPGKIKHVYGPTESTVFATSYDVHEVEEGAvsipIGGPISN 578
Cdd:cd05928   277 YRMLVqqDLSSYKFPSLQHCVTGGEPLN-PEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGS----MGKASPP 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  579 TAIYIVNAQNKLQPIGVAGELCVAGD-----GLARGYLNRPDLTAEKFADNpfapgerMYRTGDLARWLPDGTIEYVGRI 653
Cdd:cd05928   352 YDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRA 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  654 DDQVKIRGFRIELGEIEAHLLKLEAI-EKATVVVRESANGE--KQLC----AYYVADRSLPANEVRSTLSQELPAYMLPS 726
Cdd:cd05928   425 DDVINSSGYRIGPFEVESALIEHPAVvESAVVSSPDPIRGEvvKAFVvlapQFLSHDPEQLTKELQQHVKSVTAPYKYPR 504
                         490       500
                  ....*....|....*....|...
gi 386647928  727 Y--FVQleQMPLTTNGKVDRRAL 747
Cdd:cd05928   505 KveFVQ--ELPKTVTGKIQRNEL 525
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
1320-1795 6.39e-08

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 59.75  E-value: 6.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1320 NDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL 1399
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1400 TQThlqeraqqwgqtlqavlcLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL 1479
Cdd:cd05939    81 FNL------------------LDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGM 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1480 DQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDridpARlHYWISEEK--ITIFEstpaliipfmdYVAEhgld 1557
Cdd:cd05939   143 RPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFS----AS-NFWDDCVKynCTIVQ-----------YIGE---- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1558 msSMELLITSSDSCSVTDYRV-----------LQERFGSQFRIINA---YGVTE------------------AAIDSSLY 1605
Cdd:cd05939   203 --ICRYLLAQPPSEEEQKHNVrlavgnglrpqIWEQFVRRFGIPQIgefYGATEgnsslvnidnhvgacgfnSRILPSVY 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1606 DEPLAKLPEAGNVPIGKAalnakfyivDAHLNPVPVGVLGELcIGGIGVAR------GYLNRPElTEEKFVDSPFVEGER 1679
Cdd:cd05939   281 PIRLIKVDEDTGELIRDS---------DGLCIPCQPGEPGLL-VGKIIQNDplrrfdGYVNEGA-TNKKIARDVFKKGDS 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1680 LYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVV--VVREDAKGQKVLCAYFTAESELKLS 1757
Cdd:cd05939   350 AFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIVDPERKVDLD 429
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 386647928 1758 ELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:cd05939   430 RFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
5945-6420 7.29e-08

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 59.50  E-value: 7.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5945 AERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRI 6024
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6025 rymledsgaklllvqGHLLDRASfADKLVNLNDDGAYHE-DGSNLEPVNGPEHLTY-------VIYTSGTTGRPKGVMVE 6096
Cdd:PRK09029   93 ---------------EELLPSLT-LDFALVLEGENTFSAlTSLHLQLVEGAHAVAWqpqrlatMTLTSGSTGLPKAAVHT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6097 HRN-------VVRLVKntnyvelneqthilqtgavvFDAST--------FE------IWGALLNGGRLyVVRNEtildav 6155
Cdd:PRK09029  157 AQAhlasaegVLSLMP--------------------FTAQDswllslplFHvsgqgiVWRWLYAGATL-VVRDK------ 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6156 slknaiqqygintmwltAPLYNQLSQ---------------QDSGMFAGLKTLIVGGdvlsvPHINRVLREHA---GLSI 6217
Cdd:PRK09029  210 -----------------QPLEQALAGcthaslvptqlwrllDNRSEPLSLKAVLLGG-----AAIPVELTEQAeqqGIRC 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6218 VNGYGPTEnttfsTTHTIVGEQKEAVP-IGKPINNSTAYIVDsklsllpvgvwGELIVGGDGVARGYLNRPELTaekfve 6296
Cdd:PRK09029  268 WCGYGLTE-----MASTVCAKRADGLAgVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV------ 325
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6297 sSFLPGERCYRTGDLARWLpDGTLEYKGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVRED-ESGQKQLcAYFVA 6375
Cdd:PRK09029  326 -PLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADaEFGQRPV-AVVES 402
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 386647928 6376 ERELTIGELRAALSQELPNYMIPshfVPLERMPLT-PNG--KIDRRAL 6420
Cdd:PRK09029  403 DSEAAVVNLAEWLQDKLARFQQP---VAYYLLPPElKNGgiKISRQAL 447
PLN02736 PLN02736
long-chain acyl-CoA synthetase
5030-5308 7.33e-08

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 59.73  E-value: 7.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5030 PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREyrLDQFPV--------------RLLQLASFSFDVFVGdiartL 5095
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS--TKFYPSdvhisylplahiyeRVNQIVMLHYGVAVG-----F 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5096 YNGGTMVICpkDDridparlhywISEEKITIFESTPALIIPFMD--------------------YVA-----EHGLDMSS 5150
Cdd:PLN02736  293 YQGDNLKLM--DD----------LAALRPTIFCSVPRLYNRIYDgitnavkesgglkerlfnaaYNAkkqalENGKNPSP 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5151 M----------------VLLITSSD---SCSVTDYrvLQERFGSqfRIINAYGVTEAAIDSSLYDE-------------- 5197
Cdd:PLN02736  361 MwdrlvfnkikaklggrVRFMSSGAsplSPDVMEF--LRICFGG--RVLEGYGMTETSCVISGMDEgdnlsghvgspnpa 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5198 ---PLAKLPEAGnvpigkaalnakfYIVDAhlNPVPvgvLGELCIGGIGVARGYLNRPELTEEkfvdspFVEGERLYRTG 5274
Cdd:PLN02736  437 cevKLVDVPEMN-------------YTSED--QPYP---RGEICVRGPIIFKGYYKDEVQTRE------VIDEDGWLHTG 492
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 386647928 5275 DLARWMPDGNVDFIGRIDNQAKI-RGYRIETGEIE 5308
Cdd:PLN02736  493 DIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIE 527
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2837-2914 7.96e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 53.41  E-value: 7.96e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   2837 AGADYVAPRSEEEKVLADVWQAVLG---AERVGATDHFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTVAQLSKH 2912
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGhaaAEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEH 81

                    ..
gi 386647928   2913 IR 2914
Cdd:smart00823   82 LA 83
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
1324-1707 8.45e-08

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 59.44  E-value: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1324 TYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ-- 1401
Cdd:PLN02430   78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQdk 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 --THLQERAQQWGQTLQAVLCL----DDEAAYAED---------------ASNVANVNEPH--DLAYVIYTSGTTGRPKG 1458
Cdd:PLN02430  158 kiKELLEPDCKSAKRLKAIVSFtsvtEEESDKASQigvktyswidflhmgKENPSETNPPKplDICTIMYTSGTSGDPKG 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1459 VMIEHRSLVNTAAGYrrEYRLDQFPVRL---------LQLAS----------FSFDVFVGdiartLYNGGTMVIcpKDDr 1519
Cdd:PLN02430  238 VVLTHEAVATFVRGV--DLFMEQFEDKMthddvylsfLPLAHildrmieeyfFRKGASVG-----YYHGDLNAL--RDD- 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1520 idparlhywISEEKITIFESTPALIIPFMD----------------YVAEHGLDMSSMELLITSSDSCSVTD---YRVLQ 1580
Cdd:PLN02430  308 ---------LMELKPTLLAGVPRVFERIHEgiqkalqelnprrrliFNALYKYKLAWMNRGYSHKKASPMADflaFRKVK 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1581 ERFGSQFR------------------------IINAYGVTEAAIDSSL-----------------YDE-PLAKLPEAGNV 1618
Cdd:PLN02430  379 AKLGGRLRllisggaplsteieeflrvtscafVVQGYGLTETLGPTTLgfpdemcmlgtvgapavYNElRLEEVPEMGYD 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1619 PIGKaalnakfyivdahlNPVpvgvlGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFI 1698
Cdd:PLN02430  459 PLGE--------------PPR-----GEICVRGKCLFSGYYKNPELTEEVMKDGWF-------HTGDIGEILPNGVLKII 512

                  ....*....
gi 386647928 1699 GRIDNQAKI 1707
Cdd:PLN02430  513 DRKKNLIKL 521
PLN02736 PLN02736
long-chain acyl-CoA synthetase
1440-1473 8.68e-08

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 59.34  E-value: 8.68e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 386647928 1440 PHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGY 1473
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGS 253
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
4910-5385 9.25e-08

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 58.98  E-value: 9.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4910 NDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLL 4989
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4990 TQthlqeraqqwgqtLQAALCLDdeaayAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNTAAGYRREYRL 5069
Cdd:cd05939    81 FN-------------LLDPLLTQ-----SSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGM 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5070 DQFPVRLLQLASFSFDVFVGDIARTLYNGGTMVICPKDDridpARlHYWISEEK--ITIFEstpaliipfmdYVAEhgld 5147
Cdd:cd05939   143 RPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFS----AS-NFWDDCVKynCTIVQ-----------YIGE---- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5148 MSSMVLLITSSDSCSVTDYRVL---------QERFGSQFRIINA---YGVTE------------------AAIDSSLYDE 5197
Cdd:cd05939   203 ICRYLLAQPPSEEEQKHNVRLAvgnglrpqiWEQFVRRFGIPQIgefYGATEgnsslvnidnhvgacgfnSRILPSVYPI 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5198 PLAKLPEAGNVPIGKAalnakfyivDAHLNPVPVGVLGELcIGGIGVAR------GYLNRPElTEEKFVDSPFVEGERLY 5271
Cdd:cd05939   283 RLIKVDEDTGELIRDS---------DGLCIPCQPGEPGLL-VGKIIQNDplrrfdGYVNEGA-TNKKIARDVFKKGDSAF 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5272 RTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVV--VVREDAKGQKVLCAHFTAESELKLSEL 5349
Cdd:cd05939   352 LSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIVDPERKVDLDRF 431
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 386647928 5350 RSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:cd05939   432 SAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
6435-6505 9.30e-08

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 53.02  E-value: 9.30e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928   6435 APRTEQEKALAAVWQ----AVLG---AERVGVTDHFFELGGDSIKSIQVSSRLHQA-GYKLEIRDLFKYPTLAQLSQHI 6505
Cdd:smart00823    4 LPPAERRRLLLDLVReqvaAVLGhaaAEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHL 82
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
6529-6732 1.01e-07

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 59.67  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6529 WFFDQsLADLHH-FNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFRKSENGYAAW-NRAIGEGELyslEVADFRDV 6606
Cdd:PRK10252   18 WMAEK-LSPLPSaWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWvDPALTFPLP---EIIDLRTQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6607 KSAE-QAVEAKANEIQSSIDLEVG-PLFKAGLFQCADGDHLL-LVIHHGVVDGVSWRILLEDVALGYEQAAKGEEVRLPA 6683
Cdd:PRK10252   94 PDPHaAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWyQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASP 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 6684 KTDsFRTWSEQLAAYAQSPAMENERAYWEQ-------IAQTAVAPLPKDKQSDRSL 6732
Cdd:PRK10252  174 FTP-FADVVEEYQRYRASEAWQRDAAFWAEqrrqlppPASLSPAPLPGRSASADIL 228
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
4913-5311 1.08e-07

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 59.36  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFML-EDSAASVLLTQ 4991
Cdd:PLN02387  107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLnETEVTTVICDS 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 THLQERAQQWGQ--TLQAALCLDDEAAYAEDA------------SNV----------ANVNEPHDLAYVIYTSGTTGRPK 5047
Cdd:PLN02387  187 KQLKKLIDISSQleTVKRVIYMDDEGVDSDSSlsgssnwtvssfSEVeklgkenpvdPDLPSPNDIAVIMYTSGSTGLPK 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5048 GVMIEHRSLVNTAAGYR--------REYRLDQFPV-RLLQLASFSFDVFVGdiARTLYnGGTMVICPKDDRI------Dp 5112
Cdd:PLN02387  267 GVMMTHGNIVATVAGVMtvvpklgkNDVYLAYLPLaHILELAAESVMAAVG--AAIGY-GSPLTLTDTSNKIkkgtkgD- 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5113 arlhywISEEKITIFESTPALIIPFMDYV-----AEHGL-----DMSSMVLLITSSDSC-----------SVTDYRVLQE 5171
Cdd:PLN02387  343 ------ASALKPTLMTAVPAILDRVRDGVrkkvdAKGGLakklfDIAYKRRLAAIEGSWfgawglekllwDALVFKKIRA 416
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5172 RFGSQFR------------------------IINAYGVTE--AAIDSSLYDEP---------------LAKLPEAGnvpi 5210
Cdd:PLN02387  417 VLGGRIRfmlsggaplsgdtqrfiniclgapIGQGYGLTEtcAGATFSEWDDTsvgrvgpplpccyvkLVSWEEGG---- 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5211 gkaalnakFYIVDAhlnPVPvgvLGELCIGGIGVARGYLNRPELTEEKF-VDSpfvEGERLYRTGDLARWMPDGNVDFIG 5289
Cdd:PLN02387  493 --------YLISDK---PMP---RGEIVIGGPSVTLGYFKNQEKTDEVYkVDE---RGMRWFYTGDIGQFHPDGCLEIID 555
                         490       500
                  ....*....|....*....|...
gi 386647928 5290 RIDNQAKIR-GYRIETGEIETQL 5311
Cdd:PLN02387  556 RKKDIVKLQhGEYVSLGKVEAAL 578
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
7937-8012 1.42e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 52.64  E-value: 1.42e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928   7937 TGADFVEPRTPVEAELARIWQEVLGIGPISVKD---NFFELGGHSLRATVLSSKVNKELNVNLPLRDIFRFPTVEALAQ 8012
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
3991-4339 1.59e-07

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 58.67  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3991 VGPNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASlSFDA---SCWEIFKALffgATLYIPT 4067
Cdd:PRK06334  180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLP-PFHAygfNSCTLFPLL---SGVPVVF 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4068 STTILDYPLFESYMNENGITATILPPTYAAYL------NPDRMPSLKKLITGGSA---ASVEFVQQWKDKVLYFNAYGPT 4138
Cdd:PRK06334  256 AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYIlktakkQESCLPSLRFVVIGGDAfkdSLYQEALKTFPHIQLRQGYGTT 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4139 EASIVTSIWDEASDslgdRKSVPIGRPLANHRIYVVdSHNRMLPV--GVAGELCISGVGLARGYLNRPEltAEKFVDnpf 4216
Cdd:PRK06334  336 ECSPVITINTVNSP----KHESCVGMPIRGMDVLIV-SEETKVPVssGETGLVLTRGTSLFSGYLGEDF--GQGFVE--- 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4217 EPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIRGYRIELGEVETQLAK---IDAVQEAIVLAREDANGQQQLVAYFVAq 4293
Cdd:PRK06334  406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgQNAADHAGPLVVCGLPGEKVRLCLFTT- 484
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 386647928 4294 RELTAAELRATM-SQELPNYMIPSYFVQLAQMPLTPNGKIDRKALPA 4339
Cdd:PRK06334  485 FPTSISEVNDILkNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
1323-1707 1.75e-07

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 58.70  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1323 LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ- 1401
Cdd:PLN02861   78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQe 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1402 --------------THL-------------QERAQQWGqtlqaVLCLDDEAaYAEDASNVANVNEPH--DLAYVIYTSGT 1452
Cdd:PLN02861  158 skissilsclpkcsSNLktivsfgdvsseqKEEAEELG-----VSCFSWEE-FSLMGSLDCELPPKQktDICTIMYTSGT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1453 TGRPKGVMIEHRSLVNTAAGYRREYRL--------DQFpVRLLQLASFsFDVFVGDIArtLYNGGTMVICPKDDRIdpar 1524
Cdd:PLN02861  232 TGEPKGVILTNRAIIAEVLSTDHLLKVtdrvateeDSY-FSYLPLAHV-YDQVIETYC--ISKGASIGFWQGDIRY---- 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1525 LHYWISEEKITIFESTP------------------ALIIPFMDYVAEHGLdmSSMELLITSSDSCSVTDYRV---LQERF 1583
Cdd:PLN02861  304 LMEDVQALKPTIFCGVPrvydriytgimqkissggMLRKKLFDFAYNYKL--GNLRKGLKQEEASPRLDRLVfdkIKEGL 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1584 GSQFRII------------------------NAYGVTE--AAIDSSLYDEplakLPEAGNVPIGKAALNAKFYIV----- 1632
Cdd:PLN02861  382 GGRVRLLlsgaaplprhveeflrvtscsvlsQGYGLTEscGGCFTSIANV----FSMVGTVGVPMTTIEARLESVpemgy 457
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 1633 DAhLNPVPvgvLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQAKI 1707
Cdd:PLN02861  458 DA-LSDVP---RGEICLRGNTLFSGYHKRQDLTEEVLIDGWF-------HTGDIGEWQPNGAMKIIDRKKNIFKL 521
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
2489-2828 1.78e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 58.60  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2489 YIIYTSGTTGKPKGVmVEHHG--LCSLKqMFANTLQINAQDRVVqfasLSFDASCWEVFQTLFFGATLY----------I 2556
Cdd:PTZ00237  258 YILYTSGTTGNSKAV-VRSNGphLVGLK-YYWRSIIEKDIPTVV----FSHSSIGWVSFHGFLYGSLSLgntfvmfeggI 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2557 PTKETILDYQWfeRYMSDNGITTA-TLPPTYAVYLNPDhmPDFKRLIAAGSASSL---------------ELLQQwKDKV 2620
Cdd:PTZ00237  332 IKNKHIEDDLW--NTIEKHKVTHTlTLPKTIRYLIKTD--PEATIIRSKYDLSNLkeiwcggevieesipEYIEN-KLKI 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2621 KYFNAYGPTEdSICTTIWTPSTEDIsQLKSVPIGGPIVNHRIYIVDAhyQPVPVGVAGELCIA---GVGLARGYLNRPDL 2697
Cdd:PTZ00237  407 KSSRGYGQTE-IGITYLYCYGHINI-PYNATGVPSIFIKPSILSEDG--KELNVNEIGEVAFKlpmPPSFATTFYKNDEK 482
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2698 TAEKFvdNPFePGerMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLKVASVQEAIVIAHDDASGQKQL 2777
Cdd:PTZ00237  483 FKQLF--SKF-PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVP 557
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2778 CAYFV-----ADRTMTVGELRGE----LSGELPGYMIPAHFVQLERMPLTPNGKIDRKAL 2828
Cdd:PTZ00237  558 IGLLVlkqdqSNQSIDLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
762-835 2.78e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 51.87  E-value: 2.78e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928    762 EPRTELEAGIVNIWKEILKI---EKISVKDSFFELGGHSLRATTMVSRLHKELNISLPLRDVFRYPTVEKLAEAISG 835
Cdd:smart00823    8 ERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
2365-2507 3.37e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 57.68  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2365 VFEGQQ-LTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSA 2443
Cdd:PTZ00216  115 HFNETRyITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETEC 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2444 QVLL--AQR-----RLQERVSFAGTVV--------TVDDE--QAYA-----GDGSNLESAVGPN------DLAYIIYTSG 2495
Cdd:PTZ00216  195 KAIVcnGKNvpnllRLMKSGGMPNTTIiyldslpaSVDTEgcRLVAwtdvvAKGHSAGSHHPLNipenndDLALIMYTSG 274
                         170
                  ....*....|..
gi 386647928 2496 TTGKPKGVMVEH 2507
Cdd:PTZ00216  275 TTGDPKGVMHTH 286
PLN02654 PLN02654
acetate-CoA ligase
275-747 3.70e-07

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 57.60  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  275 DAVAVTFE------DRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEER 348
Cdd:PLN02654  104 DKIAIYWEgnepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  349 IRYMLEDSGTQVLLSQG---------HLQERVSFS-----------GTWIRLDDEEAYHEDGS----------------- 391
Cdd:PLN02654  184 LAQRIVDCKPKVVITCNavkrgpktiNLKDIVDAAldesakngvsvGICLTYENQLAMKREDTkwqegrdvwwqdvvpny 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  392 ----NLESVNGPEHLtYVIYTSGTTGKPKGNLTTHRNIIrVVKNTNYidvtgqdkllqlsSYSFD--------------- 452
Cdd:PLN02654  264 ptkcEVEWVDAEDPL-FLLYTSGSTGKPKGVLHTTGGYM-VYTATTF-------------KYAFDykptdvywctadcgw 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  453 --GSTFDIFGALLNGAK-LVLVPKETVLDVAKLAGLIEKQQISVMFIT-TAFFNVLVDMNPDCLRHARAIL--FG--GER 524
Cdd:PLN02654  329 itGHSYVTYGPMLNGATvLVFEGAPNYPDSGRCWDIVDKYKVTIFYTApTLVRSLMRDGDEYVTRHSRKSLrvLGsvGEP 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  525 VSVSHVRKALGHLGPGK--IKHVYGPTESTVFATSY--DVHEVEEGAVSIPIGG--PIsntaiyIVNAQNKLQPIGVAGE 598
Cdd:PLN02654  409 INPSAWRWFFNVVGDSRcpISDTWWQTETGGFMITPlpGAWPQKPGSATFPFFGvqPV------IVDEKGKEIEGECSGY 482
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  599 LCVAGD--GLARGYLNrpdlTAEKFADNPFAPGERMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKL 676
Cdd:PLN02654  483 LCVKKSwpGAFRTLYG----DHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSH 558
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  677 EAIEKATVVVRESANGEKQLCAYYVADRSLP-ANEVRSTL----SQELPAYMLPSYFVQLEQMPLTTNGKVDRRAL 747
Cdd:PLN02654  559 PQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPySEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
271-747 4.35e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 57.07  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  271 ERRPDAVAVTFE------DRQLTYGELNERANRLARTLRNAGVQADQLVGL---MV-ERSLEM-----IVGIMGILKAGg 335
Cdd:PRK00174   78 KTRGDKVAIIWEgddpgdSRKITYRELHREVCRFANALKSLGVKKGDRVAIympMIpEAAVAMlacarIGAVHSVVFGG- 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  336 ayvpIDPEYPEERIrymlEDSGTQVL----------------------LSQGHLQERV------SFSGTWIR-------- 379
Cdd:PRK00174  157 ----FSAEALADRI----IDAGAKLVitadegvrggkpiplkanvdeaLANCPSVEKVivvrrtGGDVDWVEgrdlwwhe 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  380 -LDDEEAYHEDgsnlESVNGpEHLTYVIYTSGTTGKPKGnltthrniirVVKNT-NYidvtgqdkLLQLSS---YSFD-- 452
Cdd:PRK00174  229 lVAGASDECEP----EPMDA-EDPLFILYTSGSTGKPKG----------VLHTTgGY--------LVYAAMtmkYVFDyk 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  453 ---------------GSTFDIFGALLNGAKLVL---VPkeTVLDVAKLAGLIEKQQISVmFIT--TAFfnvlvdmnpdcl 512
Cdd:PRK00174  286 dgdvywctadvgwvtGHSYIVYGPLANGATTLMfegVP--NYPDPGRFWEVIDKHKVTI-FYTapTAI------------ 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  513 rhaRAILFGGERVSVSHVRKALGHLG----PgkIK--------HVYG----PTESTVFATsydvhevEEGAVSI-PIGG- 574
Cdd:PRK00174  351 ---RALMKEGDEHPKKYDLSSLRLLGsvgeP--INpeawewyyKVVGgercPIVDTWWQT-------ETGGIMItPLPGa 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  575 ----PISNTAIY------IVNAQNKLQPIGVAGELCVAGD--GLARGYLNRPdltaEKFADNPFAPGERMYRTGDLARWL 642
Cdd:PRK00174  419 tplkPGSATRPLpgiqpaVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGARRD 494
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  643 PDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLEAIEKATVVVR-ESANGEkQLCAYYVADRSLPAN-----EVRSTLS 716
Cdd:PRK00174  495 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRpDDIKGQ-GIYAFVTLKGGEEPSdelrkELRNWVR 573
                         570       580       590
                  ....*....|....*....|....*....|...
gi 386647928  717 QELPAYMLPS--YFVqlEQMPLTTNGKVDRRAL 747
Cdd:PRK00174  574 KEIGPIAKPDviQFA--PGLPKTRSGKIMRRIL 604
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
11-142 4.36e-07

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 56.88  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   11 AFWNKIFEGEENPPTALPYSKAQKQAPALVRR--MSTALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSSSSIL 88
Cdd:cd20483   192 DFWKEKLEGIPDASKLLPFAKAERPPVKDYERstVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLT 271
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928   89 VGMPvvtkpnENRRP-----------VNqLVILREEVRDDSTFKALLGEAKNSVTSSINHQNVPF 142
Cdd:cd20483   272 IGMV------DGDRPhpdfddlvgffVN-MLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVPF 329
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
4914-5297 4.73e-07

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 57.13  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4914 TYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ-- 4991
Cdd:PLN02430   78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQdk 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 --THLQERAQQWGQTLQAALCL----DDEAAYAED---------------ASNVANVNEPH--DLAYVIYTSGTTGRPKG 5048
Cdd:PLN02430  158 kiKELLEPDCKSAKRLKAIVSFtsvtEEESDKASQigvktyswidflhmgKENPSETNPPKplDICTIMYTSGTSGDPKG 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5049 VMIEHRSLVNTAAGYrrEYRLDQFPVRL---------LQLAS----------FSFDVFVGdiartLYNGGTMVIcpKDDr 5109
Cdd:PLN02430  238 VVLTHEAVATFVRGV--DLFMEQFEDKMthddvylsfLPLAHildrmieeyfFRKGASVG-----YYHGDLNAL--RDD- 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5110 idparlhywISEEKITIFESTPALIIPFMD----------------YVAEHGLDMSSMVLLITSSDSCSVTD---YRVLQ 5170
Cdd:PLN02430  308 ---------LMELKPTLLAGVPRVFERIHEgiqkalqelnprrrliFNALYKYKLAWMNRGYSHKKASPMADflaFRKVK 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5171 ERFGSQFR------------------------IINAYGVTEAAIDSSL-----------------YDE-PLAKLPEAGNV 5208
Cdd:PLN02430  379 AKLGGRLRllisggaplsteieeflrvtscafVVQGYGLTETLGPTTLgfpdemcmlgtvgapavYNElRLEEVPEMGYD 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5209 PIGKaalnakfyivdahlNPVpvgvlGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFI 5288
Cdd:PLN02430  459 PLGE--------------PPR-----GEICVRGKCLFSGYYKNPELTEEVMKDGWF-------HTGDIGEILPNGVLKII 512

                  ....*....
gi 386647928 5289 GRIDNQAKI 5297
Cdd:PLN02430  513 DRKKNLIKL 521
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
2677-2829 5.19e-07

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 56.54  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2677 AGELCIAGVGLARGYLnrPDltaekFVDNPfepgeRMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLK 2756
Cdd:PRK07445  301 TGNITIQAQSLALGYY--PQ-----ILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 2757 VASVQEAIVIAHDDAS-GQKQLCAYFVADRTMTVGELRGELSGELPGYMIPAHFVQLERMPLTPNGKIDRKALP 2829
Cdd:PRK07445  369 TGLVQDVCVLGLPDPHwGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
7585-7846 5.25e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 57.04  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7585 PNHLAYVIYTSGTTGKPKGVMVehhglcSLKLMFAETLRITEEDRVVQF---ASLSF--DASCWE---IFKALFFGATLY 7656
Cdd:PTZ00342  303 PDFITSIVYTSGTSGKPKGVML------SNKNLYNTVVPLCKHSIFKKYnpkTHLSYlpISHIYErviAYLSFMLGGTIN 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7657 IPAKDtiLDYpLFESYMNENGITAAILPPTYA-IYLSP----DRLPSLKKLIT------------GGSAASVEFV----Q 7715
Cdd:PTZ00342  377 IWSKD--INY-FSKDIYNSKGNILAGVPKVFNrIYTNImteiNNLPPLKRFLVkkilslrksnnnGGFSKFLEGIthisS 453
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7716 QWKDK----------------------------VRYFNAYGPTEASIVTSVwaasPDGLDLRSVPIGRPIANHQIFIVDS 7767
Cdd:PTZ00342  454 KIKDKvnpnlevilngggklspkiaeelsvllnVNYYQGYGLTETTGPIFV----QHADDNNTESIGGPISPNTKYKVRT 529
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7768 -----QNHMLPvgvAGELCISGAGLARGYLNRPELTAEKFVDNPFlagermYRTGDLARWLPDGNIEYLGRIDHQVKI-R 7841
Cdd:PTZ00342  530 wetykATDTLP---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQ 600

                  ....*
gi 386647928 7842 GYRIE 7846
Cdd:PTZ00342  601 GEYIE 605
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
5932-6416 6.37e-07

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 56.90  E-value: 6.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5932 PSDKTIHQLFEEQAERI-PDHLAVT-FEDKQLTYGELNERANRLARTLRNaGVQPDQMVGLMVERSLEMVVGMIAILKAG 6009
Cdd:PRK06814  628 DYDRTLFEALIEAAKIHgFKKLAVEdPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAG 706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6010 gaYVPIdpdypedriryMLE-DSGAKLLLV------------------QGHL---------------LD----RASFADK 6051
Cdd:PRK06814  707 --RVPA-----------MINfSAGIANILSackaaqvktvltsrafieKARLgpliealefgiriiyLEdvraQIGLADK 773
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6052 LVNLNDDGAYHEdgsnLEPVNGPEHLTYVIYTSGTTGRPKGVMVEHRNVvrlvkntnyvelneQTHILQTGAV------- 6124
Cdd:PRK06814  774 IKGLLAGRFPLV----YFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNL--------------LANRAQVAARidfsped 835
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6125 -VFDA----STFEIWGA----LLNGGRLYVVRN--------ETILDAvslkNAIQQYGINTmWLT-----APLYNqlsqq 6182
Cdd:PRK06814  836 kVFNAlpvfHSFGLTGGlvlpLLSGVKVFLYPSplhyriipELIYDT----NATILFGTDT-FLNgyaryAHPYD----- 905
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6183 dsgmFAGLKTLIVGGDVLSvPHINRVLREHAGLSIVNGYGPTE-------NTTFsttHTIVGEQKEAVPIgkpinnstay 6255
Cdd:PRK06814  906 ----FRSLRYVFAGAEKVK-EETRQTWMEKFGIRILEGYGVTEtapvialNTPM---HNKAGTVGRLLPG---------- 967
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6256 iVDSKLSLLPvGV--WGELIVGGDGVARGYLNrpeltAEKfvessflPG------ERCYRTGDLARWLPDGTLEYKGRID 6327
Cdd:PRK06814  968 -IEYRLEPVP-GIdeGGRLFVRGPNVMLGYLR-----AEN-------PGvleppaDGWYDTGDIVTIDEEGFITIKGRAK 1033
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6328 EQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLcAYFVAERELTIGE-LRAALSQELPNYMIPSHFVPLER 6406
Cdd:PRK06814 1034 RFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERI-ILLTTASDATRAAfLAHAKAAGASELMVPAEIITIDE 1112
                         570
                  ....*....|
gi 386647928 6407 MPLTPNGKID 6416
Cdd:PRK06814 1113 IPLLGTGKID 1122
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
2480-2830 6.75e-07

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 56.36  E-value: 6.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2480 SAVGPNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASlSFDA---SCWEVFQTLffgATLYI 2556
Cdd:PRK06334  178 SDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLP-PFHAygfNSCTLFPLL---SGVPV 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2557 PTKETILDYQWFERYMSDNGITTATLPPTYAVYL------NPDHMPDFKRLIAAGSASSLELLQQWKD---KVKYFNAYG 2627
Cdd:PRK06334  254 VFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYIlktakkQESCLPSLRFVVIGGDAFKDSLYQEALKtfpHIQLRQGYG 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2628 PTEdsiCTTIWTPSTEDiSQLKSVPIGGPIVNHRIYIVDAH-YQPVPVGVAGELCIAGVGLARGYL-NRPdltAEKFVDn 2705
Cdd:PRK06334  334 TTE---CSPVITINTVN-SPKHESCVGMPIRGMDVLIVSEEtKVPVSSGETGLVLTRGTSLFSGYLgEDF---GQGFVE- 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2706 pfEPGERMYRTGDLAKWLPDGTIEYLGRIDHQVKIRGYRIELGEIEEQLLK---VASVQEAIVIAHDDASGQKQLCAYFV 2782
Cdd:PRK06334  406 --LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgQNAADHAGPLVVCGLPGEKVRLCLFT 483
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 2783 ADRTmTVGELRGEL-SGELPGYMIPAHFVQLERMPLTPNGKIDRKALPA 2830
Cdd:PRK06334  484 TFPT-SISEVNDILkNSKTSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
2948-3244 6.80e-07

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 56.17  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2948 HFNQSVmLHRRDGFDEAAIRKVLQKLVEHHDALRVVFhksengytAWnRAIGEGELYGLE-------VVDLKG--IEESA 3018
Cdd:cd19547    24 YFNQNV-LELVGGTDEDVLREAWRRVADRYEILRTGF--------TW-RDRAEPLQYVRDdlappwaLLDWSGedPDRRA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3019 QAVEAK-ANEIQSSIDLEAGPFVKAGLFQCADGDHLLIVIHHGVV-DGVSWRILLEDLAIGYEQAVKGEELRF-PAKtdA 3095
Cdd:cd19547    94 ELLERLlADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILlDGWCLSLIWGDVFRVYEELAHGREPQLsPCR--P 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3096 YRTWSEQL-AAYAQSPVIERelaYWKRVAQtEVQPLPKDEQvdvslQQDSESISIEWTREETEQLLKGVH---RAYNTEM 3171
Cdd:cd19547   172 YRDYVRWIrARTAQSEESER---FWREYLR-DLTPSPFSTA-----PADREGEFDTVVHEFPEQLTRLVNeaaRGYGVTT 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928 3172 NDILLAALGMAVQKWSGLDRVLVNLEGHGRESIMTDIDItrTVGWFTSKYPVVLELEQGKDISYLLKKTKEDL 3244
Cdd:cd19547   243 NAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
5956-6102 8.52e-07

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 56.15  E-value: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5956 FEDKQLTYGELNERANRLARTLRN-AGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAK 6034
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6035 LLLVQGHLLDraSFADKLVNLNDDG---------AYHEDGSNL---------EPVNG--PEHLTYV-----IYTSGTTGR 6089
Cdd:cd05938    81 VLVVAPELQE--AVEEVLPALRADGvsvwylshtSNTEGVISLldkvdaasdEPVPAslRAHVTIKspalyIYTSGTTGL 158
                         170
                  ....*....|...
gi 386647928 6090 PKGVMVEHRNVVR 6102
Cdd:cd05938   159 PKAARISHLRVLQ 171
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
7467-7609 8.67e-07

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 56.15  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7467 FENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQ 7545
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7546 VLLTQRHLQE--------------CVSFDGKVIAADDEQAYGE--DGSNLEPVVG-------PNHLAYVIYTSGTTGKPK 7602
Cdd:cd05938    81 VLVVAPELQEaveevlpalradgvSVWYLSHTSNTEGVISLLDkvDAASDEPVPAslrahvtIKSPALYIYTSGTTGLPK 160

                  ....*..
gi 386647928 7603 GVMVEHH 7609
Cdd:cd05938   161 AARISHL 167
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
1586-1796 8.77e-07

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 55.77  E-value: 8.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1586 QFRIINAYGVTEAA--IDSSLYDEPLAklpeaGNVPIGKAALNAKFYIVDAHLnpvpvgvlGELCIGGIGVARGYLnrPE 1663
Cdd:PRK07445  254 QLRLAPTYGMTETAsqIATLKPDDFLA-----GNNSSGQVLPHAQITIPANQT--------GNITIQAQSLALGYY--PQ 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1664 lteekFVDSPfvegeRLYRTGDLARWMPDGNVDFIGRidNQAKI--RGYRIETGEIETQLLKAEGVREAVVVVREDAK-G 1740
Cdd:PRK07445  319 -----ILDSQ-----GIFETDDLGYLDAQGYLHILGR--NSQKIitGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwG 386
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1741 QKVLCAYFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALP 1796
Cdd:PRK07445  387 EVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
prpE PRK10524
propionyl-CoA synthetase; Provisional
2355-2503 9.86e-07

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 56.11  E-value: 9.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2355 AERiPDHPAVVF------EGQQLTYRELNERANRLARTLQALGVKTDQPV----GLMLERSLEM------------VVGM 2412
Cdd:PRK10524   64 AKR-PEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVliymPMIAEAAFAMlacarigaihsvVFGG 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2413 FA---------------VLKA-----GGAYVPIDPEYpeDRISYMLEDSSAQVLLAQRRLQERVSFAGTVVTVDDEQAYA 2472
Cdd:PRK10524  143 FAshslaariddakpvlIVSAdagsrGGKVVPYKPLL--DEAIALAQHKPRHVLLVDRGLAPMARVAGRDVDYATLRAQH 220
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 386647928 2473 GDGSN----LESavgpNDLAYIIYTSGTTGKPKGV 2503
Cdd:PRK10524  221 LGARVpvewLES----NEPSYILYTSGTTGKPKGV 251
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
6524-6840 1.17e-06

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 55.38  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6524 TPIQRWFFDQSLadlhHFNQAFMLHR----KDRFDEAALRQVLQKLAEHHDALRTVFRKSENGyaawnraigeGEL---- 6595
Cdd:cd19545     5 TPLQEGLMALTA----RQPGAYVGQRvfelPPDIDLARLQAAWEQVVQANPILRTRIVQSDSG----------GLLqvvv 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6596 --YSLEVADFRDVKSAEQAveakaneiqssiDLEVGPLFKAGLFQCA------DGDHLLLVIHHGVVDGVSWRILLEDVA 6667
Cdd:cd19545    71 keSPISWTESTSLDEYLEE------------DRAAPMGLGGPLVRLAlvedpdTERYFVWTIHHALYDGWSLPLILRQVL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6668 lgyeQAAKGEEVRLPAktdSFRTWSEQLaAYAQSPAMENeraYWEQI---AQTAVAP-LP---KDKQSDRSLQQdsesiT 6740
Cdd:cd19545   139 ----AAYQGEPVPQPP---PFSRFVKYL-RQLDDEAAAE---FWRSYlagLDPAVFPpLPssrYQPRPDATLEH-----S 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6741 IQWSRketeqllkkvHRAYNTEMNDILLTALGMAVQKWSGLDRLLVNLEGHGRESIMTDID------ITrTVgwftskyP 6814
Cdd:cd19545   203 ISLPS----------SASSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEqivgptIA-TV-------P 264
                         330       340
                  ....*....|....*....|....*..
gi 386647928 6815 VLLQMEPGRSLSTRIKKVKEDL-RRIP 6840
Cdd:cd19545   265 LRVRIDPEQSVEDFLQTVQKDLlDMIP 291
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
4173-4337 1.32e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 55.53  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4173 VVDSHNRMLPVGVAGELCI--SGVGLARGYLNRPEltaeKFVDNPFEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIR 4250
Cdd:PRK00174  437 VVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVS 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4251 GYRIELGEVETQLAKIDAVQEAIVLAREDANGQQQLVAYFV------AQRELtAAELRATMSQELPNYMIPS--YFVQla 4322
Cdd:PRK00174  513 GHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkggeePSDEL-RKELRNWVRKEIGPIAKPDviQFAP-- 589
                         170
                  ....*....|....*
gi 386647928 4323 QMPLTPNGKIDRKAL 4337
Cdd:PRK00174  590 GLPKTRSGKIMRRIL 604
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
399-665 1.76e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 55.49  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  399 PEHLTYVIYTSGTTGKPKGNLTTHRNI----IRVVKNTNYIDVTGQDKL--LQLS-------SYS--FDGSTFDIFGALL 463
Cdd:PTZ00342  303 PDFITSIVYTSGTSGKPKGVMLSNKNLyntvVPLCKHSIFKKYNPKTHLsyLPIShiyerviAYLsfMLGGTINIWSKDI 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  464 N----------GAKLVLVPK-------ETVLDVAKLAGL---IEKQQISVM--FITTAFFNVLVDM-----------NPD 510
Cdd:PTZ00342  383 NyfskdiynskGNILAGVPKvfnriytNIMTEINNLPPLkrfLVKKILSLRksNNNGGFSKFLEGIthisskikdkvNPN 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  511 ClrhaRAILFGGERVSvSHVRKALGHLGPGKIKHVYGPTEST--VFATSYDVHEVEEgavsipIGGPISNTAIYIVNAQN 588
Cdd:PTZ00342  463 L----EVILNGGGKLS-PKIAEELSVLLNVNYYQGYGLTETTgpIFVQHADDNNTES------IGGPISPNTKYKVRTWE 531
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  589 KLQPIGV--AGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGDLARWLPDGTIEYVGRIDDQVKI-RGFRIE 665
Cdd:PTZ00342  532 TYKATDTlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
2372-2740 1.84e-06

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 55.21  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2372 TYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLAQ-- 2449
Cdd:PLN02430   78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQdk 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2450 -------------RRLQERVSFAgtvvTVDDEQAYAGDGSNLES------------------AVGPNDLAYIIYTSGTTG 2498
Cdd:PLN02430  158 kikellepdcksaKRLKAIVSFT----SVTEEESDKASQIGVKTyswidflhmgkenpsetnPPKPLDICTIMYTSGTSG 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2499 KPKGVMVEHHGLCSLKQ---MFANTLQ--INAQDRVVQFASLS--FDascwEVFQTLFF--GATL-------------YI 2556
Cdd:PLN02430  234 DPKGVVLTHEAVATFVRgvdLFMEQFEdkMTHDDVYLSFLPLAhiLD----RMIEEYFFrkGASVgyyhgdlnalrddLM 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2557 PTKETILD--YQWFERYMsdNGITTA--TLPPT-----YAVY------LNPDH-------MPDF-------------KRL 2601
Cdd:PLN02430  310 ELKPTLLAgvPRVFERIH--EGIQKAlqELNPRrrlifNALYkyklawMNRGYshkkaspMADFlafrkvkaklggrLRL 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2602 IAAGSAS-SLELLQQWKDKVKYF--NAYGPTEDSICTTIWTPstEDISQLKSVpiGGPIVNHRIY---IVDAHYQPVPVG 2675
Cdd:PLN02430  388 LISGGAPlSTEIEEFLRVTSCAFvvQGYGLTETLGPTTLGFP--DEMCMLGTV--GAPAVYNELRleeVPEMGYDPLGEP 463
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 2676 VAGELCIAGVGLARGYLNRPDLTAEKFVDNPFEpgermyrTGDLAKWLPDGTIEYLGRIDHQVKI 2740
Cdd:PLN02430  464 PRGEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEILPNGVLKIIDRKKNLIKL 521
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
4913-5297 1.87e-06

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 55.23  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4913 LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDRIQFMLEDSAASVLLTQ- 4991
Cdd:PLN02861   78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQe 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4992 --------------THL-------------QERAQQWGQTlqaalCLDDEAaYAEDASNVANVNEPH--DLAYVIYTSGT 5042
Cdd:PLN02861  158 skissilsclpkcsSNLktivsfgdvsseqKEEAEELGVS-----CFSWEE-FSLMGSLDCELPPKQktDICTIMYTSGT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5043 TGRPKGVMIEHRSLVNTAAGYRREYRL--------DQFpVRLLQLASFsFDVFVGDIArtLYNGGTMVICPKDDRIdpar 5114
Cdd:PLN02861  232 TGEPKGVILTNRAIIAEVLSTDHLLKVtdrvateeDSY-FSYLPLAHV-YDQVIETYC--ISKGASIGFWQGDIRY---- 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5115 LHYWISEEKITIFESTP------------------ALIIPFMDYVAEHGLdmSSMVLLITSSDSCSVTDYRV---LQERF 5173
Cdd:PLN02861  304 LMEDVQALKPTIFCGVPrvydriytgimqkissggMLRKKLFDFAYNYKL--GNLRKGLKQEEASPRLDRLVfdkIKEGL 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5174 GSQFRII------------------------NAYGVTE--AAIDSSLYDEplakLPEAGNVPIGKAALNAKFYIV----- 5222
Cdd:PLN02861  382 GGRVRLLlsgaaplprhveeflrvtscsvlsQGYGLTEscGGCFTSIANV----FSMVGTVGVPMTTIEARLESVpemgy 457
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 5223 DAhLNPVPvgvLGELCIGGIGVARGYLNRPELTEEKFVDSPFvegerlyRTGDLARWMPDGNVDFIGRIDNQAKI 5297
Cdd:PLN02861  458 DA-LSDVP---RGEICLRGNTLFSGYHKRQDLTEEVLIDGWF-------HTGDIGEWQPNGAMKIIDRKKNIFKL 521
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
668-741 2.00e-06

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 49.08  E-value: 2.00e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928   668 EIEAHLLKLEAIEKATVV-VRESANGEKqLCAYYV--ADRSLPANEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGK 741
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVgVPDELKGEA-PVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
286-673 2.54e-06

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 54.74  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYML-EDSGTQVLLSQ 364
Cdd:PLN02387  107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLnETEVTTVICDS 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  365 GHLQERVSFSGTW------IRLDDEEAYHEDG------------SNLE----------SVNGPEHLTYVIYTSGTTGKPK 416
Cdd:PLN02387  187 KQLKKLIDISSQLetvkrvIYMDDEGVDSDSSlsgssnwtvssfSEVEklgkenpvdpDLPSPNDIAVIMYTSGSTGLPK 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  417 GNLTTHRNIIRVV-----------KNTNYIDVTGQDKLLQLSSYSfdgSTFDIFGALLNGAKLVL------VPKETVLDV 479
Cdd:PLN02387  267 GVMMTHGNIVATVagvmtvvpklgKNDVYLAYLPLAHILELAAES---VMAAVGAAIGYGSPLTLtdtsnkIKKGTKGDA 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  480 AKL-------------------------AGLIEKQQISVMF------ITTAFF----------NVLVdmnpdcLRHARAI 518
Cdd:PLN02387  344 SALkptlmtavpaildrvrdgvrkkvdaKGGLAKKLFDIAYkrrlaaIEGSWFgawglekllwDALV------FKKIRAV 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  519 LfGGervsvsHVRKALGHLGP--------------GKIKHVYGPTESTVFATSYDVHEVEEGAVsipiGGPISNTAIYIV 584
Cdd:PLN02387  418 L-GG------RIRFMLSGGAPlsgdtqrfiniclgAPIGQGYGLTETCAGATFSEWDDTSVGRV----GPPLPCCYVKLV 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  585 N-------AQNKLQPigvAGELCVAGDGLARGYLNRPDLTAEKFADNpfAPGERMYRTGDLARWLPDGTIEYVGRIDDQV 657
Cdd:PLN02387  487 SweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIV 561
                         490
                  ....*....|....*..
gi 386647928  658 KIR-GFRIELGEIEAHL 673
Cdd:PLN02387  562 KLQhGEYVSLGKVEAAL 578
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1449-1709 2.61e-06

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 54.38  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1449 TSGTTGRPKGVM-----------IEHRSLvnTAAGYRREyrlDqfpvrLLQLAsFSFDVFVGdiARTLYNG----GTMVI 1513
Cdd:COG1541    91 SSGTTGKPTVVGytrkdldrwaeLFARSL--RAAGVRPG---D-----RVQNA-FGYGLFTG--GLGLHYGaerlGATVI 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1514 cpkddRI---DPARLHYWISEEKITIFESTP--ALIIpfMDYVAEHGLDM--SSMELLITSSDSCSVTDYRVLQERFGSq 1586
Cdd:COG1541   158 -----PAgggNTERQLRLMQDFGPTVLVGTPsyLLYL--AEVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERWGI- 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1587 fRIINAYGVTE----AAIDSSlyDEPLAKLPEagnvpigkaalnAKFY--IVD-AHLNPVPVGVLGELCIGGigvargyl 1659
Cdd:COG1541   230 -KAYDIYGLTEvgpgVAYECE--AQDGLHIWE------------DHFLveIIDpETGEPVPEGEEGELVVTT-------- 286
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 1660 nrpeLTEEkfvDSPFVegeRlYRTGDLARWMPD-----------GNVdfIGRIDNQAKIRG 1709
Cdd:COG1541   287 ----LTKE---AMPLI---R-YRTGDLTRLLPEpcpcgrthpriGRI--LGRADDMLIIRG 334
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
3875-4017 3.43e-06

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 54.22  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3875 FEKSQLTYGELNERANRLARTLRD-AGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQ 3953
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3954 ALLTQRHLRE--------------RVSFAGTFVAVDDEQAYHA--DGSNLEPVVG-------PNHLAYVIYTSGTTGKPK 4010
Cdd:cd05938    81 VLVVAPELQEaveevlpalradgvSVWYLSHTSNTEGVISLLDkvDAASDEPVPAslrahvtIKSPALYIYTSGTTGLPK 160

                  ....*..
gi 386647928 4011 GVMVEHH 4017
Cdd:cd05938   161 AARISHL 167
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
3993-4255 4.40e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 53.95  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3993 PNHLAYVIYTSGTTGKPKGVMVEHHGL---------CSLKLMFANTLQMTE------QDRVVQFASL---------SFDA 4048
Cdd:PTZ00342  303 PDFITSIVYTSGTSGKPKGVMLSNKNLyntvvplckHSIFKKYNPKTHLSYlpishiYERVIAYLSFmlggtiniwSKDI 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4049 SCW--EIF--KALFFGAT------LYIPTSTTILDYPLFESYM----------NENGITATILPPT--YAAYLNPDRMPS 4106
Cdd:PTZ00342  383 NYFskDIYnsKGNILAGVpkvfnrIYTNIMTEINNLPPLKRFLvkkilslrksNNNGGFSKFLEGIthISSKIKDKVNPN 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4107 LKKLITGGSAASVEFVQQWKD--KVLYFNAYGPTEAS---IVTSIWDEASDSlgdrksvpIGRPLANHRIYVVDS----- 4176
Cdd:PTZ00342  463 LEVILNGGGKLSPKIAEELSVllNVNYYQGYGLTETTgpiFVQHADDNNTES--------IGGPISPNTKYKVRTwetyk 534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4177 HNRMLPvgvAGELCISGVGLARGYLNRPELTAEKFVDNPFepgermYRTGDLVRWLPDGNLEYLGRIDHQVKI-RGYRIE 4255
Cdd:PTZ00342  535 ATDTLP---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
3880-4066 4.88e-06

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 53.90  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYMLEDSGAQALL--T 3957
Cdd:cd05933     9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVveN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3958 QR-------------HLRERVSFAGTF-----------------VAVDDEQaYHADGSNLEPvvgpNHLAYVIYTSGTTG 4007
Cdd:cd05933    89 QKqlqkilqiqdklpHLKAIIQYKEPLkekepnlyswdefmelgRSIPDEQ-LDAIISSQKP----NQCCTLIYTSGTTG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4008 KPKGVMVEHHGLCSLKLMFANTLQMTE----QDRVVQFASLSF-DASCWEIFKALFFGATLYIP 4066
Cdd:cd05933   164 MPKGVMLSHDNITWTAKAASQHMDLRPatvgQESVVSYLPLSHiAAQILDIWLPIKVGGQVYFA 227
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
1437-1795 5.54e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 53.59  E-value: 5.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1437 VNEPHDLaYVIYTSGTTGRPKGVMiehRS----LVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMV 1512
Cdd:PTZ00237  251 VESSHPL-YILYTSGTTGNSKAVV---RSngphLVGLKYYWRSIIEKDI-PTVVFSHSSIGWVSFHGFLYGSLSLGNTFV 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1513 ------ICPKDDRIDparlhYW--ISEEKITIFESTPALIIPF--MDYVAEH---GLDMSSMELLITSSDSC--SVTDYr 1577
Cdd:PTZ00237  326 mfeggiIKNKHIEDD-----LWntIEKHKVTHTLTLPKTIRYLikTDPEATIirsKYDLSNLKEIWCGGEVIeeSIPEY- 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1578 vLQERFGSqfRIINAYGVTEAAIdSSLYDEPLAKLPeagNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIG---GIGV 1654
Cdd:PTZ00237  400 -IENKLKI--KSSRGYGQTEIGI-TYLYCYGHINIP---YNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSF 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1655 ARGYLNRPELTEEKFVDSPfvegeRLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVV 1734
Cdd:PTZ00237  473 ATTFYKNDEKFKQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIG 547
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1735 REDAKGQKVLCAYFT-----AESELKLSELRSS----LSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 1795
Cdd:PTZ00237  548 IYDPDCYNVPIGLLVlkqdqSNQSIDLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
PRK09192 PRK09192
fatty acyl-AMP ligase;
284-423 6.61e-06

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 53.47  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  284 RQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPID-P------EYPEERIRYMLEDS 356
Cdd:PRK09192   48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPmgfggrESYIAQLRGMLASA 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928  357 GTQVLLSQGHLQERVS---------FSGTWIRLDDEEAyheDGSNLeSVNGPEHLTYVIYTSGTTGKPKGNLTTHR 423
Cdd:PRK09192  128 QPAAIITPDELLPWVNeathgnpllHVLSHAWFKALPE---ADVAL-PRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
PLN02736 PLN02736
long-chain acyl-CoA synthetase
2340-2733 7.13e-06

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 53.18  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2340 DYEADKTIHQLFEEQAERIPDHP---------AVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVV 2410
Cdd:PLN02736   39 DHPEIGTLHDNFVYAVETFRDYKylgtrirvdGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2411 gmfaVLKAGGAY----VPIDPEYPEDRISYMLEDSSAQ-VLLAQRRLQERVSFAGTVVTVDDEQAYAGDGSNLES----- 2480
Cdd:PLN02736  119 ----VDHACSAYsyvsVPLYDTLGPDAVKFIVNHAEVAaIFCVPQTLNTLLSCLSEIPSVRLIVVVGGADEPLPSlpsgt 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2481 -----------AVG-----------PNDLAYIIYTSGTTGKPKGVMVEHHGLCSLKQMFANTLQINAQDRVVQFASLsfd 2538
Cdd:PLN02736  195 gveivtyskllAQGrsspqpfrppkPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPL--- 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2539 ASCWE---VFQTLFFGATLYIptketildYQW-FERYMSDngitTATLPPT------------YAVYLN----------- 2591
Cdd:PLN02736  272 AHIYErvnQIVMLHYGVAVGF--------YQGdNLKLMDD----LAALRPTifcsvprlynriYDGITNavkesgglker 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2592 ------------------PDHMPD---FK----------RLIAAG----SASSLELLqqwkdKVKY----FNAYGPTEDS 2632
Cdd:PLN02736  340 lfnaaynakkqalengknPSPMWDrlvFNkikaklggrvRFMSSGasplSPDVMEFL-----RICFggrvLEGYGMTETS 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2633 iCTTiwtpSTEDISQLKSVPIGGPIVNHRIYIVDA---HY----QPVPvgvAGELCIAGVGLARGYLNRPDLTAEkFVDN 2705
Cdd:PLN02736  415 -CVI----SGMDEGDNLSGHVGSPNPACEVKLVDVpemNYtsedQPYP---RGEICVRGPIIFKGYYKDEVQTRE-VIDE 485
                         490       500
                  ....*....|....*....|....*...
gi 386647928 2706 pfepgERMYRTGDLAKWLPDGTIEYLGR 2733
Cdd:PLN02736  486 -----DGWLHTGDIGLWLPGGRLKIIDR 508
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
7585-7924 7.23e-06

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 53.18  E-value: 7.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7585 PNHLAYVIYTSGTTGKPKGVMVEHHGLcslkLMFAETLR----ITEEDRVVQFASL--SFDASCwEIFKALFFGATLYI- 7657
Cdd:PRK08043  364 PEDAALILFTSGSEGHPKGVVHSHKSL----LANVEQIKtiadFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLy 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7658 PAKdtiLDYPLFESYMNENGITAAILPPT----YAIYLSPDRLPSLKKLITGGSAASVEFVQQWKDK--VRYFNAYGPTE 7731
Cdd:PRK08043  439 PSP---LHYRIVPELVYDRNCTVLFGTSTflgnYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKfgLRILEGYGVTE 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7732 ASIVTSV---WAASPDgldlrsvPIGRPIANhqifiVDSQnhMLPV-GVA--GELCISGAGLARGYL--NRPELTAEKFV 7803
Cdd:PRK08043  516 CAPVVSInvpMAAKPG-------TVGRILPG-----MDAR--LLSVpGIEqgGRLQLKGPNIMNGYLrvEKPGVLEVPTA 581
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7804 DNPflAGER---MYRTGDLARWLPDGNIEYLGRIDHQVKIRGYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLcAY 7880
Cdd:PRK08043  582 ENA--RGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEAL-VL 658
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 386647928 7881 FVADRELTvselRGTLSQE-----LPGYMIPSYFVQLEQMPLTPNGKID 7924
Cdd:PRK08043  659 FTTDSELT----REKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPD 703
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
7764-7925 8.15e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 53.22  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7764 IVDSQNHMLPVGVAGELCI--SGAGLARGYLNRPEltaeKFVDNPFLAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIR 7841
Cdd:PRK00174  437 VVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVS 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7842 GYRIELGEIEEQLLKIASVQETIVIARGDANGQQQLCAYFV------ADRELtVSELRGTLSQEL-----PGYMipsYFV 7910
Cdd:PRK00174  513 GHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkggeePSDEL-RKELRNWVRKEIgpiakPDVI---QFA 588
                         170
                  ....*....|....*
gi 386647928 7911 qlEQMPLTPNGKIDR 7925
Cdd:PRK00174  589 --PGLPKTRSGKIMR 601
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
596-748 8.15e-06

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 52.69  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  596 AGELCVAGDGLARGYLnrPDltaekFADNPfapgeRMYRTGDLARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLK 675
Cdd:PRK07445  301 TGNITIQAQSLALGYY--PQ-----ILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386647928  676 LEAIEKATVV-VRESANGEkQLCAYYVADRSLPA-NEVRSTLSQELPAYMLPSYFVQLEQMPLTTNGKVDRRALP 748
Cdd:PRK07445  369 TGLVQDVCVLgLPDPHWGE-VVTAIYVPKDPSISlEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
5210-5385 8.83e-06

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 52.85  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5210 IGKAALNAKFYIVDAHLNPVPVGVLGELCI-----GGIGVARGYLNRPELTEEkfvdspfVEGERLYRTGDLARWMPDGN 5284
Cdd:cd05928   345 MGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAA-------TIRGDFYLTGDRGIMDEDGY 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5285 VDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED------AKGQKVLCAHFTAESELKLS-ELRSSLSQEL 5357
Cdd:cd05928   418 FWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDpirgevVKAFVVLAPQFLSHDPEQLTkELQQHVKSVT 497
                         170       180       190
                  ....*....|....*....|....*....|
gi 386647928 5358 PGYMIPSY--FVQleQLPLTANGKIDRKAL 5385
Cdd:cd05928   498 APYKYPRKveFVQ--ELPKTVTGKIQRNEL 525
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
253-740 9.40e-06

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 52.84  E-value: 9.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  253 GTDYPRDTTIHRLFEEqaerrpdavavtFEdrQLTYGELNERANRLARTLR-NAGVQADQLVGLMVERSLEMIVGIMGIL 331
Cdd:cd17632    49 VTDPATGRTTLRLLPR------------FE--TITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALT 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  332 KAGGAYVPIDPEYPEERIRYMLEDSGTQVL-LSQGHL-----------------------------------QERVSFSG 375
Cdd:cd17632   115 RLGAVSVPLQAGASAAQLAPILAETEPRLLaVSAEHLdlaveavleggtpprlvvfdhrpevdahraalesaRERLAAVG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  376 TWIRLDDEEAYHEDGSNLESVNGPE----HLTYVIYTSGTTGKPKGNLTTHRNIIRV-VKNTNYIDVTGQDK-LLQLSSY 449
Cdd:cd17632   195 IPVTTLTLIAVRGRDLPPAPLFRPEpdddPLALLIYTSGSTGTPKGAMYTERLVATFwLKVSSIQDIRPPASiTLNFMPM 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  450 SFDGSTFDIFGALLNGAKLVLVPK---ETVLD------------VAKLAGLIEKQQISVMFITTAFFNVLVDMNPDCLRH 514
Cdd:cd17632   275 SHIAGRISLYGTLARGGTAYFAAAsdmSTLFDdlalvrptelflVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAE 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  515 ARAILFGGervsvshvRKALGHLGPGKIKhvygpTESTVFATS-YDVHeVEEGAVSIPIGGPISNTAIyivnaqnkLQP- 592
Cdd:cd17632   355 LRERVLGG--------RLLAAVCGSAPLS-----AEMKAFMESlLDLD-LHDGYGSTEAGAVILDGVI--------VRPp 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  593 ------IGVA-------------GELCVAGDGLARGYLNRPDLTAEKFADNPFapgermYRTGD-LARWLPDgTIEYVGR 652
Cdd:cd17632   413 vldyklVDVPelgyfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDvMAELGPD-RLVYVDR 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  653 IDDQVKirgfrIELGEIEAhLLKLEAIEKATVVVRE---SANGEKQ-LCAYYV----ADRSLPANEVRSTLSQ------- 717
Cdd:cd17632   486 RNNVLK-----LSQGEFVT-VARLEAVFAASPLVRQifvYGNSERAyLLAVVVptqdALAGEDTARLRAALAEslqriar 559
                         570       580
                  ....*....|....*....|....*.
gi 386647928  718 --ELPAYMLPSYFVqLEQMPLT-TNG 740
Cdd:cd17632   560 eaGLQSYEIPRDFL-IETEPFTiANG 584
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
5039-5299 1.02e-05

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 52.46  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5039 TSGTTGRPKGVM-----------IEHRSLvnTAAGYRREyrlDqfpvrLLQLAsFSFDVFVGdiARTLYNG----GTMVI 5103
Cdd:COG1541    91 SSGTTGKPTVVGytrkdldrwaeLFARSL--RAAGVRPG---D-----RVQNA-FGYGLFTG--GLGLHYGaerlGATVI 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5104 cpkddRI---DPARLHYWISEEKITIFESTP--ALIIpfMDYVAEHGLDMSSMVL--LITSSDSCSVTDYRVLQERFGSq 5176
Cdd:COG1541   158 -----PAgggNTERQLRLMQDFGPTVLVGTPsyLLYL--AEVAEEEGIDPRDLSLkkGIFGGEPWSEEMRKEIEERWGI- 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5177 fRIINAYGVTE----AAIDSSlyDEPLAKLPEAgnvpigkaalnaKFY--IVD-AHLNPVPVGVLGELCIGGigvargyl 5249
Cdd:COG1541   230 -KAYDIYGLTEvgpgVAYECE--AQDGLHIWED------------HFLveIIDpETGEPVPEGEEGELVVTT-------- 286
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386647928 5250 nrpeLTEEkfvDSPFVegeRlYRTGDLARWMPD-----------GNVdfIGRIDNQAKIRG 5299
Cdd:COG1541   287 ----LTKE---AMPLI---R-YRTGDLTRLLPEpcpcgrthpriGRI--LGRADDMLIIRG 334
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
5027-5385 1.06e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 52.82  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5027 VNEPHDLaYVIYTSGTTGRPKGVMiehRS----LVNTAAGYRREYRLDQfPVRLLQLASFSFDVFVGDIARTLYNGGTMV 5102
Cdd:PTZ00237  251 VESSHPL-YILYTSGTTGNSKAVV---RSngphLVGLKYYWRSIIEKDI-PTVVFSHSSIGWVSFHGFLYGSLSLGNTFV 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5103 ------ICPKDDRIDparlhYW--ISEEKITIFESTPALIIPF--MDYVAEH---GLDMSSMVLLITSSDSC--SVTDYr 5167
Cdd:PTZ00237  326 mfeggiIKNKHIEDD-----LWntIEKHKVTHTLTLPKTIRYLikTDPEATIirsKYDLSNLKEIWCGGEVIeeSIPEY- 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5168 vLQERFGSqfRIINAYGVTEAAIdSSLYDEPLAKLPeagNVPIGKAALNAKFYIVDAHLNPVPVGVLGELCIG---GIGV 5244
Cdd:PTZ00237  400 -IENKLKI--KSSRGYGQTEIGI-TYLYCYGHINIP---YNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSF 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5245 ARGYLNRPELTEEKFVDSPfvegeRLYRTGDLARWMPDGNVDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVV 5324
Cdd:PTZ00237  473 ATTFYKNDEKFKQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIG 547
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5325 REDAKGQKVLCAHFT-----AESELKLSELRSS----LSQELPGYMIPSYFVQLEQLPLTANGKIDRKAL 5385
Cdd:PTZ00237  548 IYDPDCYNVPIGLLVlkqdqSNQSIDLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
5176-5386 1.13e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 52.30  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5176 QFRIINAYGVTEAA--IDSSLYDEPLAklpeaGNVPIGKAALNAKFYIVDAHLnpvpvgvlGELCIGGIGVARGYLnrPE 5253
Cdd:PRK07445  254 QLRLAPTYGMTETAsqIATLKPDDFLA-----GNNSSGQVLPHAQITIPANQT--------GNITIQAQSLALGYY--PQ 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5254 lteekFVDSPfvegeRLYRTGDLARWMPDGNVDFIGRidNQAKI--RGYRIETGEIETQLLKAEGVREAVVVVREDAK-G 5330
Cdd:PRK07445  319 -----ILDSQ-----GIFETDDLGYLDAQGYLHILGR--NSQKIitGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwG 386
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 5331 QKVLCAHFTAESELKLSELRSSLSQELPGYMIPSYFVQLEQLPLTANGKIDRKALP 5386
Cdd:PRK07445  387 EVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1620-1795 1.31e-05

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 52.08  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1620 IGKAALNAKFYIVDAHLNPVPVGVLGELCI-----GGIGVARGYLNRPELTEEkfvdspfVEGERLYRTGDLARWMPDGN 1694
Cdd:cd05928   345 MGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAA-------TIRGDFYLTGDRGIMDEDGY 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1695 VDFIGRIDNQAKIRGYRIETGEIETQLLKAEGVREAVVVVRED------AKGQKVLCAYFTAESELKLS-ELRSSLSQEL 1767
Cdd:cd05928   418 FWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDpirgevVKAFVVLAPQFLSHDPEQLTkELQQHVKSVT 497
                         170       180       190
                  ....*....|....*....|....*....|
gi 386647928 1768 PGYMIPSY--FVQleQLPLTANGKIDRKAL 1795
Cdd:cd05928   498 APYKYPRKveFVQ--ELPKTVTGKIQRNEL 525
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
9-152 1.34e-05

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 52.10  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    9 ETAFWNKIFEGEEnPPTALPYSKAQKQAPAlvRRMST---ALSKEVSERIIQMSKGAPLPAYMILLTGVQSLLYKYTSSS 85
Cdd:cd19546   194 QIAYWRDALAGAP-DELELPTDRPRPVLPS--RRAGAvplRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGT 270
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386647928   86 SILVGMpVVTKPNENRR------PVNQLVILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERLELQ 152
Cdd:cd19546   271 DVTVGT-VLPRDDEEGDlegmvgPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALP 342
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2937-3121 1.49e-05

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 51.88  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2937 WFFEPQFAEPHHFNQSVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFhkSENGytawnrAIGEGEL-----YGLEVVDL 3011
Cdd:cd20483    12 WFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAY--FEGD------DFGEQQVlddpsFHLIVIDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3012 KGIEESAQAVEAKANEIQSS-IDLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKGEEL-- 3087
Cdd:cd20483    84 SEAADPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFaLVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLat 163
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 386647928 3088 --RFPAKTDAYRTWSEQLaayAQSPVIERELAYWKR 3121
Cdd:cd20483   164 vpPPPVQYIDFTLWHNAL---LQSPLVQPLLDFWKE 196
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
2341-2507 1.71e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 52.04  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2341 YEADKTIHQLFEEQAERIPDHPAV-----------------VFEGQQL------TYRELNERANRLARTLQALGVKTDQP 2397
Cdd:PLN02387   54 WEGATTLAALFEQSCKKYSDKRLLgtrklisrefetssdgrKFEKLHLgeyewiTYGQVFERVCNFASGLVALGHNKEER 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2398 VGLMLERSLEMVVGMFAVLKAGGAYVPIDPEYPEDRISYMLEDSSAQVLLA-QRRLQERVSFAGTVVTV----------- 2465
Cdd:PLN02387  134 VAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICdSKQLKKLIDISSQLETVkrviymddegv 213
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2466 DDEQAYAGDG-------SNLE-----SAVGP-----NDLAYIIYTSGTTGKPKGVMVEH 2507
Cdd:PLN02387  214 DSDSSLSGSSnwtvssfSEVEklgkeNPVDPdlpspNDIAVIMYTSGSTGLPKGVMMTH 272
prpE PRK10524
propionyl-CoA synthetase; Provisional
7456-7604 1.86e-05

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 51.87  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7456 AERmPEKAAVVFENTQ------LTYRELNERANRLARTLRAEGVQADQPVGL---MI-ERSLEM------------IVGA 7513
Cdd:PRK10524   64 AKR-PEQLALIAVSTEtdeertYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIympMIaEAAFAMlacarigaihsvVFGG 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7514 FA---------------IMKA-----GGAYVPIDPEYPEdRIRyMLEDSGAQVLLTQRHLQECVSFDGKVIAADDEQAYG 7573
Cdd:PRK10524  143 FAshslaariddakpvlIVSAdagsrGGKVVPYKPLLDE-AIA-LAQHKPRHVLLVDRGLAPMARVAGRDVDYATLRAQH 220
                         170       180       190
                  ....*....|....*....|....*....|...
gi 386647928 7574 EDgsNLEPV--VGPNHLAYVIYTSGTTGKPKGV 7604
Cdd:PRK10524  221 LG--ARVPVewLESNEPSYILYTSGTTGKPKGV 251
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
7489-7925 1.97e-05

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 51.69  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7489 RAEGVQA-------DQPVGLMIERSLEM---IVGAFAimkAGGAyVPIDP---------EYPEDRIRYMLEDSGAQVLLT 7549
Cdd:PRK05851   40 RAENVAArlldrdrPGAVGLVGEPTVELvaaIQGAWL---AGAA-VSILPgpvrgaddgRWADATLTRFAGIGVRTVLSH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7550 QRHLQECVSFDGKVIAADDEQAYGEDGSNLEPVVGPNHLAYVIYTSGTTGKPKGVMVEHHG-LCSLKLMFAETLRITEED 7628
Cdd:PRK05851  116 GSHLERLRAVDSSVTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAvLSNLRGLNARVGLDAATD 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7629 RVVQFASLSFDASCWEIFKALFFGATLYIPAKDTILDYPL-FESYMNENG--ITAAI-----LPPTYAIYLSPDRLPSLK 7700
Cdd:PRK05851  196 VGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFSASPFrWLSWLSDSRatLTAAPnfaynLIGKYARRVSDVDLGALR 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7701 KLITGGSAASVEFVQQWKDKVRYFN--------AYGPTEASIVTSVWA----------ASPDGLDLRSVPI-GRPIANHQ 7761
Cdd:PRK05851  276 VALNGGEPVDCDGFERFATAMAPFGfdagaaapSYGLAESTCAVTVPVpgiglrvdevTTDDGSGARRHAVlGNPIPGME 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7762 IFIVDSQNhmlPVGVA----GELCISGAGLARGYLNRPELTAEKFvdnpflagermYRTGDLArWLPDGNIEYLGRIDHQ 7837
Cdd:PRK05851  356 VRISPGDG---AAGVAgreiGEIEIRGASMMSGYLGQAPIDPDDW-----------FPTGDLG-YLVDGGLVVCGRAKEL 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7838 VKIRGYRIELGEIEEQLLKIASVQETIVIARG-DANGQQQ---LCAYFV-ADRELTVSELRGTLSQELPgyMIPSYFVQL 7912
Cdd:PRK05851  421 ITVAGRNIFPTEIERVAAQVRGVREGAVVAVGtGEGSARPglvIAAEFRgPDEAGARSEVVQRVASECG--VVPSDVVFV 498
                         490
                  ....*....|....*
gi 386647928 7913 E--QMPLTPNGKIDR 7925
Cdd:PRK05851  499 ApgSLPRTSSGKLRR 513
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
7466-7626 3.20e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 51.13  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7466 VFENTQ-LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAI----MKAGGAYVPIDpeypEDRIRYMLE 7540
Cdd:PTZ00216  115 HFNETRyITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYANLG----EDALAYALR 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7541 D--------SGAQV-----LLTQRHLQECV---------SFDGK---VIAADDEQAYGEDGSNLEPVVGP---NHLAYVI 7592
Cdd:PTZ00216  191 EteckaivcNGKNVpnllrLMKSGGMPNTTiiyldslpaSVDTEgcrLVAWTDVVAKGHSAGSHHPLNIPennDDLALIM 270
                         170       180       190
                  ....*....|....*....|....*....|....
gi 386647928 7593 YTSGTTGKPKGVMVEHHGLCSLKLMFAEtlRITE 7626
Cdd:PTZ00216  271 YTSGTTGDPKGVMHTHGSLTAGILALED--RLND 302
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
1308-1467 3.75e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 51.13  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1308 ERTPEVAavvYENDR--LTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDYPSDR 1385
Cdd:PTZ00216  108 ERTMEVT---HFNETryITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDA 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1386 IQFMLEDSAASVLLTQ--------THLQEraqqwGQTLQAVL-CLD-----------------DEAAYAEDASNVANVNE 1439
Cdd:PTZ00216  185 LAYALRETECKAIVCNgknvpnllRLMKS-----GGMPNTTIiYLDslpasvdtegcrlvawtDVVAKGHSAGSHHPLNI 259
                         170       180       190
                  ....*....|....*....|....*....|.
gi 386647928 1440 P---HDLAYVIYTSGTTGRPKGVMIEHRSLV 1467
Cdd:PTZ00216  260 PennDDLALIMYTSGTTGDPKGVMHTHGSLT 290
PLN02654 PLN02654
acetate-CoA ligase
5958-6420 5.11e-05

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 50.67  E-value: 5.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5958 DKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPDYPEDRIRYMLEDSGAKLLL 6037
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6038 VQgHLLDRASfadKLVNLND--DGAYHEDGSN-------------------------------------------LEPVN 6072
Cdd:PLN02654  198 TC-NAVKRGP---KTINLKDivDAALDESAKNgvsvgicltyenqlamkredtkwqegrdvwwqdvvpnyptkceVEWVD 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6073 GPEHLtYVIYTSGTTGRPKGVmvehrnvvrlvkntnyvelneqthiLQT--GAVVFDASTFE------------------ 6132
Cdd:PLN02654  274 AEDPL-FLLYTSGSTGKPKGV-------------------------LHTtgGYMVYTATTFKyafdykptdvywctadcg 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6133 --------IWGALLNGGRLYVVRNE-TILDAVSLKNAIQQYGInTMWLTAPLYNQLSQQDSGMFA---GLKTLIVGGDVL 6200
Cdd:PLN02654  328 witghsyvTYGPMLNGATVLVFEGApNYPDSGRCWDIVDKYKV-TIFYTAPTLVRSLMRDGDEYVtrhSRKSLRVLGSVG 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6201 SV--PHINRVLREHAGLS---IVNGYGPTENTTFSTTHTIVGEQKEAVPIGKPINNSTAYIVDSKLSLLPVGVWGELIVG 6275
Cdd:PLN02654  407 EPinPSAWRWFFNVVGDSrcpISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVK 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6276 GD--GVAR---GYLNRPELTAEKFVESSFLPGERCYRTGDLARWLpdgtleyKGRIDEQVKIRGYRIELGEIEEQLLKVA 6350
Cdd:PLN02654  487 KSwpGAFRtlyGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWL-------TGRVDDVINVSGHRIGTAEVESALVSHP 559
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 6351 SVKEATVIVREDE-SGQKQLCAYFVAERELTIGELRAALSQELPN----YMIPS--HFVPleRMPLTPNGKIDRRAL 6420
Cdd:PLN02654  560 QCAEAAVVGIEHEvKGQGIYAFVTLVEGVPYSEELRKSLILTVRNqigaFAAPDkiHWAP--GLPKTRSGKIMRRIL 634
PLN02736 PLN02736
long-chain acyl-CoA synthetase
3993-4242 5.32e-05

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 50.48  E-value: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3993 PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFANTLQMTEQDRVVQFASLsfdASCWE---IFKALFFGATL--YIPT 4067
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPL---AHIYErvnQIVMLHYGVAVgfYQGD 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4068 STTILD-----YP-LFES--------YmneNGITATILPPTY-------AAY------LNPDRMPS-------------- 4106
Cdd:PLN02736  297 NLKLMDdlaalRPtIFCSvprlynriY---DGITNAVKESGGlkerlfnAAYnakkqaLENGKNPSpmwdrlvfnkikak 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4107 ----LKKLITGGSAAS---VEFVqqwkdKVLY----FNAYGPTEASIVTSIWDEasdslGDRKSVPIGRPLANHRIYVVD 4175
Cdd:PLN02736  374 lggrVRFMSSGASPLSpdvMEFL-----RICFggrvLEGYGMTETSCVISGMDE-----GDNLSGHVGSPNPACEVKLVD 443
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4176 -------SHNRMLPvgvAGELCISGVGLARGYLnRPELTAEKFVDNpfepgERMYRTGDLVRWLPDGNLEYLGR 4242
Cdd:PLN02736  444 vpemnytSEDQPYP---RGEICVRGPIIFKGYY-KDEVQTREVIDE-----DGWLHTGDIGLWLPGGRLKIIDR 508
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
4906-5057 5.93e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 50.36  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4906 VVYENDR--LTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVW------------------------- 4958
Cdd:PTZ00216  113 VTHFNETryITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWsqsmvaatvyanlgedalayalret 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4959 --KA---GGAYVPldpdypsDRIQFMLEDSA-ASVLLTQTHLQERAQQWGQTLQAALCLDDEAAYAEDASNVANVNEPHD 5032
Cdd:PTZ00216  193 ecKAivcNGKNVP-------NLLRLMKSGGMpNTTIIYLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPENNDD 265
                         170       180
                  ....*....|....*....|....*
gi 386647928 5033 LAYVIYTSGTTGRPKGVMIEHRSLV 5057
Cdd:PTZ00216  266 LALIMYTSGTTGDPKGVMHTHGSLT 290
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
6551-6683 5.99e-05

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 49.74  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6551 DRFdEAALRQVLqklaEHHDALRTVFrksengyaAWnraigEG------------ELySLEVADFRDVKSAEQAVEAKAN 6618
Cdd:cd19544    39 DAF-LAALQQVI----DRHDILRTAI--------LW-----EGlsepvqvvwrqaEL-PVEELTLDPGDDALAQLRARFD 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386647928 6619 EIQSSIDLEVGPLFKAGLFQCADGD--HLLLVIHHGVVDGVSWRILLEDVALgYEQaakGEEVRLPA 6683
Cdd:cd19544   100 PRRYRLDLRQAPLLRAHVAEDPANGrwLLLLLFHHLISDHTSLELLLEEIQA-ILA---GRAAALPP 162
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
7-149 1.23e-04

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 48.80  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    7 ERETAFWNKIFEG--EENPptaLPYSKaQKQAPALVRRMSTALS--KEVSERIIQMSK--GAPLpaYMILLTGVQSLLYK 80
Cdd:cd19538   189 ARQLAYWKKQLAGlpDEIE---LPTDY-PRPAESSYEGGTLTFEidSELHQQLLQLAKdnNVTL--FMVLQAGFAALLTR 262
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928   81 YTSSSSILVGMPVVTKPNENRRP-----VNQLViLREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTERL 149
Cdd:cd19538   263 LGAGTDIPIGSPVAGRNDDSLEDlvgffVNTLV-LRTDTSGNPSFRELLERVKETNLEAYEHQDIPFERLVEAL 335
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
6519-6715 1.31e-04

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 49.02  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6519 GEIGLTPIQR--WFFDQSLADLHHFNQAFMLHRKDRFDEAALRQVLQKLAEHHDALRTVFrkSENGYAAWNRAIG-EGEL 6595
Cdd:cd19546     3 DEVPATAGQLrtWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF--PGDGGDVHQRILDaDAAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6596 YSLEVadfrdVKSAEQAVEAK-ANEIQSSIDLEVGPLFKAGLFQCADGDH-LLLVIHHGVVDGVSWRILLEDVALGYEQA 6673
Cdd:cd19546    81 PELPV-----VPATEEELPALlADRAAHLFDLTRETPWRCTLFALSDTEHvLLLVVHRIAADDESLDVLVRDLAAAYGAR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 386647928 6674 AKG---EEVRLPAKTDSFRTWSEQLAAYAQSPamenERAYWEQIA 6715
Cdd:cd19546   156 REGrapERAPLPLQFADYALWERELLAGEDDR----DSLIGDQIA 196
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
2372-2507 1.43e-04

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 48.84  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2372 TYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGA----YVP---ID-PEYPED--RISYMLEDS 2441
Cdd:PRK07768   31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASltmlHQPtprTDlAVWAEDtlRVIGMIGAK 110
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2442 ----SAQVLLAQRRLQERvsfAGTVVTVDDEQAyAGDGSNLEsaVGPNDLAYIIYTSGTTGKPKGVMVEH 2507
Cdd:PRK07768  111 avvvGEPFLAAAPVLEEK---GIRVLTVADLLA-ADPIDPVE--TGEDDLALMQLTSGSTGSPKAVQITH 174
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
286-682 1.87e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 48.68  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  286 LTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPI-DP----------EYPEERIRYMLE 354
Cdd:PLN02861   78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLyDTlganavefiiNHAEVSIAFVQE 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  355 DSGTQVLLSQ----GHLQERVSFsGTWIRLDDEEAYH--------EDGSNLESVNG---PEHLT---YVIYTSGTTGKPK 416
Cdd:PLN02861  158 SKISSILSCLpkcsSNLKTIVSF-GDVSSEQKEEAEElgvscfswEEFSLMGSLDCelpPKQKTdicTIMYTSGTTGEPK 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  417 GNLTTHRNIIRVVKNTNY-IDVTGQDKLLQLSSYSF-----------------DGSTFDIFGA----LLNGAKLVlvpKE 474
Cdd:PLN02861  237 GVILTNRAIIAEVLSTDHlLKVTDRVATEEDSYFSYlplahvydqvietycisKGASIGFWQGdiryLMEDVQAL---KP 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  475 TVL-DVAKL-----AGLIEKQQISVMFITTAF---FNV-LVDMNPDCLRHARAILFggERVSVSHVRKALGhlgpGKI-- 542
Cdd:PLN02861  314 TIFcGVPRVydriyTGIMQKISSGGMLRKKLFdfaYNYkLGNLRKGLKQEEASPRL--DRLVFDKIKEGLG----GRVrl 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  543 ---------KHV---------------YGPTES-----TVFATSYD--------VHEVEEGAVSIPIGG--PISNTAiyi 583
Cdd:PLN02861  388 llsgaaplpRHVeeflrvtscsvlsqgYGLTEScggcfTSIANVFSmvgtvgvpMTTIEARLESVPEMGydALSDVP--- 464
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  584 vnaqnklqpigvAGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRiddqvKIRGFR 663
Cdd:PLN02861  465 ------------RGEICLRGNTLFSGYHKRQDLTEEVLIDGWF-------HTGDIGEWQPNGAMKIIDR-----KKNIFK 520
                         490
                  ....*....|....*....
gi 386647928  664 IELGEIEAhllkLEAIEKA 682
Cdd:PLN02861  521 LSQGEYVA----VENLENT 535
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
3880-4242 2.18e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 48.30  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3880 LTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAGGAYIPIDPEYPEDRIRYML----------ED 3949
Cdd:PLN02861   78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIInhaevsiafvQE 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3950 SGAQALLT-----QRHLRERVSFaGTFVAVDDEQAYHADGS-----------NLEPVVGPNH---LAYVIYTSGTTGKPK 4010
Cdd:PLN02861  158 SKISSILSclpkcSSNLKTIVSF-GDVSSEQKEEAEELGVScfsweefslmgSLDCELPPKQktdICTIMYTSGTTGEPK 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4011 GVMVEHHGLCSLKLMFANTLQMTEQ------------------DRVVQFASLSFDASC--WE------------------ 4052
Cdd:PLN02861  237 GVILTNRAIIAEVLSTDHLLKVTDRvateedsyfsylplahvyDQVIETYCISKGASIgfWQgdirylmedvqalkptif 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4053 -----IFKALFFGATLYIpTSTTILDYPLFE-SYMNENGITATILPPTYAAYLNPDRMPSLKKLITGG-------SAASV 4119
Cdd:PLN02861  317 cgvprVYDRIYTGIMQKI-SSGGMLRKKLFDfAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGrvrlllsGAAPL 395
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4120 -----EFVQQWKDKVLYfNAYGPTE--ASIVTSIWDEASdSLGdrkSVPIGRPLANHRIYVV-----DSHNRMlPvgvAG 4187
Cdd:PLN02861  396 prhveEFLRVTSCSVLS-QGYGLTEscGGCFTSIANVFS-MVG---TVGVPMTTIEARLESVpemgyDALSDV-P---RG 466
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386647928 4188 ELCISGVGLARGYLNRPELTAEKFVDNPFEpgermyrTGDLVRWLPDGNLEYLGR 4242
Cdd:PLN02861  467 EICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGDIGEWQPNGAMKIIDR 514
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
4134-4263 2.32e-04

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 48.19  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4134 AYGPTE--ASIVTSIWDEASdslgdrksvpIGR---PLANHRIYVVD-------SHNRMLPvgvAGELCISGVGLARGYL 4201
Cdd:PLN02387  451 GYGLTEtcAGATFSEWDDTS----------VGRvgpPLPCCYVKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYF 517
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 4202 NRPELTAEKF-VDnpfEPGERMYRTGDLVRWLPDGNLEYLGRIDHQVKIR-GYRIELGEVETQL 4263
Cdd:PLN02387  518 KNQEKTDEVYkVD---ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
PLN02736 PLN02736
long-chain acyl-CoA synthetase
7585-7833 2.83e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 48.17  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7585 PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKLMFAETLRITEEDRVVQFASLsfdASCWE---IFKALFFGAT------- 7654
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPL---AHIYErvnQIVMLHYGVAvgfyqgd 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7655 ---------------------LYIPAKDTI---------LDYPLFESYMN------ENGITAAILPPTYAIYLSPDRLPS 7698
Cdd:PLN02736  297 nlklmddlaalrptifcsvprLYNRIYDGItnavkesggLKERLFNAAYNakkqalENGKNPSPMWDRLVFNKIKAKLGG 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7699 LKKLITGG----SAASVEFVqqwkdKV----RYFNAYGPTEASIVTSvwaaSPDGLDLRSVPIGRPIANHQIFIVD---- 7766
Cdd:PLN02736  377 RVRFMSSGasplSPDVMEFL-----RIcfggRVLEGYGMTETSCVIS----GMDEGDNLSGHVGSPNPACEVKLVDvpem 447
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7767 ---SQNHMLPvgvAGELCISGAGLARGYLNRPELTAEKFVDNPFLagermyRTGDLARWLPDGNIEYLGR 7833
Cdd:PLN02736  448 nytSEDQPYP---RGEICVRGPIIFKGYYKDEVQTREVIDEDGWL------HTGDIGLWLPGGRLKIIDR 508
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
594-679 2.85e-04

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 47.84  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  594 GVAGElCVAGDGLargYLN---------RPDlTAEkfadnPFAPGER------------M----YRTGDLARWLPD---- 644
Cdd:COG1541   243 GVAYE-CEAQDGL---HIWedhflveiiDPE-TGE-----PVPEGEEgelvvttltkeaMplirYRTGDLTRLLPEpcpc 312
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 386647928  645 GT----IEYV-GRIDDQVKIRGFRIELGEIEAHLLKLEAI 679
Cdd:COG1541   313 GRthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEV 352
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
4361-4425 3.13e-04

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 43.01  E-value: 3.13e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928   4361 LAHIWQDVLGL---EKVGVKDNFFELGGHSLRATALASKVRKELNMELPLRHIFQFPTVEQLAEAIGQ 4425
Cdd:smart00823   17 VREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
282-689 3.46e-04

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 47.73  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  282 EDRQLTYGELNERANRLARTLRN-AGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDPEYPEERIRYMLEDSG--- 357
Cdd:cd05905    11 EATTLTWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKvrv 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  358 ---TQVLLSQGHLQERVSF-------SGTWIRLDDEEAYHEDGSNLESVNGP------EHLTYVIYTSGTTGKPKGNLTT 421
Cdd:cd05905    91 altVEACLKGLPKKLLKSKtaaeiakKKGWPKILDFVKIPKSKRSKLKKWGPhpptrdGDTAYIEYSFSSDGSLSGVAVS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  422 HRNIIRVVKNTNYIDVTGQDKLL--QLSSYSFDGSTFDIFGALLNGAKLVLVPKETVL-DVAKLAGLIEKQQISVMFITT 498
Cdd:cd05905   171 HSSLLAHCRALKEACELYESRPLvtVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKtNPLLWLQTLSQYKVRDAYVKL 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  499 AFFNVLVDMNPDCLRHARA-----------ILFGGERVSVSHVR---KALGHLG--PGKIKHVYG--------------- 547
Cdd:cd05905   251 RTLHWCLKDLSSTLASLKNrdvnlsslrmcMVPCENRPRISSCDsflKLFQTLGlsPRAVSTEFGtrvnpficwqgtsgp 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  548 -PTESTV--FATSYDVHEV-EEGAV-SIPI---GGPISNTAIYIVNAQNKLQ-PIGVAGELCVAGDGLARGYLNRPDLTA 618
Cdd:cd05905   331 ePSRVYLdmRALRHGVVRLdERDKPnSLPLqdsGKVLPGAQVAIVNPETKGLcKDGEIGEIWVNSPANASGYFLLDGETN 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  619 EKFADNP-----FAPGERMY-RTGDL----------ARWLPDGTIEYVGRIDDQVKIRGFRIELGEIEAHLLKLE----- 677
Cdd:cd05905   411 DTFKVFPstrlsTGITNNSYaRTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHpyrgr 490
                         490
                  ....*....|....*.
gi 386647928  678 -AIEKAT---VVVRES 689
Cdd:cd05905   491 cAVFSITglvVVVAEQ 506
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
7472-7637 3.75e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 47.53  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7472 LTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPI-DP----------EYPEDRIRYMLE 7540
Cdd:PLN02861   78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLyDTlganavefiiNHAEVSIAFVQE 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7541 DSGAQVLLTQR----HLQECVSFdGKVIAADDEQAYGEDGS-----------NLEPVVGPNH---LAYVIYTSGTTGKPK 7602
Cdd:PLN02861  158 SKISSILSCLPkcssNLKTIVSF-GDVSSEQKEEAEELGVScfsweefslmgSLDCELPPKQktdICTIMYTSGTTGEPK 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 386647928 7603 GVMVEHH----GLCSLKLMFAETLR-ITEEDRVVQFASLS 7637
Cdd:PLN02861  237 GVILTNRaiiaEVLSTDHLLKVTDRvATEEDSYFSYLPLA 276
PRK07868 PRK07868
acyl-CoA synthetase; Validated
1302-1415 4.52e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 47.40  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 1302 LFEKQAERTPEVAAVVYENDRLTYRELNERANRLARMLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDy 1381
Cdd:PRK07868  452 IIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPD- 530
                          90       100       110
                  ....*....|....*....|....*....|....
gi 386647928 1382 pSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTL 1415
Cdd:PRK07868  531 -TDLAAAVRLGGVTEIITDPTNLEAARQLPGRVL 563
PRK07868 PRK07868
acyl-CoA synthetase; Validated
5939-6018 4.56e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 47.40  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5939 QLFEEQAERIPDHLAVTFEDKQLTYGELNERANRLARTLRNAGVQPDQMVGLMVERSLEMVVGMIAILKAGGAYVPIDPD 6018
Cdd:PRK07868  451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPD 530
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
7585-7840 4.72e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 47.50  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7585 PNHLAYVIYTSGTTGKPKGVMVEHHGLCSLKL---MFAETL--RITEEDRVVQFASLS--FDascwEIFKALFF--GATL 7655
Cdd:PLN02430  219 PLDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdLFMEQFedKMTHDDVYLSFLPLAhiLD----RMIEEYFFrkGASV 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7656 -------------YIPAKDTIL-DYP-LFESYmnENGITAAI--LPPT-----YAIY---------------LSP----- 7693
Cdd:PLN02430  295 gyyhgdlnalrddLMELKPTLLaGVPrVFERI--HEGIQKALqeLNPRrrlifNALYkyklawmnrgyshkkASPmadfl 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7694 ------DRLPS-LKKLITGGSAASVE-----------FVQQwkdkvryfnAYGPTEASIVTSVwaASPDGLDLRSVpIGR 7755
Cdd:PLN02430  373 afrkvkAKLGGrLRLLISGGAPLSTEieeflrvtscaFVVQ---------GYGLTETLGPTTL--GFPDEMCMLGT-VGA 440
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7756 PIANHQIFIVD-SQNHMLPVGV--AGELCISGAGLARGYLNRPELTAEKFVDNPFlagermyRTGDLARWLPDGNIEYLG 7832
Cdd:PLN02430  441 PAVYNELRLEEvPEMGYDPLGEppRGEICVRGKCLFSGYYKNPELTEEVMKDGWF-------HTGDIGEILPNGVLKIID 513

                  ....*...
gi 386647928 7833 RIDHQVKI 7840
Cdd:PLN02430  514 RKKNLIKL 521
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
2952-3122 5.50e-04

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 46.70  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2952 SVMLHRRDGFDEAAIRKVLQKLVEHHDALRVVFhkSENGYTAWNRAIG-EGELYGLEVVdlKGIEESAQAVEAKANEiqS 3030
Cdd:cd19546    30 SVALRLRGRLDRDALEAALGDVAARHEILRTTF--PGDGGDVHQRILDaDAARPELPVV--PATEEELPALLADRAA--H 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3031 SIDLEAGPFVKAGLFQCADGDH-LLIVIHHGVVDGVSWRILLEDLAIGYEQAVKG---EELRFPAKTDAYRTWSEQLAAY 3106
Cdd:cd19546   104 LFDLTRETPWRCTLFALSDTEHvLLLVVHRIAADDESLDVLVRDLAAAYGARREGrapERAPLPLQFADYALWERELLAG 183
                         170
                  ....*....|....*...
gi 386647928 3107 AQSP--VIERELAYWKRV 3122
Cdd:cd19546   184 EDDRdsLIGDQIAYWRDA 201
PLN02736 PLN02736
long-chain acyl-CoA synthetase
5931-6101 5.72e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 47.02  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 5931 YPSDKTIHQLFEEQAERIPD--HLAVTFED-------KQLTYGELNERANRLARTLRNAGVQPDQMVGL-MVERSLEMVV 6000
Cdd:PLN02736   40 HPEIGTLHDNFVYAVETFRDykYLGTRIRVdgtvgeyKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLyFINRPEWLIV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6001 GMiailkAGGAY----VPIDPDYPEDRIRYML-----------------------EDSGAKLLLVQGHLLDR-----ASF 6048
Cdd:PLN02736  120 DH-----ACSAYsyvsVPLYDTLGPDAVKFIVnhaevaaifcvpqtlntllsclsEIPSVRLIVVVGGADEPlpslpSGT 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 6049 ADKLVNLNddgAYHEDG-SNLEPVNGP--EHLTYVIYTSGTTGRPKGVMVEHRNVV 6101
Cdd:PLN02736  195 GVEIVTYS---KLLAQGrSSPQPFRPPkpEDVATICYTSGTTGTPKGVVLTHGNLI 247
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
5-184 6.47e-04

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 46.68  E-value: 6.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928    5 AFERETAFWNKIFEGEENPPTALPYSKAqKQAPALVR----RMSTALSKEVSERIIQMSKGA---PLPAYmilLTGVQSL 77
Cdd:cd19532   177 ALDEDLAYWKSEFSTLPEPLPLLPFAKV-KSRPPLTRydthTAERRLDAALAARIKEASRKLrvtPFHFY---LAALQVL 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928   78 LYKYTSSSSILVGMpvvtkPNENRRP----------VNqLVILREEVRDDSTFKALLGEAKNSVTSSINHQNVPFRLMTE 147
Cdd:cd19532   253 LARLLDVDDICIGI-----ADANRTDedfmetigffLN-LLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFDVLLD 326
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 386647928  148 RLELQ-YADGVPVVNTLValkqlhitDYRQSAVSDVLF 184
Cdd:cd19532   327 ELGVPrSATHSPLFQVFI--------NYRQGVAESRPF 356
PRK07868 PRK07868
acyl-CoA synthetase; Validated
3859-3928 6.61e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 47.02  E-value: 6.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3859 LFEEQALRNPDAVAVVFEKSQLTYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGIMAIMKAG 3928
Cdd:PRK07868  452 IIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLG 521
PRK07868 PRK07868
acyl-CoA synthetase; Validated
264-342 7.37e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 47.02  E-value: 7.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928  264 RLFEEQAERRPDAVAVTFEDRQLTYGELNERANRLARTLRNAGVQADQLVGLMVERSLEMIVGIMGILKAGGAYVPIDP 342
Cdd:PRK07868  451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP 529
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
7020-7308 7.57e-04

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 46.24  E-value: 7.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7020 VQGSLDAEQFARSWNDLVARHAILRTNFFSGPRGEPLqivyrdkrigFVYEDLSHLPAdeRQASVERLEQediARGFDLE 7099
Cdd:PRK09294   30 LRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWE----------LVADDLLHPGI--VVVDGDAARP---LPELQLD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7100 Q-DALVRVAVIRtQETSYRVLWSFHHILMDGWCLPLVVKELFETY-EAYVQGDRPEQKAAPAySQYIEWLENQDSAAASA 7177
Cdd:PRK09294   95 QgVSLLALDVVP-DDGGARVTLYIHHSIADAHHSASLLDELWSRYtDVVTTGDPGPIRPQPA-PQSLEAVLAQRGIRRQA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7178 Y-----WSNYLAGYEGQTALPQEKAQKRSEGYVAEHVVCELDKELSERMNRAAKQCRVTVNTLMQAVwgVILQKYNATD- 7251
Cdd:PRK09294  173 LsgaerFMPAMYAYELPPTPTAAVLAKPGLPQAVPVTRCRLSKAQTSSLAAFGRRHRLTVNALVSAA--ILLAEWQLRRt 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386647928 7252 ---DVVYGSVVSGR-----PAEIPGIEEMIGLF-------INTIPVRVACQPEESFAD--VMGRMQEAALESGR 7308
Cdd:PRK09294  251 phvPLPYVYPVDLRfrltpPVAATEGTNLLGAAtylaeigPDTDIVDLARAIAATLRAdlADGVIQQSFLHFGT 324
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2962-3192 1.07e-03

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 46.58  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 2962 DEAAIRKVLQKLVEHHDALRVVFHKSENGYTAW-NRAIGEGELyglEVVDLKG-IEESAQAVEAKANEIQSSIDLEAG-P 3038
Cdd:PRK10252   43 DAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWvDPALTFPLP---EIIDLRTqPDPHAAAQALMQADLQQDLRVDSGkP 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3039 FVKAGLFQCADGDHLLIV-IHHGVVDGVSWRILLEDLAIGYEQAVKGEELR---FPAKTDAYrtwsEQLAAYAQSPVIER 3114
Cdd:PRK10252  120 LVFHQLIQLGDNRWYWYQrYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPaspFTPFADVV----EEYQRYRASEAWQR 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3115 ELAYWKR-------VAQTEVQPLPKDEQVDvslqqDSESISIEWTREETEQLL---KGVHRAyntemnDILLAALGMAVQ 3184
Cdd:PRK10252  196 DAAFWAEqrrqlppPASLSPAPLPGRSASA-----DILRLKLEFTDGAFRQLAaqaSGVQRP------DLALALVALWLG 264

                  ....*...
gi 386647928 3185 KWSGLDRV 3192
Cdd:PRK10252  265 RLCGRMDY 272
PRK07868 PRK07868
acyl-CoA synthetase; Validated
4892-5005 1.36e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 45.86  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4892 LFEKQAECTPEAAAVVYENDRLTYRELNERANRLARTLRAQGVKPNQLVGILADRSADLLVGALAVWKAGGAYVPLDPDy 4971
Cdd:PRK07868  452 IIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPD- 530
                          90       100       110
                  ....*....|....*....|....*....|....
gi 386647928 4972 pSDRIQFMLEDSAASVLLTQTHLQERAQQWGQTL 5005
Cdd:PRK07868  531 -TDLAAAVRLGGVTEIITDPTNLEAARQLPGRVL 563
acyl_WS_DGAT TIGR02946
acyltransferase, WS/DGAT/MGAT; This bacteria-specific protein family includes a characterized, ...
4457-4682 1.69e-03

acyltransferase, WS/DGAT/MGAT; This bacteria-specific protein family includes a characterized, homodimeric, broad specificity acyltransferase from Acinetobacter sp. strain ADP1, active as wax ester synthase, as acyl coenzyme A:diacylglycerol acyltransferase, and as acyl-CoA:monoacylglycerol acyltransferase. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274360 [Multi-domain]  Cd Length: 446  Bit Score: 45.37  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4457 QLEGAAQSYNMPGVMGLEGALDRERFEETFRKLIARHETLR---TGFELIDGEPVQRIYPEVD--FAVETVQ----ASEQ 4527
Cdd:TIGR02946   10 RLETPTRPMHIGALAVFEGPLSFEALRALLESRLPLAPRFRqrlREVPLGLGHPYWVEDPDFDldYHVRRVAlpapGTRR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4528 EAKAIVRDFI-RPFDLAKPpLLRVGLIE-LAPERCILMLDMHHIVSDGVSAdvlVEEFARLYSGE----ELPGLRI---- 4597
Cdd:TIGR02946   90 ELLELVGRLMsTPLDRSRP-LWEMHLIEgLAGGRFAVLTKVHHALADGVAG---LRLLARLLDDDpdppPLPAPPPppqp 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  4598 QYKDYAVWQQSEAQKEQLKRQeaywLEAFRGelpVLEMptdyARPAVQSYAGD---TLDF-----RMNSEIS-------- 4661
Cdd:TIGR02946  166 STRGLLSGALSGLPSALLRRV----ASTAPG---VVRA----AGRAVEGVARSarpALPFtapptPLNGPISrkrrfaaq 234
                          250       260
                   ....*....|....*....|....*
gi 386647928  4662 ----EGLKRIAAESGATLYMVLLAA 4682
Cdd:TIGR02946  235 slplADVKAVAKAFGVTINDVVLAA 259
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
6306-6392 1.87e-03

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 45.14  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 6306 YRTGDLARWLPD----GT----LEY-KGRIDEQVKIRGYRIELGEIEEQLLKVASVKEATVIVREDESGQKQLCAYFVAE 6376
Cdd:COG1541   297 YRTGDLTRLLPEpcpcGRthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELA 376
                          90
                  ....*....|....*.
gi 386647928 6377 RELTIGELRAALSQEL 6392
Cdd:COG1541   377 PGASLEALAEAIAAAL 392
PRK07868 PRK07868
acyl-CoA synthetase; Validated
2349-2427 1.96e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 45.48  E-value: 1.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 2349 QLFEEQAERIPDHPAVVFEGQQLTYRELNERANRLARTLQALGVKTDQPVGLMLERSLEMVVGMFAVLKAGGAYVPIDP 2427
Cdd:PRK07868  451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP 529
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
3881-4271 1.96e-03

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 45.19  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3881 TYGELNERANRLARTLRDAGVRPDQLVGLMVERSLEMVVGimaiMKAGGAY----IP------------------IDPEY 3938
Cdd:PLN02430   78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA----MEACAAHslicVPlydtlgpgavdyivdhaeIDFVF 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 3939 PED-RIRYMLEDSGAQAlltqrhlrERVSFAGTFVAVDDEQAYHADGSNLEPV-------VG-----------PNHLAYV 3999
Cdd:PLN02430  154 VQDkKIKELLEPDCKSA--------KRLKAIVSFTSVTEEESDKASQIGVKTYswidflhMGkenpsetnppkPLDICTI 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4000 IYTSGTTGKPKGVMVEHHGLCSLKL---MFANTLQ--MTEQDRVVQFASLS--FDascwEIFKALFF--GATL-YIPTST 4069
Cdd:PLN02430  226 MYTSGTSGDPKGVVLTHEAVATFVRgvdLFMEQFEdkMTHDDVYLSFLPLAhiLD----RMIEEYFFrkGASVgYYHGDL 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4070 TILDYPLFEsymnengitatiLPPTYAAylnpdRMPSLKKLITGGSAASVE---------FVQQWKDKVLYFNA-YGPTE 4139
Cdd:PLN02430  302 NALRDDLME------------LKPTLLA-----GVPRVFERIHEGIQKALQelnprrrliFNALYKYKLAWMNRgYSHKK 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4140 ASIVTSI--WDEASDSLGDRKSVPI--GRPLANH-----RI----YVV-----------------DSHNRMLPVGV---- 4185
Cdd:PLN02430  365 ASPMADFlaFRKVKAKLGGRLRLLIsgGAPLSTEieeflRVtscaFVVqgygltetlgpttlgfpDEMCMLGTVGApavy 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 4186 --------------------AGELCISGVGLARGYLNRPELTAEKFVDNPFEpgermyrTGDLVRWLPDGNLEYLGRIDH 4245
Cdd:PLN02430  445 nelrleevpemgydplgeppRGEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEILPNGVLKIIDRKKN 517
                         490       500
                  ....*....|....*....|....*..
gi 386647928 4246 QVKI-RGYRIELGEVETQLAKIDAVQE 4271
Cdd:PLN02430  518 LIKLsQGEYVALEYLENVYGQNPIVED 544
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
1404-1469 2.65e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 45.09  E-value: 2.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 1404 LQERAQQWGQTLqavlCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNT 1469
Cdd:PTZ00342  271 LKEKAKKLGISI----ILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNT 332
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
4994-5059 2.65e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 45.09  E-value: 2.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386647928 4994 LQERAQQWGQTLqaalCLDDEAAYAEDASNVANVNEPHDLAYVIYTSGTTGRPKGVMIEHRSLVNT 5059
Cdd:PTZ00342  271 LKEKAKKLGISI----ILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNT 332
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
1739-1789 2.87e-03

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 40.22  E-value: 2.87e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386647928  1739 KGQkVLCAYFTAESELKLS--ELRSSLSQELPGYMIPSYFVQLEQLPLTANGK 1789
Cdd:pfam13193   25 KGE-APVAFVVLKPGVELLeeELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
prpE PRK10524
propionyl-CoA synthetase; Provisional
3994-4012 2.88e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 44.55  E-value: 2.88e-03
                          10
                  ....*....|....*....
gi 386647928 3994 NHLAYVIYTSGTTGKPKGV 4012
Cdd:PRK10524  233 NEPSYILYTSGTTGKPKGV 251
PRK07868 PRK07868
acyl-CoA synthetase; Validated
7451-7564 3.97e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 44.32  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7451 LFEEQAERMPEKAAVVFENTQLTYRELNERANRLARTLRAEGVQADQPVGLMIERSLEMIVGAFAIMKAGGAYV--PIDP 7528
Cdd:PRK07868  452 IIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVlmPPDT 531
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 386647928 7529 EYPEdriryMLEDSGAQVLLTQ-RHLQECVSFDGKVI 7564
Cdd:PRK07868  532 DLAA-----AVRLGGVTEIITDpTNLEAARQLPGRVL 563
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
5409-5473 4.39e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.93  E-value: 4.39e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928   5409 LVSIWQEVLGL---EKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIAR 5473
Cdd:smart00823   17 VREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
7778-7854 4.42e-03

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 44.34  E-value: 4.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386647928 7778 GELCISGAGLARGYLNRPELTAEKF-VDNpflAGERMYRTGDLARWLPDGNIEYLGRIDHQVKIR-GYRIELGEIEEQL 7854
Cdd:PLN02387  503 GEIVIGGPSVTLGYFKNQEKTDEVYkVDE---RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
592-659 4.90e-03

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 44.04  E-value: 4.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928  592 PIGV--AGELCVAGDGLARGYLNRPDLTAEKFADNPFapgermyRTGDLARWLPDGTIEYVGRIDDQVKI 659
Cdd:PLN02430  459 PLGEppRGEICVRGKCLFSGYYKNPELTEEVMKDGWF-------HTGDIGEILPNGVLKIIDRKKNLIKL 521
PRK03584 PRK03584
acetoacetate--CoA ligase;
272-316 5.14e-03

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 44.02  E-value: 5.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386647928  272 RRPDAVAVTF--ED---RQLTYGELNERANRLARTLRNAGVQA-DQLVGLM 316
Cdd:PRK03584   96 RRDDRPAIIFrgEDgprRELSWAELRRQVAALAAALRALGVGPgDRVAAYL 146
PLN02736 PLN02736
long-chain acyl-CoA synthetase
399-426 5.36e-03

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 43.93  E-value: 5.36e-03
                          10        20
                  ....*....|....*....|....*...
gi 386647928  399 PEHLTYVIYTSGTTGKPKGNLTTHRNII 426
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNLI 247
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1819-1883 5.83e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.54  E-value: 5.83e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386647928   1819 LASIWQEVLGL---EKVGVKDNFFELGGHSLRATLLVGKVHKEMNVELPLRDVFRCSTVEEMAQAIAR 1883
Cdd:smart00823   17 VREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
7468-7631 6.13e-03

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 43.49  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7468 ENTQLTYRELNERANRLARTLRAE-GVQADQPVGLMIERSLEMIVGAFAIMKAGGAYVPIDPEYPEDRIRYMLEDSGAQV 7546
Cdd:cd05905    11 EATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386647928 7547 LLT------------QRHLQECVSFDG----KVIAADDEQAYGEDGSNL---EPVVGPNHLAYVIYTSGTTGKPKGVMVE 7607
Cdd:cd05905    91 ALTveaclkglpkklLKSKTAAEIAKKkgwpKILDFVKIPKSKRSKLKKwgpHPPTRDGDTAYIEYSFSSDGSLSGVAVS 170
                         170       180
                  ....*....|....*....|....
gi 386647928 7608 HHGLCSLKLMFAETLRITEEDRVV 7631
Cdd:cd05905   171 HSSLLAHCRALKEACELYESRPLV 194
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH